Wvsom Fom Test #2 Compilation

Front 1

[OPP Structural Screening]

What does a static structural screening exam provide details for?

Back 1

the presence of a somatic dysfunction

does not identify the dysfunction, just that one is present

Front 2

[OPP Structural Screening]

What are the lateral anatomical aspects of the optimal gravitational line?

Back 2

Anterior aspect of the lateral malleolus
middle of the tibial plateau
greater trochanter
body of L3 (center of the body mass)
middle of the humeral head
external auditory meatus

Front 3

[OPP Structural Screening]

What are the posterior anatomical aspects of the optimal gravitational line?

Back 3

Popliteal creases
greater trochanter
iliac crests
inferior angles of the scapula
acromion processes
mastoid processes

Front 4

[OPP Structural Screening]


Interpret positive hip drop test

Back 4

–ask the standing patient to bend one knee
–this causes the hip on that side to drop toward the floor
–this induces the lumbar spine to bend in the opposite direction to keep the eyes level
–the hip usually drops >=25 degrees
–if less drop = positive test
positive hip drop test = restricted lumbar side–bending on OPPOSITE SIDE

Front 5

[OPP Structural Screening]


Interpret positive hip drop test

Back 5

–stand behind the patient & stabilize the head & shoulder with one arm
–use the other arm to push the shoulder inferiorly & medially
–this induces sidebending in the thoracic spine
–comparing the sides = the side w more resistance indicates restricted thoracic sidebending

Front 6

[OPP Structural Screening]


Discus the treatment of a patient with short leg syndrome (unlevel sacral base)

Back 6

OMT
Exercise
PT
heel–lift on side w depressed sacral base

Front 7

[OPP Structural Screening]

Properly name a scoliotic curve

Back 7

Major double scoliosis
single scoliosis
junctional scholiosis

Front 8

[OPP Structural Screening]

List some risk factors associated with the presence & severity of scoliotic curves

Back 8

Females: 3–5 times more likely
Bone Maturity
Initial curve magnitude
– smaller curves in mature patients = lower risk of progression
– > 45 deg curves in growing patients or >50 deg curves in mature will progress over time

Front 9

[OPP Structural Screening]

What are the causes of scoliosis?

Back 9

Idiopathic! (70–90% nfc)

Front 10

[OPP Structural Screening]

Differentiate between structural & functional scholiosis

Back 10

If patient sidebends towards convexity (toward rib hump)

functional – hump diminishes/disappears
Structural – does not reduce

Front 11

[OPP Structural Screening]

Describe the utilization of the Adam's Test to screen for scholiosis

Back 11

method: patient bends forward = presents a rib hump
Rib hump on right, rotation to right
Rib hump on left, rotation to left

Front 12

[OPP Structural Screening]

Classify scoliosis based on the degree of deviation found by the Cobb method of measuring scoliotic curves

Back 12

mild = 10–15 degrees

moderate = 20–45 degrees

severe > 50 degrees

Front 13

[OPP Structural Screening]

Describe at what scoliotic angle you will encounter impaired respiratory function

Back 13

> 50 degrees deviation

Front 14

[OPP Structural Screening]

Describe at what scoliotic angle you will encounter impaired cardiovascular function

Back 14

> 75 degrees deviations

Front 15

[OPP Structural Screening]

What are the three etiological classifications of scoliosis

Back 15

Congenital
Neuromuscular
Idiopathic

Front 16

[OPP Structural Screening]


Describe the Congenital classification of scoliosis

Back 16

Failure of formation

failure of segmenetation

mixed

Front 17

[OPP Structural Screening]


Describe the Neuromuscular classification of scoliosis

Back 17

Neuropathic

Myopathic

mixed

Front 18

[OPP Structural Screening]


Describe the Idiopathic classification of scoliosis

Back 18

Infantile – birth to 3y

Juvenile – 4–9y

Adolescent – >10y

Front 19

[OPP Structural Screening]


Detail the heel lift protocol

Back 19

flexible pt = 1/8" lift, no more than 1/16" q2wk

fragile pt = 1/16" lift, no more than 1/16" q2wk

injured – full amount immediately

Front 20

[OPP Structural Screening]


Define kyphosis

Back 20

excessive outward curvature of the spine, causing hunching of the back.

Front 21

[OPP Structural Screening]


Define Lordosis

Back 21

a posture assumed by some female mammals during mating, in which the back is arched downward.

Front 22

[intro to epidemiology]

Describe the useful aspects of epidemiology

Back 22

–to study the history of the disease
–community diagnoses
–determine risk for individuals, groups, populations
–assessment, evaluations, research
–Identification of syndromes
–Determine causes of disease, sources of disease, & effective tx for disease

Front 23

[intro to epidemiology]

Define ENDEMIC

Back 23

A disease or pathogen present or usually Prevalent in a given population or geographic region at all times.

Front 24

[intro to epidemiology]

Define EPIDEMIC

Back 24

A disease occurring suddenly in numbers far exceeding those attributable to ENDEMIC disease, occurring suddenly in numbers clearly in excess of normal expectancy.

Front 25

[intro to epidemiology]

Define PANDEMIC

Back 25

A widespread epidemic distributed or occurring widely throughout a region, country, continent or globally.

Front 26

[intro to epidemiology]

Define INCIDENCE

Back 26

The rate of occurrence of an event, the number of NEW cases of disease occurring over a specified period of time; may be expressed per a known population size.

Front 27

[intro to epidemiology]

Define PREVALENCE

Back 27

The number of cases of disease occurring within a population at any one given point in time.

Front 28

[intro to epidemiology]

Define Primary Prevention

Back 28

involves halting any occurrence of a disease or disorder before it happens.
(1) Immunizations
(2) Smoking Cessation
(3) Weight loss
(4) Physical fitness activities
(5) Nutrition
(6) Sun exposure limitation

Front 29

[intro to epidemiology]

Define Secondary Prevention

Back 29

Health Screening and Detection activities.
(1) Breast self exam, Mammography
(2) Prostate exam, PSA
(3) Stool Hemocult, Colonoscopy
(4) Blood Pressure Screening
(5) Periodic blood tests – glucose, lipids, others

Front 30

[intro to epidemiology]

Define Tertiary Prevention

Back 30

preventing complications in those who have developed disease/illness and have been diagnosed.
(1) CVA (stroke rehabilitation)
(2) Cardiac rehabilitation, following MI
(3) Post knee/hip replacement Physical Therapy
(4) Diabetic foot exams

Front 31

[intro to epidemiology]

Describe the types of studies useful to epidemiology

Back 31

Cohort study
Case Control Study
Occupational Epidemiology study
Cross–sectional study
Clinical trial study

Front 32

[intro to epidemiology]

Describe the Clinical trial study...

Back 32

(a) Study pointed at development of new preventive strategies and new treatments for disease.
(b) Also called Randomized Clinical trials.

Front 33

[DS – Intro to Immunology]

Describe the non–specific or innate defense system

Back 33

–is always prepared, responding immediately to protect the body from all foreign substances
–First–line of defense within nonspecific immune system includes the body membranes (skin & mucosae) that prevent entry of MOs
–Second–line of defense within the nonspecific immune system is the chemical signals released when the external defenses are penetrated, using antimicrobial proteins as well as phagocytes & other defense cells to inhibit the spread of foreign bodies

Front 34

[DS – Intro to Immunology]

Describe the specific (or adaptive) defense system

Back 34

performs the attack against foreign substances & provides a 3rd line of defense for the body.
– the adaptive defense system is a functional system that is made of individual immune cells (lymphocytes), which inhabit lymphatic tissues & circulate in the body fluids, & a diverse array of molecules.
–the immune system protects the body from most infectious MOs, cancer cells, & transplanted organs/grafts. The immune system will directly attack foreign bodies & indirectly attack by releasing mobilizing chemicals & protective antibody molecules. Immunity is a high resistance to disease.

Front 35

[DS – Intro to Immunology]

Describe the major features & characteristics of adaptive immune systems

Back 35

– It is antigen specific: recognizes and is directed against particular antigens, against pathogens or foreign substances that stimulate the immune response
– It is systemic: Immunity is not restricted to the initial infection site
– It has memory: After an initial exposure, it recognizes and mounts even stronger attacks on the previously encountered pathogens

Front 36

[DS – Intro to Immunology]

Compare & contrast active immunity & passive immunity

Back 36

– Active Immunity: Naturally acquired active immunity occurs when the person is exposed to a live pathogen, develops the disease, and becomes immune as a result of the primary immune response.
– Artificially acquired active immunity can be induced by a vaccine, a substance that contains the antigen.
Passive Immunity: –Artificially acquired passive immunity is a short–term immunization by the injection of antibodies. Naturally acquired passive immunity occurs during pregnancy, in which certain antibodies are passed from the maternal into the fetal bloodstream.

Front 37

[DS – Intro to Immunology]

Describe the primary immune response

Back 37

– constitutes cellular proliferation and differentiation, occurs on the first exposure to a particular antigen.
i)

Front 38

[DS – Intro to Immunology]

Describe the secondary immune response

Back 38

occurs during a re–exposed to the same antigen; short lag phase, increased immune response

Front 39

[DS – Intro to Immunology]

Describe the major functions of the B–Cells

Back 39

lymphocytes that oversee humoral immunity; B–cells can be distinguished from other lymphocytes, such as T–cells and natural killer cells (NK cells), by the presence of a protein on the B–cell's outer surface known as a B–cell receptor (BCR). This specialized receptor protein allows a B–cell to bind to a specific antigen.

Front 40

[DS – Intro to Immunology]

Describe the major functions of the T–Cells

Back 40

a type of lymphocyte (itself a type of white blood cell) that play a central role in cell–mediated immunity. They can be distinguished from other lymphocytes, such as B cells and natural killer cells (NK cells), by the presence of a T–cell receptor (TCR) on the cell surface. They are called T–cells because they mature in the thymus (although some also mature in the tonsils).[1][2] There are several subsets of T cells: Helper, Cytotoxic, Memory, Regulatory, Natural Killer, and Mucosal Associated Invariant T Cells.

Front 41

[DS – Intro to Immunology]

List the major Antigen–Presenting Cells

Back 41

Dendritic Cells

Macrophages

B–Lymphocytes

Front 42

[DS – Intro to Immunology]

Describe the APC aspect of the dendritic cell

Back 42

process antigen material and present it on the cell surface to the T cells of the immune system.
They act as messengers between the innate and the adaptive immune systems.
Dendritic cells are present in those tissues that are in contact with the external environment, such as the skin
Once activated, they migrate to the lymph nodes where they interact with T cells & B cells to initiate and shape the adaptive immune response.

Front 43

[DS – Intro to Immunology]

Describe the APC aspect of the Macrophage

Back 43

are a type of WBC that engulf & digest cellular debris, foreign substances, microbes, and cancer cells in phagocytosis

Front 44

[DS – Intro to Immunology]

Describe the APC aspect of the B–lymphocyte

Back 44

principal functions of B–cells are to make antibodies against antigens, to perform the role of antigen–presenting cells (APCs), and to develop into memory B–cells after activation by antigen interaction. B–cells also release cytokines (proteins), which are used for signaling immune regulatory functions.

Front 45

[DS – Intro to Immunology]

Explain the role of Naive Lymphocytes

Back 45

– A naive T–cell is considered mature and unlike activated T cells or memory T cells it has not encountered its cognate antigen within the periphery.
– A naive B–cell has not been exposed to an antigen. Once exposed, it either becomes a memory B cell or a plasma cell that secretes antibodies specific to the antigen that was originally bound. Plasma cells do not last long in the circulation, this is in contrast to memory cells that last for very long periods of time. Memory cells do not secrete antibody until activated by their specific antigen.

Front 46

[DS – Intro to Immunology]

Explain the role of Effector Lymphocytes

Back 46

– Effector cells are the relatively short–lived activated cells that defend the body in an immune response.
– Effector B cells are called plasma cells and secrete antibodies
– Activated T cells include cytotoxic T–cells & helper T–cells, which carry out cell–mediated responses.

Front 47

[DS – Intro to Immunology]

Explain the role of Memory Lymphocytes

Back 47

– Memory T cells have become "experienced" by having encountered antigen during a prior infection, cancer, or vaccination. At a second encounter with the invader, memory T–cells can reproduce to mount a faster & stronger immune response than the first time the immune system responded to the invader.
– Memory B cells are a B–cell sub–type that are formed within germinal centers following primary infection and are important in generating an accelerated and more robust antibody–mediated immune response in the case of re–infection

Front 48

[DS – Intro to Immunology]

List the primary immunologic organs & tissues

Back 48

Thymus gland

Bone Marrow

Front 49

[DS – Intro to Immunology]

List the secondary immunologic organs & tissues

Back 49

Spleen
Lymph Nodes
Lymphoid Tissues

Front 50

[DS – Intro to Immunology]

Contrast Cell–Mediated Immunity with Humoral Immunity

Back 50

– Cell–Mediated Immunity does not involve antibodies, but rather involves the activation of phagocytes, antigen–specific cytotoxic T–lymphocytes, and the release of various cytokines in response to an antigen.
– Humoral Immunity: called the antibody–mediated immune system, is the aspect of immunity that is mediated by macromolecules (as opposed to cell–mediated immunity) found in extracellular fluids such as secreted antibodies, complement proteins and certain antimicrobial peptides. Humoral immunity is so named because it involves substances found in the humours, or body fluids.

Front 51

[Intro to Immunology]

Compare & contrast the innate defenses & the adaptive/acquired immune response

Back 51

Innate: body's natural barrier/defenses, non–specific, cells use pattern–recognition receptors to recognize pathogen–associated molecular patterns
Adaptive: antigen–specific, clonal response, Memory, Lymphocytes use antigen–specific receptors that recognize specific epitopes

Front 52

[Intro to Immunology]

What are PRRs?

Back 52

Pattern–recognition Receptors

Front 53

[Intro to Immunology]

What are PAMPs?

Back 53

Pathogen–associated Molecular Patterns

Front 54

[Intro to Immunology]

What are the Mechanical, Chemical, and Microbiological mechanisms of defense in the

SKIN

Back 54

– Epithelial cells joined by tight junctions
– Flow of fluid, perspiration, sloughing off of skin
– Sebum (fatty acids, lactic acid, lysozyme)
– Antimicrobial peptides (defensins)
– Normal flora

Front 55

[Intro to Immunology]

What are the Mechanical, Chemical, and Microbiological mechanisms of defense in the

GI tract

Back 55

– Epithelial cells joined by tight junctions
– Flow of fluid, mucus, food, saliva
– acidity, enzymes (proteases)
– Antimicrobial peptides (defensins)
– Normal flora
–vomit, diarrhea

Front 56

[Intro to Immunology]

What are the Mechanical, Chemical, and Microbiological mechanisms of defense in the

Respiratory Tract

Back 56

– Epithelial cells joined by tight junctions
– Flow of fluid, mucus, (cilia, air flow)
– lysozyme in nasal secretions
– Antimicrobial peptides (defensins)
– Normal flora
– cough, sneeze

Front 57

[Intro to Immunology]

What are the Mechanical, Chemical, and Microbiological mechanisms of defense in the

Urogenital Tract

Back 57

– Epithelial cells joined by tight junctions
– Flow of fluid, urine, mucus, sperm
– Acidity in vaginal secretions, spermine & zinc in semen
– Antimicrobial peptides (defensins)
– Normal flora

Front 58

[Intro to Immunology]

What are the Mechanical, Chemical, and Microbiological mechanisms of defense in the

Eyes

Back 58

– Epithelial cells joined by tight junctions
– Flow of fluid, tears
– lysozyme in tears
– Antimicrobial peptides (defensins)
– Normal flora

Front 59

[Intro to Immunology]

Compare & contrast the innate immunity & adaptive immunity

[think: summary table of differences]

Back 59

Innate: recognition, rapid response (hours), fixed spectrum, limited # of specificities, constant during response

Adaptive: recognition, slow response (days to wks), variable spectrum, numerous highly selective specificities, improves during response

Front 60

[Intro to Immunology]

List the basic principles of the clonal selection mechanism of lymphocyte activations

Back 60

1. Lymphocytes clone with diverse receptors arise in generative lymphoid organs
2. Clones of mature lymphocytes specific for many antigens enter lymphoid tissues
3. antigen–specific clones are activated/selected by antigens
4. antigen specific immune responses occur

Front 61

[Intro to Immunology]

Given, clonal selection, why do we still have infections?

Back 61

– The initial attack that bypasses the primary defense will trigger the adaptive the second defenses.
– These need to initially learn to identify the foreign substance which take time (1–3 wks).
– Subsequent invasions will trigger a 2–3 day response instead due to memory cells

Front 62

[Intro to Immunology]

Define immunologic memory

Back 62

long–lived lymphocyte clones that derive from contact with the antigen
virus inhaled/inoculated > innate/barrier defenses > virus attaches to cell > innate cellular defenses > "foreign" antigen presented to immune system > activation of naive lymphocyte > expansion & differentiation of lymphocytes > lymphocyte effector function > Memory

Front 63

[Intro to Immunology]

Define specificities

Back 63

ensures that distinct antigens elicit responses that target those antigens

Front 64

[Intro to Immunology]

Define Diversity

Back 64

enables immune systems to respond to a large variety of antigens

Front 65

[Intro to Immunology]

Define Memory

Back 65

leads to rapid & enhanced responses to repeated exposures to the same antigens

Front 66

[Intro to Immunology]

Define Clonal Expansion

Back 66

increases the # of antigen–specific lymphocytes to keep pace with microbes

Front 67

[Intro to Immunology]

Define Specialization

Back 67

generates responses that are optimal for defense against different types of microbes

Front 68

[Intro to Immunology]

Define Contraction & Homeostasis

Back 68

allows immune systems to respond to newly encountered antigens

Front 69

[Intro to Immunology]

Define Non–reactivity to self

Back 69

prevents injury to the host during response to foreign antigens

Front 70

[Intro to Immunology]

Describe the difference between (graph) the primary & secondary immunologic response (think vaccination)

Back 70

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Front 71

[Intro to Immunology]

Describe the purpose of a vaccine

[think memory cells]

Back 71

vaccination is the induction of a primary response to an organism in order to allow the creation of Memory B cells, so that when you encounter the actual disease, it induces the faster, secondary response.

Front 72

[Intro to Immunology]

Compare & contrast antigen & antigenic determinant (epitope)

Back 72

– an antigen is an agent of infection/disease

– the epitope is the piece of the antigen that the lymphocytes' receptors recognize

Front 73

[Components of the Immune System]

What are the primary immune organs

Back 73

where immune cells arise & mature

Thymus

Bone Marrow

Front 74

[Components of the Immune System]

What are the secondary immune organs

Back 74

Where immune cells get together to initiate adaptive immunity / released in an immune response

Lymph nodes, spleen, Waldeyer's Ring, lymphoid tissue, Peyer's Patch, MALT, Appendix

Front 75

[Components of the Immune System]

Describe the thymus' involvement with T–Cells

Back 75

Cortex – residence of immature T–cells

Medulla – residence of mature T–cells with forming/displayed receptors. ~5% survive & are released

Front 76

[Components of the Immune System]

Describe the Bone marrow's involvement with lymphocytes

Back 76

Formation of lymphocytes from stem cells

B–cells > create & mature in bone marrow into granulocytes & monocytes

T–cells > created & relocated to the thymus (thymocytes)

Front 77

[Components of the Immune System]

What are the two parts to the Waldeyer's Ring?

Back 77

Tonsils & adenoids

Front 78

[Components of the Immune System]

Describe the shape & function of the lymph nodes

Back 78

– bean–shaped, encapsulated, vascularized, secondary lymphoid organs clustered in groups around lymphatic channels.
– B–cells located mostly in the primary lymphoid follicles
– T–cells located mostly in the paracortical area

Front 79

[Components of the Immune System]

Describe the Spleen in regards to the lymph system

Back 79

–secondary lymphoid organ

–white–pulp surround arteries & in follicles; blood is filtered & antigens are presented to the lymphocytes (mostly B–cells)

Front 80

[Components of the Immune System]

Describe the MALT

Back 80

Mucosal–Associated Lymphoid Tissue (MALT)
– lymphoid cells & follicles in mucus membranes
– Respiratory, GI, urogenital

Front 81

[Components of the Immune System]

Compare & contrast primary & secondary lymphoid Follicles

Back 81

– A lymph follicle is a dense collection of lymphocytes, the number, size and configuration of which change in accordance with the functional state of the lymph node.
– primary – spherical aggregates of B–lymphocytes, both virgin & memory B–cells in the process of entering or leaving the node
– secondary – spherical aggregates of B–lymphocytes, both virgin & memory B–cells in the process of entering/leaving the node, Form only in response to an antigenic challenge. Germinal Centers – pale staining center where memory B cells & plasma cells are formed

Front 82

[Components of the Immune System]

List the four classes of cells of the immune system

Back 82

Lymphocytes
Antigen–presenting cells
Inflammatory Cells
Bridge Innate & Adaptive

Front 83

[Components of the Immune System]

Describe the general function of the lymphocytes

[under 4 classes of cells associated with the immune system]

Back 83

T–lymphocytes – regulators, helpers (for a proper B–cell antibody response, killers
B–lymphocytes – differentiate after encountering antigens into either a plasma cell or a memory cell

Front 84

[Components of the Immune System]

Describe MHCs

Back 84

Major Histocompatibility Complex – display peptides for T–cell activation, are responsible for self / non–self distinctions

Front 85

[Components of the Immune System]

Describe CD molecules

Back 85

a nomenclature system for cell surface molecules

CD4
CD8
CD21

Front 86

[Components of the Immune System]

What is the primary function of CD4, CD8, & CD21

Back 86

CD4 – Helper T–cell – Adhesion
CD8 – Killer T–Cell – Activation
CD21 – B–Cell – Activation

Front 87

[Components of the Immune System]

What are the antigen–presenting cells & why are they needed

[under 4 classes of cells associated with the immune system]

Back 87

Dendritic Cells, Macrophages, B–Lymphocytes

T–cells need antigens presented on surface of another cell

Front 88

[Components of the Immune System]

What are the types of Inflammatory Cells & their purpose

[under 4 classes of cells associated with the immune system]

Back 88

Neutrophils – 40–60% of blood leukocytes –> phagocytize
Eosinophils – 1–3%, combat parasitic worms
Basophils – 0–1%, mediate allergic rxs
Mast Cells – ––– mediate allergic reactions
others: epithelial, endothelial, platelets, lymphocytes, monocytes

Front 89

[Components of the Immune System]

What are the cell types that bridge the innate & adaptive systems

[under 4 classes of cells associated with the immune system]

Back 89

NK – Natural killer cell – kills tumors & virus infected cells
NKT – natural killer T–cell – recognize glycolipids
gama–delta T–cells – recognize a range of molecular patterns

Front 90

[Components of the Immune System]

Describe the general role of the MHC/HLA genes & proteins in the immune system

Back 90

displays peptides for the T–cell activation & are responsible for self / non–self distinctions

HLA = Human version of MHC

Front 91

[Components of the Immune System]

Describe the term complement with regards to an immune response

Back 91

a system of plasma proteins & surface molecules that facilitate inflammation & can destroy pathogens

Front 92

[Components of the Immune System]

Describe cytokines with regards to an immune response

Back 92

Intracellular communication molecules

Front 93

[Components of the Immune System]

Describe Immunoglobulin with regards to an immune response

Back 93

Immunoglobulins = antibody – antigen specific receptors on B–cell surface or secreted
–antigen binding, neutralization of microbial toxins, inhibiting attachment of microbes, opsonization, activate the protein–complement systems, protection of developing fetus

Front 94

[Components of the Immune System]

Define opsonization

Back 94

facilitating phagocytosis = bind to surface of MOs, help phagocytic cell to phagocytize

Front 95

[Fates of a Cell]

1. Define Pathology & its significance in medicine

Back 95

Understanding the changes in cells helps us to recognize the disease process, to explain why patients present with certain symptoms to accurately diagnose normal & abnormal conditions in patients, & to adequately care for patients on a daily basis

Front 96

[Fates of a Cell]

2. Describe cellular adaptations & their relations to disease processes

Back 96

cellular adaptations adjust to new conditions/demands for optimal functioning, reversible

affect size/number/phenotype/metabolic activity and/or functions of cells

Front 97

[Fates of a Cell]

2. Define Hypertrophy

Back 97

increase in the size of the cells

cause an increase in organ size

Front 98

[Fates of a Cell]

2. Define Hyperplasia

Back 98

Increased # of cells in tissue & organs

cause an increase in organ size

uncontrolled hyperplasia ~ cancer

Front 99

[Fates of a Cell]

2. Define Atrophy

Back 99

decrease in cell size = decreased organ size

Front 100

[Fates of a Cell]

2. Define Ischemic Atrophy

Back 100

loss of oxygenated blood supply

always accompanies Hypoxia

Front 101

[Fates of a Cell]

2. Define Hypoxia

Back 101

lack of oxygen

Front 102

[Fates of a Cell]

2. Define Nutritional Atrophy

Back 102

– less available nutrients than metabolically necessary = cell shrinkage/death

causes inflammation disease & cancer because of cytokine TNF (tumor necrosis factor)

Front 103

[Fates of a Cell]

2. Define Metaplasia

Back 103

one differentiated cell type is replaced by another

Squamous > columnar
Columnar > squamous

Front 104

[Fates of a Cell]

2. Define Dysplasia

Back 104

disordered growth
sometimes in metaplastic epithelium

Front 105

[Fates of a Cell]

2. Carcinoma in Situ means?

Back 105

dysplasia but the basement membrane is intact = non–malignant

Front 106

[Fates of a Cell]

3.What are the 5 types of cellular adaptions

(list)

Back 106

Hypertrophy
Hyperplasia
Atrophy
Metaplasia
Dysplasia

Front 107

[Fates of a Cell]

3.What are the typical causes of cellular injury?

Back 107

Oxygen deprivation
Physical Agents
Chemical Agents & drugs
Infectious Agents
Immunologic reactions
Genetic derangements
Nutritional Imbalances

Front 108

[Fates of a Cell]

3.Cell Injury: describe oxygen deprivation

Back 108

–ischemia
–cardiopulmonary failure
–Anemia / Carbon Monoxide / cyanide poisoning
–Severe blood loss

Front 109

[Fates of a Cell]

3.Cell Injury: Describe Chemical Agents & drugs

Back 109

–electrolyte imbalance
–oxygen toxicity
–toxins, industrial chemicals
–alcohol, recreational drugs, therapeutic drugs

Front 110

[Fates of a Cell]

4. Describe cell death & the consequences

Back 110

Necrosis is denaturing of intracellular proteins, enzymatic digestion of lethally injured cells, no membrane integrity
– contents leak out, inflammation results

Apoptosis = programmed cell death, plasma membrane remains intact

Front 111

[Fates of a Cell]

What are the goals of cellular adaptation that reflect the dynamic ability of the cell to alter.

Back 111

Gene transcription & translation (g1,g2)
Synthesis of new DNA/chromosomes (S)
Proliferation (M)

Front 112

[Fates of a Cell]

What are the types of cells that undergo hypertrophy?

Back 112

* usually in non–dividing cells, no new cells, only increase in the size & # of intracellular components

Cardiac muscle, Skeletal Muscle, Pregnant Uterus

Front 113

[Fates of a Cell]

Fluff: What are the two biochemical pathways by which a cell will undergo hypertrophy

Back 113

physiological = Phosphoinositide 3–kinase / Akt

pathological = signaling downstream of GPCRs

Front 114

[Fates of a Cell]


What are the two stimuli causing cellular hypertophy

Back 114

increased workload = muscles
increased hormonal stimulation = pregnancy

Front 115

[Fates of a Cell]

What are the two mechanism/stimuli for hyperplasia?

Back 115

increased growth factors

increased production of cells from tissue stem cells

Front 116

[Fates of a Cell]

What are the types of pathologic hyperplasia?

Back 116

– hormonal = increase the functional capacity (pregnancy)
– compensatory = increase tissue/organ mass after partial resection/damage (liver)

Front 117

[Fates of a Cell]

What are the types of pathological
hyperplasia?

Back 117

– excessive hormones & growth factors
endometrial hyperplasia & BPH
– viral infections = HPV

Front 118

[Fates of a Cell]

What are the two types of hyperplasia

Back 118

Controlled – no gene mutations, regression of hyperplasia if stimulation is removed

Uncontrolled – genetic aberrations occur, unrestrained proliferation, can become malignant

Front 119

[Fates of a Cell]

Give examples of physiologic atrophy

Back 119

embryonic structures – notochord

postpartum uterus

Front 120

[Fates of a Cell]

Give examples of pathologic atrophy

Back 120

Atrophy of disuse (use it or lose it)
Denervation atrophy (spinal cord injury)
Ischemic atrophy ( loss of blood)
nutritional atrophy (protein–calorie malnut.)
Endocrine atrophy (menopause)
Pressure atrophy (tourniquet)

Front 121

[Fates of a Cell]

Define Marasmus & Cachexia

Back 121

marasmus – profound protein–calorie malnutrition

Cachexia – marked muscle wasting

Front 122

[Fates of a Cell]

Which atrophy is due to an overproduction of cytokine TNF

Back 122

nutritional atrophy – cachexia

Front 123

[Fates of a Cell]

Define cytokine TNF

Back 123

TNF = tumor necrosis factor

Front 124

[Fates of a Cell]

What are the mechanisms of atrophy

Back 124

–Decreased protein synthesis
–increased protein degradation
–increased autophagy

Front 125

[Fates of a Cell]

Describe autophagy

Back 125

starved cells eat their own components

–autophagic vacuoles or residual bodies

Front 126

[Fates of a Cell]

What is known as brown atrophy?

Back 126

Lipofuscin granules

Front 127

[Fates of a Cell]

Metaplasia: What is the cell type change in the respiratory tract due to smoking?

Back 127

Columnar change to Squamous cells to resist physical damage from smoking

Front 128

[Fates of a Cell]

Metaplasia: What is the cell type change in the esophagus due to GERD

Back 128

squamous epithelial cells change to columnar in the esophagus to resist chemical damage

Front 129

[Fates of a Cell]

What is barrets esophagus?

Back 129

the change in the esophagus from squamous cell to columnar to resist chemical damage

Front 130

What are the two components of the extracellular buffer system

Back 130

bicarbonate buffer system & proteins

Front 131

What are the two components of the Intracellular buffer system

Back 131

phosphate buffer system & proteins

Front 132

Define Hydrophilic

Back 132

water loving

Front 133

Define Hydrophobic

Back 133

water–fearing

Front 134

Define Amphipathic

Back 134

molecules having both phobic and philic portions (cell membranes)

Front 135

Predict the movement of water across membranes with a Hypotonic extracellular fluid

Back 135

Higher water to solute ratio than the cell, floods the cell. The Cell will expand and eventually rupture

Front 136

Predict the movement of water across membranes with a Hypertonic extracellular fluid

Back 136

lower water to solute ratio than cell, transfer H2O from cell into solution causing shrinkage

Front 137

Predict the movement of water across membranes with a Isotonic extracellular fluid

Back 137

same water to solute ratio as cell, no net change = neutral situation

Front 138

Describe Henderson–Hasselbalch equation for acids

Back 138

pH – pKA = log of [ionized & unprotonated acids] / [protonated & unionized acids]

Front 139

Describe the Henderson–Hasselbalch situation where a acid’s pKa is higher than the pH

Back 139

the equilibrium will force more of the substance towards the fully protonated, unionized right side of the equation. A–+H+ > AH

Front 140

Describe the Henderson–Hasselbalch situation where a acid’s pKa is lower than the pH

Back 140

the equilibrium will force more of the substance towards the unprotonated, ionized left side of the equation. A–+H+ > AH

Front 141

Describe with the Henderson–Hasselbalch: the differences in ionization/protonation between acids and bases

Back 141

pH – pKA = log of [unionized base] / [protonated & ionized acids]

Front 142

Name the steps in protein expression [general]

Back 142

DNA located in the nucleus are transcribed into mRNA which are transported to the Endoplasmic Reticulum where they are translated into polypeptides

Front 143

Describe the important pieces of the Amino Acid Structure [general]

Back 143

Amino Acid – H3N+
Carboxyl Group – COO–
alpha–Carbon – center carbon attached to the Carboxyl group
Functional Group – R–group

Front 144

Explain how the properties of amino acids determine protein structure/function

Back 144

Folding provides the overall shape which determines the affinity/fitting of the receptor sites

Front 145

Describe the characteristics of polar proteins

Back 145

typically hydrophilic, water–soluble, and require active transport across membranes

Front 146

Describe the characteristics of non–polar proteins

Back 146

typically hydrophobic, lipid–soluble, and utilize passive diffusion across membranes

Front 147

Describe the characteristics of the Primary protein structure

Back 147

Sequence of the Amino Acid chain

Front 148

Describe the characteristics of the Secondary protein structure

Back 148

relationship of H–Bonding between the R–groups that cause alpha–helices and beta–sheets

Front 149

Describe the importance of the cysteine amino acid

Back 149

the cysteine amino acid contains an SH on the R–group that creates Disulfide (covalent) bonds with other cysteine molecules that are very strong.

Front 150

Describe the characteristics of the Tertiary protein structure

Back 150

overall/3–D structure of a single protein

Front 151

Describe the bonding associated with the Tertiary protein structure

Back 151

h–bonding, ionic bonding, disulfide bonds, Hydrophobic reactions

Front 152

Describe the bonding associated with the Quaternary protein structure

Back 152

h–bonding, ionic bonding, disulfide bonds, Hydrophobic reactions

Front 153

Describe the characteristics of the Quaternary protein structure

Back 153

combination of multiple protein monomers together

Front 154

Define protein: Homodimer

Back 154

2+ polypeptide chains, identical order, number, & kind of A.A. Residues

Front 155

Define protein: Heterodimer

Back 155

2+ polypeptide chains, differ in order, number, & kind of A.A. Residues

Front 156

Define term: Isoform with regards to HbF & HbA

Back 156

different structures, same function, slight alteration of specificity, activity, binding efficiency. Fetal Hemoglobin has 2–alpha globins + 2 gamma–globins while the Adult hemoglobin has 2–alpha globins + 2–beta–globins

Front 157

Define polymorphic

Back 157

Genetic Diversity, slight variations in a population

Front 158

Describe various ways [general] that a protein structure can be disrupted

Back 158

alterations in folding
temperature, pH, ionic detergents, heavy metal ions, organic solvents such as alcohol
molecules that alter bonding
post–translational modifications [specific] – phosphorylation and glycosylation
Glycation [non–specific]
Proteases

Front 159

Define the function of proteases

Back 159

break the amino acid backbone, a part of the protein half–life regulatory system

Front 160

Describe the Proteasome

Back 160

protein chopping factor in the cell, maintains cellular homeostasis through removing unwanted or dangerous proteins

Front 161

Describe Ubiquitination

Back 161

enzymatic addition of lysine residue to proteins that are targeted for proteolysis by the proteasome

Front 162

Describe the equilibrium dissociation constant Kd

Back 162

Kd is a measurement of the binding Strength/Affinity between a protein and a ligand

Front 163

Describe the result of a low Kd value

Back 163

lower Kd values reflect a high affinity or a more tightly bond between the ligand and the protein

Front 164

Describe the result of a high Kd value

Back 164

Higher Kd values reflect a low affinity or a loose bond between the ligand and the protein

Front 165

Define the term Saturable in regards to Protein–Ligand Data

Back 165

Saturable refers to the percent of the substrate that is bound to a ligand. When 100% of the substrate is bound, any excess ligand is extraneous and ineffective

Front 166

Describe Allosteric behavior

Back 166

change in protein activity by binding of effector|Enzyme NOT at the active site

Front 167

Describe Cooperativity

Back 167

assists in reaction rates based on changes within the molecule. Binding of first O2 on Hgb increases likelihood of #2 binding etc. [unloading also cooperative]

Front 168

What are the two CoEnzymes involved in Redox Reactions

Back 168

FADH – flavin adenine dinucleotide
NADH2 – nicotinamide adenine dinucleotide

Front 169

Define the mnemonic OIL RIG

Back 169

Oxidizing is Losing e–, Reducing is Gaining e–

Front 170

Define Reducing Agent

Back 170

The reducing agent is the molecule that is donating/losing the electron. The reducing agent is ultimately oxidized (lost electron)

Front 171

Define Oxidizing Agent

Back 171

The oxidizing agent is the molecule that is accepting/gaining the electron. The oxidizing agent is ultimately reduced (gained electron)

Front 172

What vitamin is NAD derived from

Back 172

niacin

Front 173

What vitamin is FAD derived from

Back 173

riboflavin

Front 174

What vitamin is TPP derived from

Back 174

Thiamine (B1)

Front 175

What vitamin is CoA derived from

Back 175

Pantothenate (B5)

Front 176

What vitamin is Tetrahydrofolate derived from

Back 176

Folic Acid

Front 177

What vitamin is Pyridoxal phosphate derived from

Back 177

Pyridoxine (B6)

Front 178

Define Michaelis–Menton’s Km

Back 178

kM is the substrate concentration that is required for the reaction to occur at ½ of the maximum (Vmax) reaction rate

Front 179

Define Michaelis–Menton’s Vmax

Back 179

Vmax is the maximum reaction rate

Front 180

What does a low Michaelis–Menton Km mean

Back 180

lower Km values show a higher affinity for the substrate, requires less [s] to achieve Vmax

Front 181

Describe the graph of a Lineweaver–Burk plot with regards to the changes in the graph caused by a competitive inhibitor

Back 181

The Km of the graph changes which changes the slope of the line and the point where it intercepts the X–Axis while the Y–Intercept stays the same

Front 182

Describe the graph of a Lineweaver–Burk plot with regards to the changes in the graph caused by a noncompetitive inhibitor

Back 182

The Vmax of the graph changes which Y–intercept point but the slope of the line and the X–intercept remain relatively unchanged.

Front 183

With regards to the Lineweaver–Burk plot, what does a larger or smaller X–Intercept value mean

Back 183

a larger X–intercept means a higher Km and a lower affinity for the substrate while a lower X–intercept means a lower Km and a stronger affinity for the substrate

Front 184

Which of the inhibitors can be overcome by increasing the concentration of substrate

Back 184

The competitive inhibitors

Front 185

Define Allosteric inhibitors

Back 185

binds at somewhere other than the active site to alter function

Front 186

Define Reversible inhibitors

Back 186

bind non–covalently to the enzyme, do not change it, and are able to be separated

Front 187

Define Irreversible inhibitors

Back 187

bind covalently to the enzyme, change it chemically, permanently

Front 188

Explain the difference between a receptor agonist and a receptor antagonist

Back 188

A receptor agonist binds & fully activates the receptor while the receptor antagonist binds but does not activate the receptor

Front 189

Describe the methods by which enzyme activity are regulated

Back 189

non–specific inhibition of enzymes such as overall temperature and pH, any proteolytic behavior
Specific inhibition of enzymes such as intentional substrates, products, drugs etc.
Phosphorylation and dephosphorylation
post–translational modifications such as the addition of objects to the protein structure or specific folding sequences
protein–protein interactions
expression level – what is needed at that point in the cellular life and function
proteolysis – ubiquitination of unneeded or harmful proteins

Front 190

define accuracy

Back 190

closeness to the known standard

Front 191

Define Precision

Back 191

reproducibility

Front 192

Define Sensitivity

Back 192

the smallest amount of detectable analyte

Front 193

Define Specificity | Selectivity

Back 193

ability of a method to measure one analyte vs another. How well a ligand will bind to Substrate A vs Substrate B

Front 194

Describe the general method and clinical uses for electrophoresis

Back 194

electrophoresis is the process of separating proteins based on size and molecular weight. Clinical Significance is the ability to detect amounts of expressed proteins.

Front 195

Describe the clinical uses for Enzyme Assays

Back 195

The examination of expressed enzymes and proteins such as the glucose oxidase test that measures the light–scattering effect of light shone through a sample of a sample

Front 196

Describe the clinical uses for Mass Spectrometry

Back 196

able to tell the amount and sequence of proteins

Front 197

Describe the clinical uses for Immunoassays

Back 197

utilizes detection antibodies labelled with radioactive, fluorescent, or colorimetric parts that allow the examination of expressed mRNA and proteins. This is useful with cancer patients. A subset of this is the ELISA test.

Front 198

Describe the general method and clinical uses for DNA sequencing

Back 198

allows for the sequencing by synthesis of DNA by tagging the bases in various methods, able to explore a patient’s genome

Front 199

Describe the general method and clinical uses for DNA fingerprinting

Back 199

DNA fingerprinting allows for the examination by fragment length, variations in the genome due to RFLP, STR, and VNTR alterations.

Front 200

Define RFLP with regards to genetic structure

Back 200

Restriction fragment length polymorphism, enzymatic digestion of the genome at known points resulting in varying fragment lengths due to polymorphisms or small sequential differences in the populous

Front 201

Define STR with regards to the genetic structure

Back 201

Short Tandem Repeats, alterations in the genetic code 2–7 base pairs long

Front 202

Define VNTR with regards to the genetic structure

Back 202

Variable Number Tandem Repeats – alterations in the genetic code > 8 base pairs long

Front 203

Define SNP with regards to the genetic structure

Back 203

Single Nucleotide Polymorphisms – alterations in the genetic code only 1 base pair long

Front 204

Describe the PCR

Back 204

PCR is polymerase chain reaction and is the process of generating large amounts of DNA from a small initial sample. This allows specific regions of DNA to be examined and tested

Front 205

Explain the difference between Northern, Southern, and Western Blotting

Back 205

Northern – studies RNA, the North is Really Cold
Southern – studies DNA, the Dukes of Hazard were in the South
Western – studies proteins, the Pacific ocean is on the West Coast

Front 206

What information can Proteomic studies provide

Back 206

proteomics refer to the investigation of all the proteins expressed by the cell. This is not examining the genome itself but rather the proteins expressed by it which are susceptible to many alteration

Front 207

What information can DNA microarray studies provide

Back 207

DNA Microarray or DNA Chip detects specific genetic mutations and determines which mRNAs are being expressed in the patient

Front 208

Define Physical Diagnosis

Back 208

determine nature of disease by physical measures that include inspection, palpation, percussion and auscultation

Front 209

History provides what percent of the diagnosis?

Back 209

90%

Front 210

What are the 4 intellectual processes involved in arriving at a diagnosis?

Back 210

Pattern Recognition
Sampling the Universe
Algorithms
Hypothesis

Front 211

Define using pattern recognition to arrive at a diagnosis:

Back 211

If it look likes a Duck, quacks like a duck.....

Front 212

Define using Sampling of the Universe to arrive at a diagnosis:

Back 212

Sampling the Universe involves an exhaustive method of performing copious tests in order to slowly limit the probability of the disease process. Useful in situations where limited information is available (ER/Trauma)

Front 213

Define using Algorithms to arrive at a diagnosis:

Back 213

Algorithms provide a distinct, tried, tested pathway of following s/sx to a diagnosis and subsequent treatment plan

Front 214

Define using hypotheses to arrive at a diagnosis:

Back 214

Gather information
Assessment of the information
Form hypothesis most likely to fit assessment
Assess the probability and utility of various ways to test the hypothesis

Front 215

Define Baye's Theorem

Back 215

use sensitivity and specificity of disease in the patient's population to determine if a certain course of action should be taken. Probability and utility enter the process to allow the physician to decide how probable a patient is to have a disease and the utility determines whether certain procedures have worth to the patient.

Front 216

Define Rapport

Back 216

Seriously.... treat your patient like he was your Mom, or... rather, how you should have treated your Mom.

Professional appearance, attitude, caring, confidentiality, communication, and preservation of dignity.

Front 217

Describe the aspects of history taking

Back 217

history taking includes the Chief Complaint, HPI, PMH, Social History, the Review of Systems

Front 218

Define HPI and the associated mnemonic

Back 218

OLD CARTS: Onset, Location, Duration, Character, Associated & Aggravating factors, Relieving Factors, Temporal factors, Severity of Symptoms

Front 219

Define PMH & the associated mnemonic

Back 219

MIIFMASH: Medical Illness, Injuries, Immunization, Family History, Medications, Allergies, Surgeries, Hospitalization

Front 220

Describe when you would include first and second degree relatives in family history

Back 220

Always include first degree relatives but only include second degree relatives when situationally appropriate

Front 221

Detail the mnemonic used for history taking–

Back 221

history taking includes the Chief Complaint, HPI, PMH, Social History, the Review of Systems

Front 222

Explain when to do a complete history

Back 222

On every new patient

Front 223

Explain when a focused history is appropriate

Back 223

on returning patients or emergent/trauma patients

Front 224

What are the cardinal principles of the physical exam

Back 224

Inspection
Auscultation
Percussion
Palpation

Front 225

Physical Exam: provide details regarding

Inspection

Back 225

yields the most # of diagnoses, generalized, localized

Front 226

Physical Exam: provide details regarding

Auscultation

Back 226

is performed from the moment you walk in the door

ex: patients breathing pattern with and without the stethoscope

Front 227

Physical Exam: provide details regarding

Percussion

Back 227

helps to locate organs and map out sizes, tests for density in tissue & air/fluid filled cavities

Front 228

What three aspects are important re: Percussion

Back 228

Tympany
Resonance
Flatness

Front 229

Define Tympany

Back 229

air filled stomach

Front 230

Define Resonance

Back 230

air filled lungs

Front 231

Define Flatness

Back 231

solid muscle e.g. thigh

Front 232

Physical Exam: provide details regarding

Palpation

Back 232

Tenderness
Texture
Temperature
Tone
Masses
Consistency
Location
Mobility
Pulsation

Front 233

What is the most important part of palpation during the physical exam?

Back 233

Keep the patient at ease

Front 234

Define Ballottement

Back 234

solid structure suspended in fluid e.g. patella

Front 235

What is important regarding the sequencing of the various parts of the physical exam?

Back 235

the sequence should be divided by system but adjusted to minimize the amount of changing positions the patient will have to do.

Front 236

Describe parts of the physical exam to be performed while the patient is in the seated position

Back 236

general appearance
vital signs
extremities
parts of the neurological & musculoskeletal systems

Front 237

Describe subjective vs. objective information

Back 237

Subjective – information given to you, what the patient tells you.

Objective – measurable information such as vital signs & head to toe exam

Front 238

Describe the difference between Autocrine, Paracrine, and Endocrine action

Back 238

Autocrine – target sites are on the same cell that produces the messenger

Paracrine – Secreted into interstitial fluid targeting adjacent cells

Endocrine – Secreted into the blood

Front 239

Describe the general characteristics of signal transduction systems

Back 239

signal/ligand released due to stimulus
ligand travels to site of action
Recognition & Binding of ligand by receptors
Binding results in a change in the receptor that creates a response in the cell

Signal is terminated

Front 240

Regarding signal transduction, describe small messenger molecules

Back 240

steroids – cortisol, estrogen, testosterone

lipid–soluble, able to diffuse across membranes

Front 241

Regarding signal transduction, describe peptide messenger molecules

Back 241

proteins
cytokines
growth factors
Hormones

require active/facilitated transport

Front 242

List the main types of plasma membrane receptors

Back 242

Ligand–gated ion channels
Receptor kinases
Receptors that act through accessory kinases
G–protein coupled receptors

Front 243

Describe intracellular receptors

Back 243

act primarily as transcription factors which regulate gene expression in the response signals being released

Front 244

Describe Protein Kinases

Back 244

Protein Kinases transfer a phosphate group from ATP to the –OH group of a specific Amino Acid side chain on a protein

Front 245

Describe Protein Phosphatases

Back 245

Protein Phosphatases catalyze the dephosphorylation & modulate the phosphorylation cascade process

Front 246

Describe Co–Repressors / Co–Activators

Back 246

modulate signaling through intracellular receptors that are transcription factors

Front 247

Explain the general mechanisms through which signal termination & desensitization occur

Back 247

Uncoupling – GPCRs uncoupling from G–proteins after the ligand binds
Endocytosis – internalization and degradation of protein receptors
Modifications by other proteins decreasing signal activity
Altered expression of the proteins

Front 248

Describe the process by which a Tyrosine Kinase Receptor connects to an adaptor protein in general terms:

Back 248

Ligand binding
Dimerization
Autophosphorylation
Connection to Adaptor protein on activated receptor site

Front 249

Describe the process by which Tyrosine Kinase Receptors activate the Ras pathway

Back 249

Ligand binding
Dimerization
Autophosphorylation
binding of Adapter protein
binding of GEF protein
attachment & activation of Ras to Ras–GTP
Ras–GTP activates Raf
Raf continues on into the MAP–K pathway

Front 250

What type of receptor initiates the MAP–K pathway through Ras

Back 250

Tyrosine–Kinase Receptors

Front 251

Define GEF proteins

Back 251

Guanine Nucleotide Exchange Factors

Front 252

Define GAP proteins

Back 252

GTPase Activating Protein

Front 253

Define the function of GTPase

Back 253

replace GTP with GDP

Front 254

What is the domain on the Adaptor Protein that binds to the phosphorylated region of the Tyrosine Kinase Receptor

Back 254

SH2 domain

Front 255

What is the domain on the Adaptor Protein that binds to the GEF protein

Back 255

SH3

Front 256

What is the function of the GEF protein?

Back 256

Catalyzes the exchange of GDP to GTP on Ras

Front 257

In Signal Transduction:

Define PI

Back 257

Phosphotidylinositol

Front 258

Define the importance of phosphatidylinositol

Back 258

membrane bound structure that through phosphorylation becomes PIP2 and PIP3

Front 259

What processes work on PIP2 leading to the release of Calcium intracellularly

Back 259

Phospholipase C + PIP2 creates IP3 and DAG

IP3 stimulates the release of Calcium from the Endoplasmic Reticulum

Front 260

What molecule is needed to change PIP2 to PIP3?

Back 260

Phosphatidylinositol 3–Kinase

Front 261

Define DAG

Back 261

Diacylglycerol

Front 262

What is the function of DAG

Back 262

DAG interacts with Protein Kinase C

Front 263

Describe the Jak–STAT pathway

Back 263

Receptor binds cytokines, dimerizes, and binds 2 Jaks which phosphorylate each other and the receptor. The receptor binds & phosphorylates 2 STATs which dissociate from the receptor, dimerize, and translocate to the nucleus

Front 264

Describe the Serine–Threonine Kinase Pathway

Back 264

TGF–beta binds to Type 2 receptor which phosphorylates the type 1 receptor.

The activated Type 1 receptor phosphorylates R–Smad.

R–Smad complexes with Co–Smad & migrates to nucleus

Front 265

Define the term GPCR

Back 265

G–Protein coupled Receptor

Front 266

Describe the G–protein structure [general]

Back 266

Subunits – alpha, beta, gamma

Alpha subunit is activated with the exchange of GDP to GTP, leaves the beta/gamma to go off intracellularly to create a cell response

Front 267

Describe the three types of G–alpha sub proteins that are relative to [general] signal transduction as covered in the directed study

Back 267

G–alpha–S
G–alpha–i
G–alpha–q

Front 268

What is the general function of G–alpha–S protein

Back 268

G–alpha–S is attached to GTP, detaches from gamma & beta components of the G–protein.
It targets the Adenylyl Cyclase which hydrolyzes GTP, G–alpha–S dissociates & returns to g/b portions of the G–protein.
Adenylyl Cyclase converts ATP to cAMP
cAMP activates Protein Kinase A which initiates the phosphorylation cascade
cAMP is degraded by cAMP phosphodiesterase

Front 269

Describe the function of G–alpha–I protein

Back 269

G–alpha–i protein inhibits Adenylyl Cyclase and thus the production of cAMP and the phosphorylation cascade

Front 270

What structure degrades cAMP

Back 270

cAMP phosphodiesterase

Front 271

What is the general function of G–alpha–Q protein

Back 271

G–Alpha–Q activates phospholipase C which ultimately stimulates DAG and IP3 release

Front 272

State the function of GAPs

Back 272

GTPase activating proteins – terminate reactions that utilize GTP

Front 273

What [DS] signal transduction reactions are inhibited by GAPs

Back 273

G–alpha–S
G–alpha–Q
Ras

Front 274

State the function of cAMP phosphodiesterase

Back 274

turns off cAMP which goes on to stimulate the phosphorylation cascade through Protein Kinase A

Front 275

What [DS] signal transduction reactions are inhibited by cAMP phosphodiesterase

Back 275

G–alpha–S due to the reliance on Adenylyl cyclase which catalyzes ATP to cAMP which travels on–wards to stimulate PKA and the phosphorylation cascade.

Front 276

What [DS] signal transduction reactions are inhibited by protein phosphodiesterase

Back 276

all phosphorylations

kinases–TK, JakSTAT, PI3–K

Front 277

State the function of protein phosphatase

Back 277

dephosphorylates proteins

Front 278

Describe receptor internalization and degradation and the effect

Back 278

tendency of cells to internalize structures and recycle the components. The reduction in the number of receptors bound to the membrane can decrease the overall sensitivity of the cell to outside messaging unless it maintains spare receptors and the fluctuation is negligible.

Front 279

Describe chemical chirality

Back 279

tendency for substances to have a combination right & left handed enantiomers

e.g. Mirror Images

Front 280

Describe chirality and the effect on pharmaceutical action

Back 280

chemical chirality influences pharmaceutical action because different isomers may be +/– effective or inactive

Front 281

Describe chirality and the effect on pharmaceutical toxicity

Back 281

chemical chirality influences toxicity because one isomer may have a therapeutic effect while the other may be toxic

ex: lamivudine. L–form tx HIV, R–form toxic

Front 282

Describe chirality and the effect on pharmaceutical metabolism

Back 282

chemical chirality influences drug–metabolism because if a dose is 50/50 racemic mixture of R–L handed structures and only half is absorbed via the GI or if one undergoes faster processing via the Renal/Liver systems, the overall effective dose is lessened than a purely 100% functional isomer

Front 283

Describe Drug Selectivity

Back 283

ability to affect one tissue, cell type, or organ while not others

Front 284

Describe determinants of drug selectivity

Back 284

Drug Dose
Drug Distribution
Receptor Distribution
Receptor Specificity & Selectivity

Front 285

What is the significance of a drugs selectivity

Back 285

a drug is given to stimulate/inhibit an effect in a specific target tissue, the drug's selectivity determines whether that drug will inhibit/stimulate ancillary tissues/processes causing side–effects not beneficial to the original cause of the administration.

Front 286

Describe the term pharmaceutical Agonist

Back 286

a drug that has an affinity to the receptor and also has intrinsic activity

Front 287

Define Intrinsic activity [pharm]

Back 287

able to produce a measurable effect

Front 288

Define the term pharmaceutical Antagonist

Back 288

a drug that has an affinity for a receptor but does not have intrinsic activity

receptor is activated but no measurable effect is produced

Front 289

Define the term pharmaceutical partial agonist

Back 289

a drug that interacts with the same receptors but cannot produce the same maximal effect as a full agonist

Front 290

Define the term Affinity [pharm]

Back 290

how strong an attraction that the drug has for the receptor.

measure of binding

Front 291

Define the term Potency [pharm]

Back 291

related to the drug binding affinity (Kd)

related to the amount of drug needed to produce a given intensity of effect

Higher binding reduces the overall drug needed to produce a specific effect

Front 292

Define the term Efficacy [pharm]

Back 292

the largest response or maximal effect – Emax
that a drug can produce

Front 293

Describe the [pharm] term Intrinsic Activity

Back 293

extent to which a bound Ligand activates a receptor

Agonist: IA=1
Antagonist: IA=0

Front 294

Describe the graph of two drugs, an agonist & a partial agonist

Back 294

The agonist will have a E–max of 100 while the partial agonist will partial agonist will have a reduced E–max.

The ED–50 value will be identical between the two.

Front 295

Define the [pharm] term E50

Back 295

The drug dose needed to reach 50% of the maximal drug effect (Emax)

Front 296

Describe the [pharm] term clinical efficacy

Back 296

depends on maximal efficacy & the drugs ability to reach the relevant receptors

Front 297

[pharm] Describe the relationship between ED–50, potency, binding affinity, and Kd

Back 297

The higher the binding affinity(lower Kd), the lower the drug concentration needed to reach 1/2 Emax (ED–50)

low ED50 = high affinity & potency, Low Kd

higher ED50 = low affinity & potency, HIGH Kd

Front 298

Describe the graded log–dose response curve

Back 298

the curve looks like a vertically stretched S with the maximum point being the Emax of the drug with the lowest point being the threshold dose.

Front 299

[pharm] Define threshold dose

Back 299

the lowest drug dose that will produce a therapeutic effect or an effect first appears

Front 300

[pharm] Describe the change to a graded log–dose response curve graph of agonists that differ in potency

Back 300

potency = drug concentration vs. effect

graph will shift R or L

there will be no change in E–Max

Front 301

[pharm] Describe the change to a graded log–dose response curve graph of agonists that differ in efficacy

Back 301

E–max will have a vertical shift (up/down)

Front 302

Describe [pharm] graphically the effect of a competitive antagonist on an agonist drug's action

Back 302

the antagonist binds to the same receptor site as the agonist, preventing it from binding while producing no intrinsic activity.
potency of drug is reduced, graph shifts right because the antagonist can be overcome with more a higher agonist concentration

No change to E–Max

Front 303

Describe [pharm] graphically the effect of a non–competitive antagonist on an agonist drug's action

Back 303

the antagonist binds to a non–active site on the receptor causing a conformational change in the receptor shape, eliminating the agonists ability to bind. IA=0.

increasing the agonist conc. has zero effect

Graph will show a downward shift in E–max

Front 304

Describe [pharm] graphically the effect of an irreversible antagonist on an agonist drug's action

Back 304

the antagonist covalently binds to receptor first, eliminating the agonists ability to bind. IA=0.

increasing the agonist conc. has zero effect

Graph will show a downward shift in E–max

Front 305

What are the advantages & disadvantages to irreversible inhibitors?

Back 305

adv – a bound inhibitor stays bound until replaced. Eliminates the need to repeatedly dose a patient to maintain therapy

dis–the body must replace the receptor before any other action can be taken (tetanus)

Front 306

Describe the concept of Spare receptors

Back 306

A cell maintains more receptors than strictly necessary to produce the maximal internal response. This increases cellular sensitivity to messengers such as hormones that are typically in low serum concentrations

effect: lower dose to provide a result

Front 307

Detail how spare receptors will interact with agonist and antagonistic drugs in a graph

Back 307

The graph of a drugs response will shift to the right without changing E–max if there are spare receptors present as there is no initial competition for sites between the agonist–antagonists.

Once all receptors are occupied, the antagonist will force the E–max downwards as they fight for an increased % of total receptors.

Front 308

[Pharm] describe chemical antagonists

Back 308

chemical interaction of two substances where a receptor is NOT involved

overall effect of the active substance is lost

IA = 0

Front 309

Name examples of chemical antagonists

Back 309

Metal chelators (EDTA) vs. toxic metals (lead)

Antiseptics

Front 310

[Pharm] describe pharmacologic antagonists

Back 310

a drug that has an intrinsic activity of 0

prevents action from happening

Front 311

[Pharm] describe physiological antagonists

Back 311

when there are opposing effects by 2 agonists
Biceps vs. Triceps = no movement of the arm

Front 312

Define ED50, LD50, TD50

Back 312

ED50 – Effective Dose in 50% of the populous

LD50 – lethal dose in 50% of the populous

TD50 – Toxic dose in 50% of the populous

Front 313

Define therapeutic index

Back 313

the ratio of Lethal dose (50%) to Effective dose (50%) that provides a measure of the safety of a drug

higher value = safer drug

Front 314

Describe the purpose of the cellular membrane

Back 314

structure/rigidity
transportation of substances in/out

Front 315

Describe why substrate transport across the cell membrane is necessary for cellular function

Back 315

cellular homeostasis

metabolism

cellular signaling

Front 316

Describe [bio] selectively permeable

Back 316

the ability of the cellular membrane to allow only desired substances to pass

Front 317

Cellular Membrane, describe the movement of Gases, Water, Ions, metabolic substrates, and proteins across the cellular membrane

Back 317

Gases & water(maybe) – simple diffusion

Ions & metabolic substrates – facilitated diff

proteins – facilitated diffusion if not necessary for cellular function

Front 318

Name the factors that determine substances membrane permeability

Back 318

size & charge – smaller = better

larger area = larger diffusion rate

Front 319

Describe the two forces in molecular movement in physiological systems

Back 319

Diffusion – randomized movement, movement from a higher to lower gradient

Bulk Flow – concerted manner, driving pressure

Front 320

List two systems that utilize bulk flow to function

Back 320

Circulation

Respiration

Front 321

Describe the term Concentration Gradient

Back 321

the concentration/charge/forces on a molecule on one side of a membrane versus those applied to the other side of the membrane.

Movement always from higher conc. gradients to lower if possible

Front 322

Describe the difference between simple & facilitated diffusion

Back 322

Simple diffusion – transfer of a molecule across a membrane without help

Facilitated diffusion – carrier molecules (transport proteins or ion channels) are needed for the molecule to move across the membrane

Front 323

Name the two types of proteins that facilitate diffusion

Back 323

transport proteins

ion–channel proteins

Front 324

list the factors that determine the rate of diffusion across the membrane

Back 324

concentration gradient
area of a membrane
membrane permeability of molecule
lipid solubility, size, charge

Front 325

Describe the graphic relationship between the rate of diffusion & concentration gradient across a membrane for a freely permeable molecule

Back 325

straight line with slope dependent on permeability coefficient vs concentration gradient
higher slope = higher permeability coeff.

Front 326

Describe the effect of saturation on the graph of the rate of molecular facilitated diffusion & concentration gradient across a membrane

Back 326

the graph will appear roughly straight with a slope depending on the permeability coefficient and concentration gradient until all of the facilitating proteins are occupied at 100% capacity where the graph will level off to a maximum rate

Front 327

Explain the role and selectivity of gating channels in controlling membrane permeability to ions

Back 327

Channels assist with membrane permeability in allowing specific ions to pass. Channels maintain different shapes.

Some require a ligand binding or specific voltage charge in order to allow passage to ions

Front 328

Describe the difference between voltage & ligand gating

Back 328

voltage – motivated by the net difference in charge across the channel

ligand – opens only when ligand–bound

Front 329

Define Active transport & its purpose

Back 329

Active transport refers to the process in which a solute is moved up a concentration gradient with an energy input (ATP)

Front 330

Explain secondary active transport

Back 330

utilizes the passage of another molecule (usually Na+) to facilitate the movement of a 2nd

Front 331

What is the functional importance of Secondary Active Transport

Back 331

move other substances into the cell by using the already existing process of sodium ion transport moving into the cell

Front 332

List the two types of secondary active transport proteins

Back 332

Symport – co–transport system, usually with glucose

Antiport – sodium in, another molecule out

Front 333

Name the secondary active transport mechanism that prevents glucose from appearing in the urine under the normal glycemic conditions

Back 333

glucose is reabsorbed via symports in the proximal renal tubules in conjunction with sodium ions

Front 334

Explain why glucose might be present in urine

Back 334

glucose will be found in the urine when the concentration of glucose exceeds the available symports, any excess glucose that is unable to be reabsorbed will be excreted in the urine (glycosuria)

Front 335

Give the Professional definition of osteopathic medicine

Back 335

Osteopathic medicine is a complete system of medical care practiced by physicians with an unlimited license that is represented by a philosophy that combines the needs of the patient with the current practices of medicine, surgery, and obstetrics. It emphasizes the interrelationship between structure and function, and that has an appreciation of the body's innate ability to heal itself.

Front 336

Give the 4 Principles of Osteopathic Medicine

Back 336

the body is a unit: body, mind & spirit

the body is capable of self–regulation, self–healing, and health maintenance

Structure & function are reciprocally interdependent

Rational treatment is based upon an understanding of these principles

Front 337

Define somatic dysfunction

Back 337

a somatic dysfunction is the impaired or altered function of related components of the somatic (body framework) system

Front 338

Describe the diagnosis of a Somatic Dysfunction

Back 338

1) Can treat with OMT

2) TART

Front 339

Define the mnemonic TART

Back 339

Tissue texture abnormalities
Asymmetry
Restriction of Motion
Tenderness

Front 340

Describe the concept of Joint Play

Back 340

movement of the synovial joint that is independent of & cannot be reproduced by a voluntary movement

essential for maximal pain free movement

can be restored by OMT

Front 341

What are the absolute contraindications of OMT

Back 341

The patient refuses to have OMT performed

Absence of a somatic dysfunction

Front 342

What are the relative contraindications of OMT

Back 342

When the potential benefits outweigh the risk of harm to the patient

Acute muscle spasms or muscle soreness or treatment reactions

Front 343

Describe direct OMT techniques [general]

Back 343

technique in which the restricted tissue is initially taken in the direction of the restriction of motion

Front 344

Describe indirect OMT techniques [general]

Back 344

techniques that initially position the restricted tissue toward the relative ease or freedom of motion

Less risk for the patient

Front 345

Discuss the range of motion diagram

Back 345

Depicts the RoM of any particular joint

Extremes:
Anatomical barrier: Passive RoM barrier

Physiological barrier: Active RoM barrier

Neutral: prone position

Front 346

Define soft tissue techniques

Back 346

a direct osteopathic technique that usually involves lateral & linear stretching, deep pressure, traction and/or separation of muscle origin & insertions while monitoring tissue response & muscle changes by palpation

Front 347

Define the differences between OMT:

Traction

Back 347

Traction – Longitudinal Muscle Stretch

think: tug of war on a rope

Front 348

Define the differences between OMT:

Kneading

Back 348

Kneading – Lateral Muscle Pressure

think: plucking a guitar string

Front 349

Define the differences between OMT:

Effleurage

Back 349

Effleurage – Stroking pressure to move fluid

Front 350

Define the differences between OMT:

Petrissage

Back 350

Petrissage – Squeezing pressure to move fluid

Front 351

Define the differences between OMT:

Tapotement

Back 351

Striking with the side of the hand

Front 352

Define the differences between OMT:

Skin Rolling

Back 352

Lifting the skin away from the deeper structures & rolling the skin fold along the body

Front 353

List the physiological mechanisms of action & therapeutic effects of soft tissue techniques

Back 353

Relax hypertonic muscles and reduce spasm
Stretch and increase the elasticity of shortened fascial structures
Enhance circulation to local myofascial structures
Improve local tissue nutrition, oxygenation, and removal of metabolic wastes
Improve abnormal neurological reflexes
Identify areas of restricted motion, tissue texture changes and sensitivity
Improve local systemic immune responses
Observe tissue response to the application of manipulative technique
Provide a general state of relaxation
Provide a general state of tonic stimulation
Optimize overall autonomic tone

Front 354

What are indications for soft tissue techniques

Back 354

any somatic dysfunction

Front 355

What are contraindications of soft tissue techniques

Back 355

local infection,
open wounds
lack of skin
soft tissue integrity
anti–coagulated patients with bruising

Front 356

Define OMT Treatment Reaction

Back 356

24–48 hours after OMT
muscle soreness relieved by rest, warm bath, mild anti–inflammatory/analgesic medication

Somatoemotional release

Front 357

Define Somatoemotional release

Back 357

if an emotion is connected in some way to a somatic dysfunction and this dysfunction later receives OMT has the risk of the unexpected recurrence of the emotion

Think: Doc's shoulder

Front 358

Where and when does replication occur?

Back 358

In the Nucleus

During S–Phase

Front 359

What is the role of helicase in DNA replication?

Back 359

separates the parental DNA strands

Hint: Zipper

Front 360

What is the role of topoisomerase in DNA replication

Back 360

relieves the supercoiling after helicase uncoils the strands

single–stranded binding proteins then keep the strands from binding back together

hint: Legs

Front 361

What is the role of single–stranded binding proteins in DNA replication

Back 361

prevents the parental strands from pairing back up after topoisomerase splits the strands and helicase uncoils the strand

Front 362

Describe the role of primase in DNA replication

Back 362

adds RNA primer once topoisomerase splits open the strands of DNA.

this is followed by DNA polymerase adding in the daughter strands

Front 363

What is the role of processivity factors in DNA replication?

Back 363

helps hold DNA polymerase onto the substrate as it creates the daughter strands

Front 364

Describe the role of RNAse in DNA replication?

Back 364

RNAse removes the RNA primers

after RNAse: ends are then joined by the ligase

Front 365

Which polymerase synthesizes the leading strand?

Back 365

DNA Polymerase E (epsilon)

Front 366

Which polymerase synthesizes the lagging strand?

Back 366

DNA Polymerase d (delta)

Front 367

Describe the function of Telomerase

Back 367

Edits the end of the lagging strand in order to get a segment containing the hydroxyl group that a ligase can use to bind the Okazaki fragments together

Front 368

What are Okazaki fragments?

Back 368

the segments of the lagging strand that are written by DNA polymerase delta and are joined by the DNA ligase

Front 369

What are the 3 types of RNA

Back 369

rRNA
mRNA
tRNA

Front 370

Describe the function of tRNA

Back 370

transport RNA moves amino acids for use in protein translation

Front 371

Describe the function of mRNA

Back 371

messenger RNA that is transcripted from DNA and it transported out of the nucleus and translated into proteins

Front 372

Describe the function of rRNA

Back 372

ribosomal RNA is a component of Ribosomes which are used to translate mRNA into proteins

Front 373

What is the importance of the TATA box?

Back 373

TATA binding protein must find the TATA box to begin transcription

Front 374

What is the role of the TATA binding protein

Back 374

TATA binding proteins locate the TATA box

Front 375

What is the role of transcription factors

Back 375

transcription factors recruit RNA polymerase which is used to synthesize RNA

Front 376

What is the function of RNA polymerase

Back 376

RNA polymerase synthesizes RNA during transcription

Front 377

What is the importance of the 5'–cap on RNA

Back 377

the 5'–cap increases the half–life of the transcripted RNA & is important in binding the transcript to the ribosome

Front 378

What is the part of RNA that increases the half–life & assists in binding the mRNA to the ribosome?

Back 378

5'–cap

Front 379

What is the polyA–tail and what does it do?

Back 379

the polyA–tail protects the transcribed mRNA from degradation

Front 380

Describe the composition of ribosomes in Eukaryotes vs. Prokaryotes

Back 380

ribosomes = rRNA + ribosomal proteins

Eukaryotes: 60s + 40s = 80s

Prokaryotes: 50s + 30s = 70s

Front 381

What are the two types of ribosomal subunits in Eukaryotes

Back 381

60s + 40s

combine into a 80s

Front 382

What are the two types of ribosomal subunits in prokaryotes

Back 382

50s + 30s

combine into a 70s

Front 383

Describe the process of transcription [general]

Back 383

TATA binding proteins find TATA box

Transcription factors recruit RNA polymerase

RNA polymerase synthesizes new RNA into mRNA

mRNA travels to the ribosomes for processing

Front 384

List the three steps of RNA translation [general]

Back 384

Initiation
Elongation
Termination

Front 385

Describe RNA translation Initiation

Back 385

tRNA gets charged by Aminoacyl tRNA synthetase

initiation factors bind – initiate translation

charged tRNA finds 80s[40s/60s] ribosomal subunit

elongation begins

Front 386

Describe RNA translation elongation

Back 386

tRNA+Amino Acid are picked up by the elongation factors
complex enters ribosomal A site
Anticodon matched against mRNA at A–site
chain is shifted to the P–site where peptide bond formed between the amino acid in P–site with the incoming amino acid in A–site
proofreading via the elongation factors

Front 387

What is the function of peptidyl transferase?

Back 387

formation of the peptide bonds between the amino acids in P–site and A–site

Front 388

What is the importance of chaperones & heat shock proteins?

Back 388

these are required to overcome kinetic barriers

force the protein into the correct desired protein folding

Front 389

Define Free ribosomes

Back 389

ribosomes not attached to the endoplasmic reticulum

Front 390

Compare the processing of proteins that are synthesized on free ribosomes vs those on the rough ER

Back 390

free ribosomes – may stay in the cytoplasm or certain organelles

ER – enter golgi apparatus and are subjected to exocytosis

Front 391

What is the translation function of aminoacyl tRNA synthetase

Back 391

charges the tRNA before synthesis

Front 392

What is the function of initiation factors in RNA translation

Back 392

required to find the start codon & thus initiate translation

Front 393

What is the role of histones?

Back 393

chromatin remodeling is needed to unwind the chromatin that are tightly bound around the histone protein. Histones are proteins that wind DNA very tightly so as to compact it into a very small area. These combine into a 4–protein octamer within the nucleus.

Front 394

What is the function of HATs

Back 394

Histone acetyltransferase – responsible for turning ON gene expression. HATs transfer an acetyl group to the chromatin to neutralize the charge–attraction between the DNA strand and the histone resulting in the DNA unwinding

Recruited by activator proteins

Front 395

What is the function of HDACs

Back 395

Histone deacetylases turn OFF gene expression by removing the acetyl group & allowing the recondensing of the histone octamer.

Recruited by repressor proteins

Front 396

Describe methylation and the effect on DNA

Back 396

methylation of genes results in them being less readily transcribed. Problems are encountered when the STOP codon is methylated.

Front 397

What is the function of methyltransferases

Back 397

maintain methylation by adding methyl groups to the daughter strands and performing maintenance methylation

Front 398

What is name for the process by which new methyl groups are added?

Back 398

De Novo Methylation

Front 399

By what mechanisms are transcription factors regulated?

Back 399

their own expression level
expression of coactivators & corepressors
presence of inhibitors
phosphorylation

Front 400

Describe alternative RNA processing & RNA editing

Back 400

RNA editing – bases are altered chemically, using different exons

by alternative splicing to allow different protein sequencing from the same gene

Front 401

Which stays with the protein: Intron or Exons?

Back 401

Exons, they exit with the protein

Front 402

Describe 3 mechanisms affecting RNA stability

Back 402

regulatory proteins
5'–cap
poly–A tail

Front 403

Describe the effect of MicroRNA on gene expression

Back 403

induce transcript degradation
block translation

Front 404

Define cell "resting membrane potential"

Back 404

The resting membrane potential of a cell is the point at which there is zero net movement of ions across the cell membrane.

Front 405

What are the two uses the resting membrane potential for a cell?

Back 405

Excitability – ability to signal electrically

Absorb & Secrete solutes – Think Nernst Potential

Front 406

What is the voltage of a cell at the typical resting membrane potential?

Back 406

–60 to –85 mV

Front 407

Describe why the cellular resting membrane potential is maintained at a specific value?

Back 407

the cell membrane overs around 60–85 mV because the membrane is fully permeable to K+ ions that have a Nernst potential of –88 mV but some Na+ ions (NP=+70) leak through forcing the membrane more positive

Front 408

What is the extracellular membrane potential in mV?

Back 408

always 0 mV

Front 409

What are two types of cells that utilize membrane potential?

Back 409

Nerve cells
muscle cells

Front 410

What are the two forces that control movement of ions across the membrane

Back 410

Concentration gradient
Electrical Gradient

Front 411

Define concentration gradient

Back 411

directs the flow of ions based on the concentration of solutes on the outside of the membrane versus those on the inside of the membrane. Solutes always move from high to low concentration if permitted

Front 412

Define electrical gradient

Back 412

difference in the electrical charges in vs outside the membrane. net flow will move to equalize the difference between negative & positive sides.

Front 413

Define Driving Force [cell membrane]

Back 413

force that dictates which direction the molecules move. Combines electrical & concentration gradients.

Front 414

Define equilibrium in terms of membrane ion movement

Back 414

No driving force for ion movement. It is established when the conc. & electrical gradient are equal but opposite

Front 415

What is the Nernst equilibrium potential

Back 415

is the membrane potential at which the concentration gradient + electrical gradient are equal but opposite e.g. balanced

Front 416

What is the NP of Sodium?

Back 416

+70 mV

Front 417

What is the NP of Potassium?

Back 417

–88 mV

Front 418

What is the NP of Chlorine?

Back 418

–47 mV

Front 419

What is the NP of Calcium?

Back 419

+122 mV

Front 420

What are the concentrations of Sodium?

Back 420

in: 10 mM
out: 140 mM

Front 421

What are the concentrations of Potassium?

Back 421

in: 140 mM
out: 5 mM

Front 422

What are the concentrations of Chlorine?

Back 422

in: 20 mM
out: 116 mM

Front 423

What are the concentrations of Calcium?

Back 423

in: 0.0001 mM
out: 1 mM

Front 424

Describe the factors that make a membrane selectively permeable to an ion

Back 424

membrane permeability to an ion depends on the # of open channels selective for that ion present in the membrane

Front 425

Describe the graphic relationship between [K+]o, Ek, and the membrane potential

Back 425

[K+]o is the concentration of K+ ions outside
Ek is the NP for potassium
Membrane potential is the membrane response to balance the gradients

Front 426

If the membrane is solely permeable to Sodium ions, what is the membrane potential?

Back 426

+70 mV

Front 427

Explain why membrane potential is different from Ek at very negative membrane potentials

Back 427

there will be slight movement of Na+ into the cell from Na+ leak channels

Front 428

What is the ratio between Na+/K+ ions in a typical resting permeability

Back 428

1 Na+ to 100 K+

in : out
10 : 140 Na
140 : 5 K

Front 429

Describe the influence of Ca2+ & Cl– ions on the resting membrane potential in nerves and in the muscle cell

Back 429

Calcium = zero influence on membrane potential

Chlorine influences skeletal muscle on most cell types.

Front 430

What is the membrane potential for Skeletal muscle cells?

Back 430

–85 mV

Front 431

Define depolarization

Back 431

a situation where the membrane or Nernst potential become less negative

Front 432

Define hyperpolarization

Back 432

Nernst or membrane potential becomes more negative

Front 433

Describe the 7 basic elements of Healthcare communication

Back 433

Open the discussion
Build a relationship
Gather information
Understanding the patients perspective
Sharing Information
Reaching agreement of problems/plans
Providing closure

Front 434

List the methods drug administration

Back 434

Oral

Front 435

Describe the benefits & disadvantages of:

Oral administration

Back 435

most common route, generally the safest, GI irritation, First–pass effect

Front 436

Define First–Pass metabolism

Back 436

metabolism of the drug by the GI bacterial enzymes, the GI tissue enzymes, and by the Liver enzymes prior to the drugs insertion into the systemic circulation

Front 437

Describe the benefits & disadvantages of:

Rectal administration

Back 437

potentially avoids first pass, absorption is slow and possibly erratic

Front 438

Describe the benefits & disadvantages of:

transdermal administration

Back 438

must be lipid–soluble, slow absorption, varying bioavailability

Front 439

Describe the benefits & disadvantages of:

sublingual administration

Back 439

direct absorption into the systemic circulation, higher bioavailability, rapid absorption

Front 440

Describe the benefits & disadvantages of:

Buccal administration

Back 440

direct absorption into the systemic circulation, higher bioavailability, rapid absorption

Front 441

Describe the benefits & disadvantages of:

topical administration

Back 441

no systemic exposure, localized effect

should be lipid–insoluble

Front 442

Describe the benefits & disadvantages of:

subcutaneous administration

Back 442

absorption is constant, complete, and slow
depends on blood flow for absorption rate
bypass First Pass effect

Front 443

Describe the benefits & disadvantages of:

intramuscular administration

Back 443

absorption by simple diffusion, generally rapidly, higher bioavailability
bypass First Pass effect

Front 444

Describe the benefits & disadvantages of:

intravenous administration

Back 444

avoids first–pass effect, fastest route, complete bioavailability, rapid effect, toxicity and occur with rapid drug administration

Front 445

Describe the benefits & disadvantages of:

inhalation administration

Back 445

local effect & systemic effect
absorption is rapid
avoids first–pass effect

Front 446

Describe the benefits & disadvantages of:

Intrathecal administration

Back 446

administration into the cerebrospinal fluid
used for local, rapid effect on the meninges & CS axis
avoids blood–brain barrier

Front 447

Describe the graph of the IV drug concentration over Time

Back 447

The IV dosage avoids the first pass effect and is placed directly into the systemic circulation at full concentration with subsequent elimination by the liver & kidneys

Front 448

Describe the graph of a PO drug concentration over time

Back 448

The PO dosage undergoes delivery through the GI system after undergoing First Pass metabolism prior to delivery into the systemic circulation where it subsequently undergoes elimination.
Rise from delivery to systemic concentration, then slow downgrade.

Front 449

Describe primary process by which drugs cross the membrane

Back 449

First Order process: rate is dependent on concentration (high to low)

Front 450

Describe the importance of lipid–solubility on drugs membrane permeability

Back 450

higher lipophilic = higher solubility = faster diffusion across the membrane

Ionization decreases the lipid–solubility.

pH controls %ionization and thus % absorbed

Front 451

Describe the relationship between pH & ionization of a drug which is either a weak organic acid or base.

Back 451

the drug must be administered so that the pH of the delivery system pushes the drug to unionized structure in order to pass through the membrane

Front 452

Define Strong vs. Weak Acids & bases.

Back 452

Strong Acid & Bases: fully ionized in all solutions

Weak Acids: only ionize at higher pH's
Weak Bases: only ionize at lower pH's

Front 453

Define pKa

Back 453

pH where the substance is 50% ionized & 50% unionized

Front 454

Provide the equation for a weak acid


(think Log)

Back 454

pH–pKa = log [ionized / unionized]

Front 455

Provide the equation for a weak base


(think Log)

Back 455

pH–pKa = log [unionized / ionized]

Front 456

List the factors that affect the rate & extent of oral absorption

Back 456

drug solubility
lipid solubility (nonionized form)
drug concentration @ absorption rate
surface area for absorption
blood flow @ absorption site
gastric emptying
food
metabolism of drug

Front 457

What determines bio–availability

Back 457

% of drug in systemic circulation after:

First pass effect
Rate of extraction

Front 458

[ANS Pharmacology]

Review the Neuroanatomy of the sympathetic neurons

Back 458

spinal cord
pre–ganglionic neuron
ACh to N–receptor @ synapse/ganglia
post–ganglionic neuron
target tissue
*sympathetic ganglion is "typically" farther from the target tissue than the parasympathetic ganglia

Front 459

[ANS Pharmacology]

Tyrosine is changed by Tyrosine Hydroxylase to becomes what drug inside the Nerve Terminal

Back 459

Dopa

Front 460

[ANS Pharmacology]

Dopa is changed by what to becomes Dopamine inside the Nerve Terminal

Back 460

Dopa decarboxylase

Front 461

[ANS Pharmacology]

Dopamine is changed to Epinephrine via what enzyme?

Back 461

Dopamine Beta–Hydroxylase

Front 462

[ANS Pharmacology]

Norepinephrine is changed to Epinephrine by what enzyme?

Back 462

phenylethanolamine–N–methyltransferase

Front 463

[ANS Pharmacology]

Describe the release & signalling of neurotransmitter from cholinergic & adrenergic neurons

Back 463

– an action potential causes the release of Ca2+ from the axon bulb so that vesicles with the neurotransmitter can go through exocytosis
–the exocytosis causes the release of the neurotransmitter into the synaptic cleft & then the neurotransmitter binds to receptor sites on the post–synaptic area

Front 464

[ANS Pharmacology]

Differentiate between the direct–acting & indirect–acting cholinomimetics

Back 464

–Direct–acting are Choline Esters that stimulate the same receptors that ACh itself would without any intermediates (RISK: will stimulate both PSNS & SNS)
–Indirect–acting are either reversible or irreversible cholinomimetics that inhibit acetylcholinesterase

Front 465

[ANS Pharmacology]

Explain the aging process of organophosphates

Back 465

– organophosphates covalently bind via phosphate group to the serine–OH group @ active site
–permanently inactivates enzyme
–restoration requires new enzyme molecules
–slow release of ethyl group (aging) makes it impossible for 2–PAM to break the bond of drug–enzyme

Front 466

[ANS Pharmacology]

Explain the effect after Muscarinic & Nicotinic Receptor activation & blockade for:

Secretory

Back 466

stimulation of the thermo–regulatory sweat
lacrimal & nasopharyngeal glands

Blockade – suppressed thermo–regulatory sweating "atropine fever"

Front 467

[ANS Pharmacology]

Explain the effect after Muscarinic & Nicotinic Receptor activation & blockade for:

Gastrointestinal

Back 467

activation – increased secretory & motor activity, salivary & gastric glands are stimulated, peristaltic activity is increased, sphincters are relaxed

Blockade – reduced motility & secretion

Front 468

[ANS Pharmacology]

Explain the effect after Muscarinic & Nicotinic Receptor activation & blockade for:

Genitourinary

Back 468

activation – stimulation of detrusor muscle & relaxation of the trigone & sphincter muscles of the bladder

Blockade – relaxes smooth muscle of the ureters & bladder walls, slow voiding

Front 469

[ANS Pharmacology]

Explain the effect after Muscarinic & Nicotinic Receptor activation & blockade for:

Respiratory

Back 469

activation – contracts the smooth muscle of the bronchial tree,

Blockade – ?

Front 470

[ANS Pharmacology]

Explain the effect after Muscarinic & Nicotinic Receptor activation & blockade for:

Cardiovascular

Back 470

activation – reduction in peripheral vascular resistance & change in the heart rate & contractility

blockade – SA & AV node sensitive to blockade, vasodilation blocked in the blood vessels

Front 471

[ANS Pharmacology]

Explain the effect after Muscarinic & Nicotinic Receptor activation & blockade for:

Central Nervous

Back 471

activation – regulation of the neurotransmitter release

blockade – sedative effects

Front 472

[ANS Pharmacology]

Explain the effect after Muscarinic & Nicotinic Receptor activation & blockade for:

Peripheral Nervous

Back 472

activation – initial response is simultaneous activation of PANS & SANS

blockade – ?

Front 473

[ANS Pharmacology]

Explain the effect after Muscarinic & Nicotinic Receptor activation & blockade for:

Neuromuscular Junction

Back 473

activation – contraction

blockade –

Front 474

[ANS Pharmacology]

Identify the major adverse effects of cholinergic agents

Back 474

excessive activation of the cholinergic system

DUMBBELSS: Diarrhea, Urination, Miosis, Bronchoconstriction, Bradycardia, Emesis, Lacrimation, Salivation, Sweating

Front 475

[ANS Pharmacology]

Explain why anti–nicotinics are rarely used

Back 475

blocking N–receptors will block the entire ANS

Front 476

[ANS Pharmacology]

List the common side effects of Anti–Muscarinic Agents (Anti–DUMBBELSS)

Back 476

Opposite of DUMBBELSS

Constipation, No Urination, Mydriasis, Bronchodilation, Tachycardia, No Emesis, No Tearing, Dry Mouth, No Sweat

Front 477

[ANS Pharmacology]

Describe the major effects of alpha–1 receptors

Back 477

–Vasoconstriction
–Increased peripheral resistance
–Increased blood pressure
–mydriasis
–increased closure of internal sphincter of the bladder

Front 478

[ANS Pharmacology]

Describe the major effects of alpha–2 receptors

Back 478

–inhibition of norepinephrine release
–inhibition of ACh release
–inhibition of insulin release

Front 479

[ANS Pharmacology]

Describe the major effects of Beta–1 receptors

Back 479

–Tachycardia
–Increased lipolysis
–increased myocardial contractility

Front 480

[ANS Pharmacology]

Describe the major effects of Beta–2 receptors

Back 480

–vasodilation
–slightly decreased peripheral resistance
–bronchodilation
–increased muscle & liver glycogenolysis
–increased release of glucagon
–relaxed uterine smooth muscle

Front 481

[ANS Pharmacology]

Identify the effects of the sympathomimetic agonists & antagonists for:

Genitourinary System

Back 481

alpha agonists can promote urinary continence

Front 482

[ANS Pharmacology]

Identify the effects of the sympathomimetic agonists & antagonists for:

Cardiovascular System

Back 482

a1 receptor – activation leads to arterial & venoconstriction
a2 receptor – activation leads to vasoconstriction
B receptors – Heart (B1)–stimulation increases cardiac output, Vascular Beds (B2) decrease peripheral resistance = vasodilation

Front 483

[ANS Pharmacology]

Identify the effects of the sympathomimetic agonists & antagonists for:

Respiratory System

Back 483

B2 receptors in bronchiole smooth muscle causes bronchodilation

Front 484

[ANS Pharmacology]

Identify the effects of the sympathomimetic agonists & antagonists for:

Central Nervous System

Back 484

depends on ability to cross BBB

effects vary from mild alerting to full block psychosis

Front 485

[ANS Pharmacology]

Identify the effects of the sympathomimetic agonists & antagonists for:

Apocrine Sweat System

Back 485

adrenoceptor stimulation leads to increased sweat production

Front 486

[ANS Pharmacology]

Identify the effects of the sympathomimetic agonists & antagonists for:

Eye System

Back 486

alpha agonists can reduce intraocular pressure & cause mydriasis

Front 487

[ANS Pharmacology]

Identify the effects of the sympathomimetic agonists & antagonists for:

Metabolism System

Back 487

activation of beta receptors can lead to lipolysis

can enhance glycogenolysis in the liver

regulation of insulin secretion

Front 488

[ANS Pharmacology]

Identify the adverse drug reactions of alpha & beta receptor blockade

Back 488

postural hypotension

reflex tachycardia

beta receptor blockade

Front 489

[ANS Pharmacology]

Describe the mechanism of postural hypotension via a/b receptor blockade

Back 489

due to antagonism of sympathetic nervous system stimulation of alpha–1 receptors in venous smooth muscle that causes less contraction = vasodilation = lower blood pressure

(often seen after the first dose of medication)

Front 490

[ANS Pharmacology]

Describe the mechanism of Reflex Tachycardia via a/b receptor blockade

Back 490

result of exposure to nonselective alpha antagonists when blood pressure is lower than normal

in the heart, the release of norepinephrine activates primarily Beta receptors as a result of agents that block

Front 491

[ANS Pharmacology]

Describe the mechanism of Beta Receptor Blockade via a/b receptor blockade

Back 491

depresses myocardial contractility & excitability, causes cardiac decompensation, severe hypotension, bradycardia, heart failure, fatigue/exercise intolerance

Front 492

[Autonomics of Select Organs]

What sympathetic receptor type causes smooth muscle contraction in the Eye

Back 492

alpha–1 adrenergic receptor

Front 493

[Autonomics of Select Organs]

What sympathetic receptor type causes smooth muscle relaxation in the eye?

Back 493

Beta–2 adrenergic receptor

Front 494

[Autonomics of Select Organs]

What parasympathetic receptor type causes smooth muscle contraction

Back 494

M Receptor

Front 495

[Autonomics of Select Organs]

Describe how the action of the Ciliary Muscle affects the lens

Back 495

Relaxed = taut suspensory ligaments = flat lens = far vision

Contracted = loosened suspensory ligaments = rounded lens = near vision

Front 496

[Autonomics of Select Organs]

What nerve, receptor, transmitter is responsible for relaxing the Ciliary muscle in order to enhance far vision

Back 496

Sympathetic

Beta–2 Receptor

Epinephrine

Front 497

[Autonomics of Select Organs]

What nerve, receptor, transmitter is responsible for contracting dilator pupillae muscle and thus dilating the pupil in order to enhance far vision

Back 497

Sympathetic

alpha–1 Receptor

Norepinephrine

Front 498

[Autonomics of Select Organs]

What nerve, receptor, transmitter is responsible for contracting the sphincter pupillae muscle and thus constricting the pupil

Back 498

Parasympathetic

M Receptor

Acetylcholine

Front 499

[Autonomics of Select Organs]

Describe the s/sx of Horner's syndrome

Back 499

pupil constricts in one eye
superior eyelid droops
dilation of ipsolateral blood vessels
No sweating on ipsolateral side

Front 500

[Autonomics of Select Organs]

Horner's Syndrome

Explain why sympathetic nerve damage causes the pupil in one eye to constrict

Back 500

lack of the sympathetic dilation mechanism via the b–1 adrenergic receptor on the dilator pupillae smooth muscle

Front 501

[Autonomics of Select Organs]

Horner's Syndrome

Explain why sympathetic nerve damage causes the dilation of ipsolateral blood vessels

Back 501

the sympathetic nerves are responsible for the vasoconstriction via alpha–adrenergic receptors

Front 502

[Autonomics of Select Organs]

Horner's Syndrome

Explain why there is a lack of sweating on the ipsolateral side

Back 502

The sympathetic nerves control sweat glands (other than the palms) via M–Receptors & Acetylcholine

Front 503

[Autonomics of Select Organs]

Horner's Syndrome

Explain why the ipsolateral eyelid droops

Back 503

the sympathetic system controls the positioning of the eyelid via contraction

(alpha–1 receptors)

Front 504

[Autonomics of Select Organs]

Describe the sequence of nerve stimulation that results in bronchodilation

Back 504

Bronchioles with Beta–2 receptors

Albuterol | Epinephrine–like agonist

Bronchial dilation

Front 505

[Autonomics of Select Organs]

Describe the sequence of nerve stimulation that results in bronchoconstriction

Back 505

Bronchial M–Receptors

Parasympathetic Nerve + Ach neurotransmitter

Bronchoconstriction

Front 506

[Autonomics of Select Organs]

Explain one of the risks of administering too much B2 receptor agonist

Back 506

B2 receptors will hide if exposed to too much agonist

Front 507

[Autonomics of Select Organs]

What are the basic roles of the SNS and PSNS in urinary tract function

Back 507

SNS– helps with filling, PSNS– helps with emptying

Front 508

[Autonomics of Select Organs]

List the target tissues, receptors and actions involved in filling and emptying the bladder

Back 508

SNS relax the detrusor muscle which is activated by B2 receptors, contract the trigone and internal sphincter which is activated by A1 receptors. PSNS contract the detrusor muscle which activate M receptors, and relax the trigone and internal sphincter which activate M receptors.

Front 509

[Autonomics of Select Organs]

How do we prevent or initiate micturition

Back 509

Spinal reflex– stretch receptors in the urinary bladder send afferent message to the spinal cord at sacral level, parasympathetic NS sends efferent message to contract the detrusor muscle, and relax the trigone and internal sphincter. Spinal reflex with superimposed higher brain center efferents use the Cortex and Brainstem to determine when it is socially acceptable to urinate.

Front 510

[Autonomics of Select Organs]

Define the role of the SNS for sweating

Back 510

The SNS stimulates the release of acetylcholine via sympathetic cholinergic neurons which bind to M receptors and cause all other sweat glands other than those in the palms of the hands to produce sweat.

Front 511

[Autonomics of Select Organs]

List the ANS function, transmitter and receptors for the rate and contractility of the heart

Back 511

The sympathetic system will stimulate the SA Node, AV Node, and Atria and ventricles, causing an increase in heart rate, conduction through the node, and contractility, respectfully. The sympathetic receptor for the heart is the β1, the transmitter NE

Front 512

[Autonomics of Select Organs]

Describe how the ANS alters blood flow during exercise

Back 512

Blood pressure is a combination of cardiac output and peripheral vascular resistance. Essentially no parasympathetic innervation of blood vessels. Sympathetics include α1 receptors for vasoconstriction (rest of blood vessels) and β2 receptors for vasodilation (blood vessels to liver/skeletal muscle/coronary/cerebral).

Front 513

[Autonomics of Select Organs]

List the ANS receptor sites and resulting function on GI sphincters and smooth muscle along the intestine

Back 513

Parasympathetic relax sphincter and increase tone and motility by the binding of Acetylcholine to M receptors. Sympathetic contract sphincter and decrease tone and motility by the binding of Norephinerine to A1, A2 and B2

Front 514

[OPP]

Describe the osteopathic approach to patient care

Back 514

The osteopathic approach has a patient–centered focus, and it optimized health using standard and unique skills, including hands–on manual diagnosis and treatment. OMT is indicated when a physician makes the diagnosis of somatic dysfunction AND relates it to a patient’s problem. It may also include pharmacological agents, exercise, nutritional counseling, surgical procedures, or lifestyle modifications.

Front 515

[OPP]

List the 5 components of the 5 Model approach

Back 515

Biomechanical
Respiratory–Circulatory
Metabolic
Neurologic
Behavioral

Front 516

[OPP]

Describe the Bioimechanical approach & goals

Back 516

views the patient from a structural or mechanical perspective. The objective is to optimize the patient’s adaptive potential through restoration of structural integrity and function. The goal of this model is biomechanical adjustment and mobilization of joints.

Front 517

[OPP]

Describe the Respiratory–Circulatory approach & goals

Back 517

focused on the respiratory and circulatory components of the homeostatic response in pathophysiological processes. This model concerns itself with the maintenance of extra– and intracellular environments through the unimpeded delivery of oxygen and nutrients and the removal of cellular waste products. The goal of this model is to improve all of the diaphragm restrictions in the body.
Think: arthritic knee, no direct OMT, instead, improve R–C flow

Front 518

[OPP]

Describe the Metabolic approach & goals

Back 518

focused on energy conservation and efficiency of metabolic functions. The goal is to enhance the self–regulatory and self–healing mechanisms while fostering energy conservation by balancing the body’s energy expenditure and enhance immune system, endocrine, and organ functions

Front 519

[OPP]

Describe the Neurologic approach & goals

Back 519

This model views the patient’s problems in terms of aberrancies or impairments of neural function. The goal is to attain autonomic balance and address neural reflex activity, remove facilitated segments, decrease afferent nerve signals, and relieve pain

Front 520

[OPP]

Describe the Behavioral approach & goals

Back 520

This model recognizes that the assessment of a patient’s health includes assessing his or her mental, emotional, and spiritual state of being as well as person lifestyle choices.

Front 521

[OPP]

Explain how these 5 coordinated body functions are interrelated & interdependent

Back 521

Case study: Otitis Media
Biomechanical: blocked eustachian tube
R–C: decreased lymphatic & vascular flow to inflamed area
Metabolic: infected middle ear = impaired immune system
Neurologic: Pain, pressure on nerves
Behavioral: altered mental state due to OM

Front 522

[OPP]

Describe the relationship of the musculoskeletal system to the 5 models

Back 522

provide the framework within which all other systems reside

represents the entry–point for both dx & tx

often reflects or gives clues as to what is occurring internally

Front 523

[OPP]

Explain how the osteopathic manipulative treatment affects physiological function & restores health:

Biomechanical

Back 523

OMT can positively affect physiological functions such as coordination and symmetry of musculoskeletal and myofascial structures in posture and motion, and works to improve quality and quantity of motion

Front 524

[OPP]

Explain how the osteopathic manipulative treatment affects physiological function & restores health:

Respiratory–Circulatory

Back 524

OMT works to increase/improve respiration, circulation, venous, and lymphatic drainage

Front 525

[OPP]

Explain how the osteopathic manipulative treatment affects physiological function & restores health:

Metabolic

Back 525

Tx (although not manipulative in nature) works to maintain metabolic processes, homeostasis, energy balance, regulatory processes, immunology, digestion, waste removal, etc.

e.g. nutritional aspects: zinc, selenium, Vit D, iron deficiencies, formula vs. breast milk

Front 526

[OPP]

Explain how the osteopathic manipulative treatment affects physiological function & restores health:

Neurological

Back 526

Treatment affects focuses on the reduction of mechanical stresses, balance of neural inputs, and the elimination of nociceptive drive

Front 527

[OPP] Define Nociceptive Drive

Back 527

of, relating to, or denoting pain arising from the stimulation of nerve cells (often as distinct from that arising from damage or disease in the nerves themselves).

Front 528

[OPP]

Explain how the osteopathic manipulative treatment affects physiological function & restores health:

Behavioral

Back 528

OMT is employed within this model with the goal of improving the body’s ability to effectively manage, compensate, or adapt to certain stressors.

Front 529

[OPP]

Describe the anatomical regions most commonly associated with:

Biomechanical

Back 529

bones, muscles, postural muscles, spine, extremities, etc

Front 530

[OPP]

Describe the anatomical regions most commonly associated with:

Respiratory–Circulatory

Back 530

thoracic inlet, thoracic and pelvic diaphragms, Tenotium cerebelli, costal cage

Front 531

[OPP]

Describe the anatomical regions most commonly associated with:

Metabolic

Back 531

internal organs, endocrine glands

Front 532

[OPP]

Describe the anatomical regions most commonly associated with:

Neurological

Back 532

head, brain, spinal cord, autonomic nervous system, peripheral nerves

Front 533

[OPP]

Describe the anatomical regions most commonly associated with:

Behavioral

Back 533

Brain

Front 534

[ANS]

Name the two components of the ANS

Back 534

Sympathetic

Parasympathetic

Front 535

[ANS]

Describe the Sympathetic Nervous System's purpose

Back 535

Fight or Flight

increase or dilate
control peripheral blood vessels
glycogenolysis

Front 536

[ANS]

Describe the Parasympathetic Nervous System's purpose

Back 536

Rest & Digest

decrease or constrictg

Front 537

[ANS]

List the names of the neurons & synapses that make up the ANS

Back 537

preganglionic | presynaptic
postganglionic | postsynaptic

Synapse | ganglion

Target tissue

Front 538

[ANS]

List the function of each of the Sympathetic target tissues

Back 538

Smooth Muscle of all organs
Cardiac Muscle
Glandular cells [sweat, salivary, digestive,

Front 539

[ANS]

List the function of each of the Parasmpathetic target tissues

Back 539

Smooth Muscle
Glands – GI & Excretory Organs, genitalia, lungs,
Atria
tear & salivary glands
eye muscles

Front 540

[ANS]

Describe the anatomical Origin & route of the parasympathetic innervation to each target tissue

Back 540

long presynaptic neuron in which there is a short postsynaptic neuron. The synapse is within or very close to the target organ

Front 541

[ANS]

Describe the anatomical Origin & route of the sympathetic innervation to each target tissue

Back 541

short presynaptic neuron from the spinal cord then to the sympathetic chain out to the body

Front 542

[ANS–2]

Describe the anatomical organization of the spinal nerve & Sympathetic Nervous System

Back 542

Anterior Root & Posterior Root for a specific segment of the body

Spinal cord gray matter (cell bodies) consist of a:
Posterior horn to which the sensory neuron enter
Anterior Horn to which the motor neuron originate

Sympathetic nerves enter sympathetic chain for synapse/ganglia

Front 543

[ANS–2]

What is segmentation in the nervous system

Back 543

Each spinal nerve innervates a different section of the body

Front 544

[ANS–2]

Sympathetic Somatic Nervous System Segmentation

Back 544

Each segment consists:
Myotomes: of a group of muscles
Schlerotomes: a group of connective tissues
Dermatomes: a patch of skin

Front 545

[ANS–2]

What vertebral region enervates:

cardiovascular

Back 545

T1–5

Front 546

[ANS–2]

What vertebral region enervates:

Respiratory

Back 546

T2–7

lungs extend slightly lower than the Heart

Front 547

[ANS–2]

What vertebral region enervates:

Stomach, Liver, Gall Bladder

Back 547

T5–9

Front 548

[ANS–2]

What vertebral region enervates:

Pancreas

Back 548

T5–11

Front 549

[ANS–2]

What vertebral region enervates:

Small Intestines

Back 549

T9–11

Front 550

[ANS–2]

What vertebral region enervates:

Ovaries & Testicles

Back 550

T9–11

Front 551

[ANS–2]

What vertebral region enervates:

Kidneys & Ureters

Back 551

T10–L1

Front 552

[ANS–2]

What vertebral region enervates:

Urinary Bladder

Back 552

T10–L1

Front 553

[ANS–2]

What vertebral region enervates:

Large Intestines, Rectum

Back 553

T8–L2

Front 554

[ANS–2]

What vertebral region enervates:

Uterus

Back 554

T10–L1

Front 555

[ANS–2]

What vertebral region enervates:

Prostate

Back 555

L1–2

Front 556

[ANS–2]

Describe the Somato–Somatic Spinal Reflex

Back 556

Somatic sensory nerve is stimulated, afferent signal enters spinal cord, stimulates interneuron, interneuron stimulates presynaptic motor neuron, efferent signal exits spinal cord, reaches synapse, signals postsynaptic motor neuron, postsynaptic motor neuron signals effect in somatic tissue.

Front 557

[ANS–2]

Describe the Viscero–Visceral Spinal Reflex

Back 557

Visceral sensory nerve is stimulated, afferent signal enters spinal cord, stimulates interneuron, interneuron stimulates presynaptic motor neuron, efferent signal exits spinal cord, reaches synapse, signals postsynaptic motor neuron, postsynaptic motor neuron signals effect in visceral tissue.

Front 558

[ANS–2]

What is the role of the Interneuron

Back 558

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Front 559

[ANS–2]

Describe spinal facilitation's relationship to somatic dysfunction

Back 559

Abnormal Reflexes:
Afferent Drive: Problem in tissue causes increased sensory input to spinal cord, which causes Facilitated Spinal Cord Segments: the properties of the other neurons in that segment change, accepting that signal as if it was meant for them, causing abnormal reflexes (somatic –> visceral or visceral –> somatic), which causes somatic dysfunction.

Front 560

[ANS–2]

What are the clinical aspects of facilitated segments

Back 560

Knowing which segments of nerves control which types of tissues allows a physician to trace the somatic dysfunction to its origin, and allow them to know which other body systems will be affected by an ailment and/or injury.

Front 561

Define pharmacokinetics

Back 561

What the body does to the drug.

e.g.
Distribution to peripheral tissues
excretion
site of action

Front 562

Define pharmacodynamics

Back 562

What the drug does to the body:
interaction with receptor
stimulus
effect

Front 563

[Microanatomy]
List the common Histological Dyes

Back 563

Hematoxylin
Eosin
Orcein
Silver
PAS – periodic acid–Schiff

Front 564

[Microanatomy]

What is the color will Hematoxylin show up as?

Back 564

blue <––> violet

Front 565

[Microanatomy]

What is the color will Eosin show up as?

Back 565

red <––> Pink

Front 566

[Microanatomy]
Define PAS

Back 566

Periodic acid–Schiff

Front 567

[Microanatomy]

What color does PAS show as?

Back 567

Magenta/Purple

Front 568

[Microanatomy]

What structures are dyed by Hematoxylin

Back 568

Nucleus
Basophilic regions of cytoplasm
Cartilage Matrix

Front 569

[Microanatomy]

What will Hematoxylin dye?

Acid or Base

Back 569

Basic structures

Front 570

[Microanatomy]

What will Eosin dye?

Acid or Base

Back 570

Acidic structures

Front 571

[microanatomy]

What is the target structure of Orcein's elastic stain?

Back 571

Brown: Elastic fibers

Front 572

[microanatomy]

slide: describe the appearance of the nucleus

Back 572

H&E will appear blue

Front 573

[microanatomy]

slide: describe the appearance of the nucleolus

Back 573

H&E will appear blue
appears w rRNA – protein formation
dark spot at center of the nucleus

Front 574

[microanatomy]

slide: describe the appearance of the nucleolus with golgi

Back 574

H&E will appear blue
dark spot at center of the nucleus
golgi: shipping new proteins out of the cell

Front 575

[microanatomy]

slide: describe the appearance of the nucleolus without golgi

Back 575

H&E will appear blue
dark spot at center of the nucleus
No golgi: proteins being made for use inside the cell

Front 576

[microanatomy]

slide: describe the appearance of the Golgi Apparatus

Back 576

H&E will appear as a clearing in the slide next to the nucleus

Front 577

[microanatomy]

slide: describe the appearance of the secretory vesicles

Back 577

H&E can be blue or pink

(only when very large)

Front 578

[microanatomy]

slide: describe the appearance of the cytoskeletal elements

Back 578

H&E will appear pink

Front 579

[microanatomy]

slide: describe the appearance of the Lipid Droplets

Back 579

H&E will appear as an empty hole

Front 580

[microanatomy]

List the various levels of structural organization in the human body

Back 580

chemical
cellular
tissue
organ
organ system
organism

Front 581

[microanatomy]

Describe the chemical structural level & provide examples

Back 581

histochemistry, cytochemistry

lipids, proteins

Front 582

[microanatomy]

Describe the cellular structural level & provide examples

Back 582

micro–anatomy
smallest living structure

fibrinoblast, keratinocyte, osteocyte, motor neuron, myocyte

Front 583

[microanatomy]

Describe the tissue structural level & provide examples

Back 583

microanatomy

Connective
Epithelial
Muscular
Nervous

Front 584

[microanatomy]

Describe the Organ structural level & provide examples

Back 584

gross anatomy

multiple tissue types working together

Front 585

[microanatomy]

Describe the Organ system structural level & provide examples

Back 585

gross anatomy

multiple organs

Digestive, skeletal, muscular, nervous, etc

Front 586

[microanatomy]

Describe the organism structural level & provide examples

Back 586

gross anatomy

multiple systems working together (osteopathic medicine)

Front 587

[microanatomy]

Describe the characteristics of the Epithelium tissue type [5 items]

Back 587

derived from all three germ layers
densely packed w little extracellular materials
always sits on a basement membrane
forms sheets that cover/line surfaces
form secretory glands

Front 588

[microanatomy]

Describe the characteristics of the Connective tissue type

Back 588

derived from mesoderm
mainly composed of extra–cellular elements, limited # of cells

Front 589

[microanatomy]

Describe the differences between Embryonic, Adult, and specialized connective tissue

Back 589

Embryonic: mesenchymal, mucous

Adult: connective tissue proper

Specialized: cartilage, bone, blood

Front 590

[microanatomy]

Describe the characteristics of the Muscle tissue type

Back 590

derived from mesoderm
contain contractile elements – myofilaments
possess many mitochondria – energy prod.
visibly longer than wide

Front 591

[microanatomy]

Describe the characteristics of the Nervous tissue type

Back 591

derived from ectoderm

Front 592

[microanatomy]

What is the name of the supporting cell for Neurons?

What is their function?

Back 592

Neuroglial cells

assist with metabolism & support the neurons

Front 593

[microanatomy]

What tissue type is derived from Ectoderm

Back 593

Nervous Tissue

Front 594

[microanatomy]

What tissue type is derived from mesoderm

Back 594

Connective & Muscle

Front 595

[microanatomy]

What tissue type has many mitochondria

Back 595

Muscle tissue

Front 596

[microanatomy]

Name the three germ layers

Back 596

ectoderm, mesoderm, and endoderm

Front 597

[microanatomy]

What tissue type is derived from all three germ layers?

Back 597

Epithelium

Front 598

[microanatomy]

How can you recognize a slide stained with Orcein?

Back 598

Brown tint

stains Elastic fibers

Front 599

[microanatomy]

What tissue does the Orcein's stain?

Back 599

Elastic fibers

Front 600

[microanatomy]

On slides with H&E, what component picks up the dark blue stain

Back 600

epithelium tissue

Front 601

[Action Potentials]

Describe the term Excitability

Back 601

ability of the cell to generate an action potential

able to send information electrically

Front 602

[Action Potentials]

list the types of cells that are excitable

Back 602

nerve cells
cardiac myocytes
skeletal muscle cells
some smooth muscle cells (e.g. GI)

Front 603

[Action Potentials]

Explain membrane potential involvement in driving insulin secretion

Back 603

high glucose inside Beta–islet cells in pancreas force an increased production of ATP
High [ATP] causes the membrane K+ channels to be blocked
this reduction in membrane K+ permeability causes the Em to more away from the NP for K+ and become more positive.
This depolarization opens Ca2+ channels, allowing Ca2+ into the cell which triggers the release of insulin

Front 604

[Action Potentials]

What channels are blocked and which are opened in the process of releasing insulin from the Beta–Islet cells in the pancreas

Back 604

K+ channels blocked due to high [ATP]
Ca2+ channels opened due to increased + Em

Front 605

[Action Potentials]

What type of gates close in the Beta Islet pancreatic cells when glucose concentration is low?

Back 605

low [ATP]
K+ channels unblocked,
Em moves to NP for K+
Em less positive = Ca2+ voltage–gated ion channels close
No insulin secretion

Front 606

[Action Potentials]

What types of channels control the release of Ca2+ in Beta–Islet pancreatic cells

Back 606

Ca2+ voltage–gated ion channels

Front 607

[Action Potentials]

Describe how the membrane potential changes during the action potential

Back 607

starting Em: ~ –70 mV
ending Em: ~+30 mV

net change: ~100 mV

Front 608

[Action Potentials]

Describe the 4 types of stimuli that can initiate an action potential

Back 608

electrical – cardiac
mechanical – sensory receptors
thermal
chemical – neurotransmitter

Front 609

[Action Potentials]

What are the stages of an action potential?

Back 609

Depolarizing phase
Plateau (if cardiac)
Repolarizing phase
Hyperpolarizing phase

Front 610

[Action Potentials]

Define Action potential

Back 610

transient reversal of membrane potential (Em)

Front 611

[Action Potentials]

Define threshold

Back 611

minimum membrane potential required to produce an action potential

Front 612

[Action Potentials]

Describe the depolarizing phase

Back 612

rapid upstroke that is a response to a stimulus that is sufficient (–50mV) to pass the threshold causing a change in the membrane potential (Em) from –70mV to +30mV

Front 613

[Action Potentials]

Describe the Action Potential Duration

Back 613

length of time between reaching threshold to the return to Resting Membrane Potential

Front 614

[Action Potentials]

Describe the repolarizing phase

Back 614

process by which the cell membrane returns from +30 mV to the Resting Membrane potential at ~ –70 mV

Front 615

[Action Potentials]

Describe the hyperpolarizing phase

Back 615

the process by which the cell, during the process of returning to Resting Membrane Potential becomes more negative via the influx of extra K+ ions for a short period before it returns to ~ –70 mV

Front 616

[Action Potentials]

Describe the differences in action potentials in various tissues

Back 616

Neuronal action potentials: 1–2 ms
ventricular action potentials: 300 ms

~300 times longer
partly due to plateau phase

Front 617

[Action Potentials]

What is one of the contributing factors in the differing lengths of repolarizations

Back 617

ion permeability

Front 618

[Action Potentials]

Define "all or none"

Back 618

All: threshold Em met, full action potential produced.

None: threshold Em not met, no membrane response

Front 619

[Action Potentials]

Describe the amplitude of the action potential

Back 619

constant amplitude regardless of the strength of the stimulus

Front 620

[Action Potentials]

Describe the behavior of the amplitude of an action potential as it is conducted along an excited cell membrane

Back 620

the action potential is conducted along an excited cell with an amplitude that does not change with distance from the initial trigger

Front 621

[Action Potentials]

Explain Refractoriness

Back 621

refers to the period in which another action potential cannot be triggered during an action potential

cellular need to recover before further action

Front 622

[Action Potentials]

Compare absolute vs. relative refractory periods

Back 622

Absolute: action potential is not possible regardless of the strength of the stimulus

Relative: the period during repolarization where the cell can trigger another action potential if the stimulus is large enough

Front 623

[Action Potentials]

Explain the membrane potential changes during an action potential

Back 623

Stimulus
membrane more permeable to Na+
drives Em to E(Na) ––> more positive –> depol.
membrane permeable to K+ increases
Em moves to Ek ––> more negative –> Repol.

Front 624

[Action Potentials]

explain the concept of driving force

Back 624

difference between the Nernst potential for the ions involved & the membrane potential

NP = E(ion) – Em
far from NP for specific ion, the driving force is large
near NP(ion), driving force is low

Front 625

[Action Potentials]

define conductance

Back 625

flow of ions across a membrane

conductance = 1 / Resistance

Front 626

[Action Potentials]

Explain the role of Na+ in the action potential

Back 626

depolarization is brought about by a rapid activation of a Na+ current

As the Em approaches the NP(Na+), the driving force decreases, Na+ influx slows near the peak of the action potential then decreases as the gates are inactivated

Front 627

[Action Potentials]

Explain the role of K+ in the action potential

Back 627

the increasingly positive Em during depolarization causes an outward flow of K+ ions until at the peak of the action potential the Na+ conductance is equal to the K+ conductance
Repolarization is brought by a reversal where the K+ conductance increases & the Na+ conductance decreases
ultimately returning the state to the original [ion] and Resting membrane potential

Front 628

[Action Potentials]

In which direction does Na+ flow during the action potential?

Back 628

Na+ current is Inward: depolarization

Front 629

[Action Potentials]

In which direction does K+ flow during the action potential?

Back 629

K+ current is outward

repolarization
hyperpolarization
refractoriness [absolute | relative]

Front 630

[Action Potentials]

Explain how the ion gradients are restored following an action potential

Back 630

Na/K ATPase

pumps out Na+ in exchange for K+

Front 631

[Action Potentials]

Describe how Na+ channels are opened during the action potential

Back 631

stimulus: small depolarization
Critical Mass: enough Na+ channels must open to cause an influx of Na+ in order to steadily change the Em more positive until threshold is reached ~ 50mV

positive feedback process

Front 632

[Action Potentials]

What is the Em needed to open Na+ channels

Back 632

approx. –50 mV

Front 633

[Action Potentials]

What determines the action potential threshold?

Back 633

whether there is enough depolarization to overcome a resting K+ efflux

Front 634

[Action Potentials]

Describe one of the causes of Hypercalcemia

Back 634

hyperparathyroidism

Front 635

[Action Potentials]

Describe the results of hypercalcemia on the action potential

Back 635

hypercalcemia caused by hyperparathyroidism results in a high extracellular [Ca2+] that shields the membrane voltage receptors, increasing the apparent threshold value needed to stimulate a depolarization

Front 636

[Action Potentials]

What physiological s/sx can show hypercalcemia

Back 636

muscle weakness

higher threshold due to membrane voltage receptor shielding results in a more difficult to achieve Action Potential

Front 637

[Action Potentials]

What is one of the causes for hypocalcemia?

Back 637

hypoparathyroidism

Front 638

[Action Potentials]

Describe the effect of hypocalcemia on the action potential

Back 638

low extracellular Ca2+ reduces the shielding effect Ca2+ has on the membrane receptors resulting in less obstruction of the voltage sensors = lower threshold to depolarize

Front 639

[Action Potentials]

What physiological s/sx can show hypocalcemia

Back 639

muscle twitching

lower threshold due to less shielding of the membrane voltage receptor results in a quicker depolarization

Front 640

[Action Potentials]

Explain what happens to the driving force for Na+ ions during the depolarization phase of the action potential

Back 640

the driving force for sodium ions decreases towards the peak of the action potential as the E(m) gets closer to E(Na)

net driving force is difference between NP for that ion & the E(m), nearer the Em is to E(Na) during upstroke, the smaller the driving force

Front 641

[Action Potentials]

Explain why the sodium ion current is brief during the action potential

Back 641

the driving force of sodium ion influx lessens near the peak of the action potential
Sodium ion channel inactivation stops sustained ion influx during the action potential

inactivation is kinetic action only

Front 642

[Action Potentials]


Describe what is meant by the Na+ channel inactivation

Back 642

Inactivation gate (IG) begins to close @–55 mV
activation gate (AG) begins to open @–50 mV
IG begins to close at the threshold point while the AG is open fully during the depolarization stage but closes slowly as the Em approaches E(Na).
purely a kinetic action

Front 643

[Action Potentials]

Be able to distinguish between Na+ inactivation, activation, closing

Back 643

Activation: Na+ channels open for depolarization due to stimulus
Inactivation: begin to close once threshold is met, limiting the influx of Na+ ions
closing: the Na+ channels are fully closed and inoperable during Membrane Resting Potential without a stimullus

Front 644

[Action Potentials]

Describe how Na+ channel activation & inactivation vary during the action potential

Back 644

@ resting: closed

Front 645

[Action Potentials]

Describe what causes Na+ channel inactivation & be able to predict hyperkalemia on Na+ channel inactivation

Back 645

Resting Membrane Potential (RMP): –70 mV
Inactivation gates close @ –55 mV
Hyperkalemia: raises RMP to ~ –55 mV
inactivation gates close
No Na+ ions allowed in regardless of stimulus
total blocking of signal

Front 646

[Action Potentials]

Explain how K+ channels are opened during the action potential

Back 646

K+ channels open through depolarization allowing a K+ efflux during repolarization causing a return to Resting Membrane Potential

Front 647

[Action Potentials]

Explain why the K+ current occurs after the Na+ current

Back 647

K+ current occurs after the Na+ current because the K+ channels open more slowly than the Na+ channels

slight difference @ which the channels open with K after Na+

Front 648

[Action Potential]

What are the two types of K+ channels that mediate K+ efflux

Back 648

Voltage–gated ion channel
inward rectifier channels

Front 649

[Action Potential]

Describe voltage–gated ion channels

Back 649

open at a set membrane voltage

Front 650

[Action Potential]

Describe inward rectifier channels

Back 650

open @ – Em
close @+ Em

account for RMP @ –88 mV due the allowance of potassium membrane permeability at resting membrane potential.
potassium always goes out

Front 651

[Action Potential]

Which gate is responsible for K+ permeability at rest?

Back 651

inward rectifier channels

Front 652

[Action Potential]

Which gate is responsible for repolarization

Back 652

Voltage–gated channels

Front 653

[Action Potential]

list the factors that determine action potential duration

Back 653

the magnitude of K+ currents:
larger = faster repolarization
smaller = slower repolarization

determined also by membrane permeability

Front 654

[Action Potential]

Explain the mechanisms of altered excitability

Back 654

Altered Depolarizing Duration in the presence of other depolarizing currents

Calcium current is triggered after a Na current, can create the plateau seen in the action potential, delays repolarization

Front 655

[Drug distribution & excretion]

describe the effects of ionization & lipid solubility on drug distribution

Back 655

Ionization: non–ionized forms of the drugs can cross the lipophilic membrane while the ionized forms cannot

Lipid solubility – lipophilic drugs can easily pass lipid membranes (think blood brain barrier & propofol)

Water soluble – escape slower, limited solubility & diffusion, more dependent on hydrostatic pressure

Front 656

[Drug distribution & excretion]

What percentage of blood flow is consumed by the brain?

Back 656

20% of blood flow

Front 657

[Drug distribution & excretion]


What percentage of blood–born energy is consumed by the brain?

Back 657

25% of the energy

Front 658

[Drug distribution & excretion]

Discuss the factors affecting the distribution of the drug into the CNS

Back 658

glial wrapping – highly lipid–soluble can rapidly reach the brain
ABC transporter – rapidly perceived toxic drugs out of the CNS back into systemic circulation
Tight Junctions – limit drug movement out of the capillaries
Basement membrane – when intact presents a barrier to the brain but is lipophilic

Front 659

[Drug distribution & excretion]

Describe the BBB – glial wrapping function

Back 659

allows highly lipid–soluble drugs to rapidly reach the brain but presents a barrier to other types

Front 660

[Drug distribution & excretion]

Describe the BBB – ABC transporters

Back 660

recognize & evacuate toxic drugs out of the CNS back into the capillaries

Front 661

[Drug distribution & excretion]

Describe the BBB – tight junctions

Back 661

prevent drug movement out of the capillaries between the cells into the brain.

other tissue types are more lenient and allow freer movement of drugs into the tissues

Front 662

[Drug distribution & excretion]

How does solubility determine a drugs entry into the CNS?

Back 662

In order to pass through the BBB, the drug must be highly lipid soluble

If the drug is polar or highly water soluble, it might need to be directly dosed into the CNS, bypassing the BBB

Front 663

[Drug distribution & excretion]

Describe possible drug related ramifications to disruptions in the integrity of the BBB

Back 663

any inflammation or injury can render the BBB leaky, resulting in the ability of drugs to enter into the CNS that normally could not or in dose changes quicker than normally allowed by the strict controlling BBB

Front 664

[Drug distribution & excretion]

Discuss the barrier characteristics of the placenta

Back 664

exhibits all modes of transfer of molecules
passive diffusion due to lipid solubility
most drugs can easily cross
drugs metabolized by the fetus can accumulate because of a change in lipid solubility by the metabolite (ionization)

Front 665

[Drug distribution & excretion]

What is the equation for the volume of distribution

Back 665

Vd = D / Cpo

Vd =apparent volume of distribution
D = drug dose
Cpo = plasma conc. of drug @ time = 0

Front 666

[Drug distribution & excretion]

Describe the meaning of a low Vd value

Back 666

a low Vd value relates to a low volume of distribution which relates to the concentration of the drug in the plasma at the time of the test. This means more of the drug is in the plasma vs. stored in the tissues

Front 667

[Drug distribution & excretion]

Describe the meaning of a high Vd value

Back 667

a high Vd value relates to a high volume of distribution which correlates to a low % of the drug in the plasma & a high % of the drug in the tissues or protein bound (e.g. somewhere else)

Front 668

[Drug distribution & excretion]

What is the estimated value of Total Body Water (TBW)

Back 668

~42 liters

Front 669

[Drug distribution & excretion]

How much of the estimated TBW is in the plasma?

Back 669

~3 liters

Front 670

[Drug distribution & excretion]

How much of the estimated TBW is in the Extracellular fluid

Back 670

~14 Liters

Front 671

[Drug distribution & excretion]

How much of the estimated TBW is in the Intracellular fluid

Back 671

~25 liters

Front 672

[Drug distribution & excretion]

What does it mean if the Vd exceeds TBW?

Back 672

that the drug is concentrated outside of the plasma

Front 673

[Drug distribution & excretion]

Describe the factors that contribute to unequal drug distribution in the body

Back 673

plasma binding
drug ionization
tissue perfusion

Front 674

[Drug distribution & excretion]

What are the primary plasma proteins involved in drug binding?

Back 674

Albumin

AAG – Alpha 1–acid glycoproteins

Front 675

[Drug distribution & excretion]

Describe the characteristics of Albumin

Back 675

binding is usually reversible

preference for acidic drugs

Front 676

[Drug distribution & excretion]

Describe the characteristics of AAG

Back 676

Alpha 1–acid glycoprotein

binding is usually reversible
preference for basic drugs

Front 677

[Drug distribution & excretion]

Describe the potential effects of plasma binding on the concentration of free drug in the blood, Vd, & elimination

Back 677

Increased protein binding will cause any bound drug to not be excreted except by active transport as well as
slow the drug movement out of the capillaries as the bound drug does not count towards the concentration gradient.

Front 678

[Drug distribution & excretion]

How will the number of plasma protein binding sites influence drug competition

Back 678

finite # of binding sites & amount of plasma proteins lead to a saturation & competition and potentially more free drug in the plasma, a higher gradient forcing more into the tissues

Front 679

[Drug distribution & excretion]

Describe protein binding site competition with regards to drugs that have a low therapeutic index

Back 679

if drug A with a low therapeutic index (higher dose = toxicity) is pushed off a protein in exchange for another then the plasma concentration of the drug A will increase, potentially risking toxicity

Front 680

[Drug distribution & excretion]

Describe the potential effects of hypoalbuminemia

Back 680

decreased plasma proteins will decrease the available protein binding sites potentially increasing the free drug, pushing more into the tissues, extending the duration of the drugs action

Front 681

[Drug distribution & excretion]

describe the distribution characteristics of thiopental/propofol & the termination

Back 681

these drugs pass quickly through the lipophilic BBB but also quickly into the Fat & muscle tissue. When the drug administration stops, the plasma concentration drops due to the increasing distribution to the muscles/fat, the drug leaves the brain. The drug concentration in the brain eventually reaches zero with the remaining amount in the muscles/fat but leaking out slow enough to stay subtherapeutic due to the speed of excretion

Front 682

[Drug distribution & excretion]

describe elimination

Back 682

removal of the drug from the body

metabolism + urinary excretion

Front 683

[Drug distribution & excretion]

Describe (CL) clearance

Back 683

quantitative measure of elimination (mL/min)

Front 684

[Drug distribution & excretion]

Describe Excretion

Back 684

process of drug elimination, primarily the kidney

Front 685

[Drug distribution & excretion]

List the methods of drug excretion

Back 685

Renal, biliary, salivary, mammary, skin, intestines, pulmonary excretion

Front 686

[Drug distribution & excretion]

Describe enterohepatic circulation

Back 686

drug metabolized once by the liver, returned to the GI tract, enzymes remove conjugate added by the liver, allowing the drug to return again into the blood

Front 687

[Drug distribution & excretion]

What will enterohepatic circulation do to a drugs half–life?

Back 687

potentially increase

Front 688

[Drug distribution & excretion]

Explain renal secretion via active transport

Back 688

active transporters (OAT, OCT) transport metabolites into the renal tubules from the peritubular capillaries

transporters are saturable

increase renal clearance

Front 689

[Drug distribution & excretion]

Explain a drugs reabsorption during the renal excretion process

Back 689

drug reabsorption greatly depends on urine pH (ionization/unionization)

pka > pH forces drug to unionized, lipophilic, reabsorbable.

decreases renal clearance

Front 690

[Drug distribution & excretion]

What will pH change with tubular reabsorption of drugs

Back 690

pKa > pH – unionized, less cleared, lower CL
pKa < pH – ionized, more cleared, higher CL

Front 691

[Drug distribution & excretion]

What is the GFR for a normal kidney?

Back 691

~120 mL/min

Front 692

[Drug distribution & excretion]

give the equation that finds the ratio of drug concentration on each side of a membrane

Back 692

Acid:
R1:2 = [1+10^(pH1–pKa)] / [1+10^(pH2–pKa)]

Base
R1:2 = [1+10^(pKa–pH1)] / [1+10^(pKa–pH2)]

Front 693

[Drug distribution & excretion]

What factors may influence the renal excretion of drugs?

Back 693

blood flow
pH / ionization
lipid–solubility
plasma protein binding
presence of other drugs
disease
age

Front 694

[Phamacokinetics]

Define "therapeutic window"

Back 694

a range of plasma concentrations between a minimal effective concentration (MEC) and a minimal toxic concentration (MTC).

Front 695

[Phamacokinetics]

Define MEC

Back 695

minimum effective concentration

Front 696

[Phamacokinetics]

Define MTC

Back 696

minimum toxic concentration

Front 697

[Phamacokinetics]

Define therapeutic drug monitoring

Back 697

Useful for: narrow therapeutic window drugs to ensure therapeutic effect & avoid toxicity
–evaluate pt compliance
–avoid irriversible toxicities
–evaluate changes in efectiveness r/t CL
–drugs that lack clearly defined endpoints

Front 698

[Phamacokinetics]

Describe Pharmacokinetic parameters

Back 698

Most important factors in dosing:

–Half–life
–Clearance
–Volume of distribution

Front 699

[Phamacokinetics]

Explain the concept of half–life

Back 699

Half–life = time required for 50% completion of a process
–index of: time–course for drug–elimination & drug–accumulation

Front 700

[Phamacokinetics]

Describe the relationship between half–life & first–order processes

Back 700

rate of elimination is directly PROPORTIONAL to drug CONCENTRATION

– %drug / minute

Front 701

[Phamacokinetics]

Describe the relationship between half–life & zero–order processes

Back 701

constant amount of drug is eliminated per unit of time regardless of drug concentration
– 10 mL / minute

Front 702

[Phamacokinetics]

How many half–lives does it take to complete a process?

Back 702

~5

Front 703

[Phamacokinetics]

Recall the maximum clearance rates for a drug eliminated by hepatic clearance, renal tubular secretion, & glomerular

Back 703

Liver blood flow (1500mL/min)
Renal blood flow (660mL/min)
Glomerular filtration rate (120–130mL/min)

Front 704

[Phamacokinetics]

Factors Affecting Drug Half–Life

Back 704

aging (decr. muscle mass, decr. distribution)

obesity (increase adipose mass, increase distribution)

Pathologic fluid (increase distribution)

Front 705

[Phamacokinetics]

Explain the concept of clearance & its relationship to drug dose & steady–state drug plasma concentration

Back 705

–apparent volume of fluid completely cleared of drug per unit of time (by metabolism and/or excretion)
–it’s an index of how well a drug is removed irreversibly from circulation
–quantitative measure of rate of removal of a substance from the body
CLsystemic = Renal + Liver + other

Front 706

[Phamacokinetics]

What can change a drugs clearance?

Back 706

P450 induction (increase CL)

P450 inhibition (decrease CL)
Cardiac failure (decrease CL)
Hepatic failure (decrease CL)
Renal failure (decrease CL)

Front 707

[Phamacokinetics]
Explain the concept of a loading dose

Back 707

a loading dose is the amount/concentration/dose of a drug that will force the drug into the tissues, quickly bringing the Vd into the therapeutic range.

Doseloading = Css * Vd
Doseloading = [Css * Vd ] / Foral

Front 708

[Phamacokinetics]

Explain the relationship between half–life, volume of distribution and clearance. Employ these relationships to predict the pharmacokinetics of a drug.

Back 708

t 1/2 = [ 0.693 * Vd ] / CL

(t1/2) is directly related to (VD)
(t1/2) is inversely related to clearance (CL)
(t1/2) is dependent on VD and CL

Front 709

[Phamacokinetics]

Given the appropriate data, calculate a new dose or a new dose interval in an individual with decreasing renal or hepatic function.

Back 709

New Dose = [CLdiseased / CLnormal] * Maint. Dose

New Dose Interval =

Front 710

[Phamacokinetics]

Discuss First–Order Kinetics

Back 710

constant fraction of drug in the body is eliminated per unit of time

–rate of elimination by metabolism or renal excretion is proportional to plasma drug concentration

–*half life, clearance, and volume of distribution are independent of dose, and clearance rate for any drug is constant

Front 711

[Phamacokinetics]

Discuss Zero–Order Kinetics

Back 711

–elimination rate is independent of drug concentration and constant per unit time
–a constant amount of drug is eliminated per unit time

–implies the clearance mechanism(s) is saturated or capacity limited (metabolism by enzymes or transporter

Front 712

[Phamacokinetics]

Explain what is meant by dose‑dependent kinetics and explain the clinical implications. Name three drugs eliminated by dose–dependent kinetics.

Back 712

Drug elimination is first order (fixed percentage of drug removed per unit time) at low concentrations; however, at high concentrations, enzymes for breaking down drug are saturated, and elimination becomes zero order (constant amount of drug removed per unit time)
–Clinical implications: A small increase in dosage can cause adverse effects.
–Phenytoin, Ethanol (reaches saturation quickly), aspirin

Front 713

[Intro to Viruses]

What are the basic structural organization of human viruses?

Back 713

– DNA or RNA genome (ss or ds)
– surrounding capsid composed of protein capsomeres
– naked or w lipid envelope
– shape: icosahedral, helical, complex

Front 714

[Intro to Viruses]

Describe some of the general characteristics of viruses (general, extra)

Back 714

– infrequently fatal
– majority of infections are asymptomatic
– obligate intracellular parasites
– no synthetic machinery
– only one type of genomic nucleic acid
– Not alive, complex mobile genetic elements

Front 715

[Intro to Viruses]

List Common DNA viruses

Back 715

HBV – Hepatitis B
HPV – human papilloma virus
Parvovirus B19
Adenovirus
Herpesviridae
Polyomaviruses

Front 716

[Intro to Viruses]

List common RNA viruses

Back 716

Influenza
RSV
Parainfluenza
Hepatitis A, C, D, E
Enteroviruses
Encephalitis viruses
Measles, Mumps, Rubella
Norwalk, Rotavirus
Virtually Everything else :P

Front 717

[Cultural Awareness]

Identify populations at risk for certain disease processes & cultural barriers

Back 717

Cancer screening & management Cardiovascular disease, diabetes, HIV infection/aids, Immunizations, Infant Mortality, Mental Health, Hepatitis, Syphilis, TB

Front 718

[Cultural Awareness]

Describe the six focus areas in which racial & ethnic minorities experience serious disparities in health access & outcomes

Back 718

Cancer screening & management
Cardiovascular Disease
Diabetes
HIV infection / Aids
Immunizations

Front 719

[Cultural Awareness]

Describe how cultural beliefs & behaviors can affect assessment of the patient & adherence to your treatment plan

Back 719

Communication
family relationships
diet & nutrition
health beliefs & practices

Front 720

[Intro to Viruses]

Describe the classifications of viruses

Back 720

By Nucleic Acid: RNA/DNA, segmented or non–segmented, linear or circular, SS or DS, +/– sense mRNA,
envelope
capsid
replication strategy

Front 721

[Intro to Viruses]

Describe the nature of viral replication

Back 721

–Attachment – viral attachment proteins connect w cellular receptors
–penetration/uncoating – retraction of receptors, capsid digestion
–biosynthesis – cellular synthetic processes redirected, become viral specific
–maturation – viral components assembled
–release – virus extracellular

Front 722

[Intro to Viruses]

Mechanisms of viral pathogenesis, including alternatives to cell distruction

Back 722

–cell destruction – lytic, inhibition of host DNA, RNA &/or protein synthesis; immune–mediated tissue damage
–transformation – cell transformation to oncogenic > cell division rate increases
–latent or persistent – ocult, virus becomes dormant, can later become re–activated
–cell fusion – to form multinucleated cells
–latent infection – chronic carrier, latent, or slow virus

Front 723

[Intro to Viruses]

Epidemiological considerations with respect to the transmission & dissemination of viral diseases

Back 723

Transmission, age, gender, ethnic background, country of origin, travel history, occupation, season, underlying medical conditions.

Front 724

[Intro to Viruses]

the role of the immune system in viral disease symptomatology & recovery from infection

Back 724

antigenic variation, some viruses encode receptors for various mediators of Immunity thus blocking their ability to interact with receptors on the virus, some viruses reduce expression of class I MHC proteins thus reducing ability of cytotoxic T–cells to kill the virus–infected cells, direct cell–to–cell propagation & attenuated virus

Front 725

[Fungal]

How many species of fungi are pathogenic?

How many are pathogenic to humans?

How many are common?

Back 725

over 100,000 species pathogenic

~175 cause disease in man

~30 common

Front 726

[Fungal]

Describe saprophytic

Back 726

lives on dead or decomposing matter, soil dwellers

Front 727

[Fungal]

Describe general characteristic differences between Fungi & bacteria

Back 727

Fungi vs. Bacteria

cell type - Eukaryotic vs. prokaryote

Cell interactions - uni/multicellular, able to differentiate vs. unicellular

Membrane - ergosterol, no cholesterol vs. no sterols

Cell Wall - peptidomanna, glycan, chitin, cellulose, chitosan vs. peptidoglycan, teichoic acid, lipopolysaccharide

Metabolism - heterotrophic only vs auto or heterotrophic

Oxygen Requirements - aerobic, anaerobic, facultative vs aerobic only

Reproduction - asexual (conidia), sexual (spores) vs asexual(fision)

Front 728

[Fungal]

Describe the differences between molds, yeasts, & dimorphisms

Back 728

molds: multicellular, long–tubelike extensions of the cell wall, grow naturally in soil environments @ 25 deg–C
Yeasts: unicellular, reproduce asexually by budding, grow @ body temperature ~37 deg–C
Dimorphisms: ability of a fungus to grow as a yeast or mold, depends on environmental condition

Front 729

[Fungal]

Describe septation

Back 729

crosswalls separating nuclei in a tube–like chain of fungi

Front 730

[Fungal]

Describe the fungal characteristics that pertain to Adherence

Back 730

some fungal species, particularly yeasts are able to colonized the mucosal surfaces of the oral, GI, & female genital tract

species of Candida that adhere best to epithelial cells are most often isolated from infections
– fungal "adhesins"

Front 731

[Fungal]

Describe the fungal characteristics that pertain to Invasion

Back 731

generally, non–invasive.

some proteases, lipases, ketatinases facilitate colonization, tissue invasion

Front 732

[Fungal]

Describe the fungal characteristics that pertain to Resistance to phagocytosis

Back 732

Most fungi are extremely susceptible to phagocytic killing. Pathogenic strains can often be shown to have increased anti–phagocytic properties

Histoplasma capsulatum in yeast form can multiply within macrophages

Front 733

[Fungal]

Describe the fungal characteristics that pertain to Tissue Injury

Back 733

No exotoxins, endotoxins. Fungal metabolic products do not injure tissues directly. Tissue injury is most often a result of inflammation & immune responses to fungal presence

Front 734

[Fungal]

Describe the important methods available to aid in the diagnosis of fungal infections

Back 734

KOH digestion & microscopy
10% KOH
Wood's lamp
culture, visualization, carbohydrate assimilation test, Ag/Ab detection, PCR

Front 735

[Fungal]

Clinical classification of medically relevant fungi

Back 735

Superficial – infections of the dead, superficial areas of the skin or hair shaft, no cellular response, cosmetic problems only
Cutaneous – living tissue is not invaded, organisms colonize the keratinized stratum corneum b/c of their keratinolytic ability > disease results from the host reaction to fungi metabolic products
subcutaneous – usually requires implantation, adaptation of organisms to tissue environment requires relatively long periods of time
systemic – agents that are inherently virulent and cause disease in healthy humans (acquired via respiratory tract) > requires significant exposure to fungal spores
opportunistic – in patients with impaired host defenses or alterations in normal bacterial flora

Front 736

[Parasites]

Define Definitive Host

Back 736

host in which the parasite reaches sexual maturity

Front 737

[Parasites]

Define Intermediate Host

Back 737

host in which asexual reproduction or larval development takes place

Front 738

[Parasites]

Define Vector

Back 738

transmitting agent, usually arthropod

Front 739

[Parasites]

Explain the difference between trophozoite & a cyst

Back 739

Trophozoite – metabolically active & motile stage of many protozoan parasites

Cyst – generally smaller & has an outer protective layer to enhance survival in the environment

Front 740

[Parasites]

World–wide, how prevalent are infections caused by parasites

Back 740

Toxoplasmosis = 1–2 billion
Ascariasis = 1 billion
Malaria = 200–300 million
Schistosomiasis = 200–300 million
Giardiasis = 200 million
Trypanosomiasis = 15–20 millions

Front 741

[Parasites]

Describe the probable roles of IgE antibody & eosinophils in combating parasitic infections

Back 741

IgE coats the parasite

Eosinophils will target, attack, & eat the parasite

Front 742

[Parasites]

Describe clinical presentation & basic characteristics of Giardia infection

Back 742

–most common cause of parasitic gastroenteritis
–infection from ingestion of cysts
–average incubation period of 10 days
–attaches to intestinal mucosa & causes shortening of the villi, inflammation of crypts & lamina propria
– diarrhea due to malabsorption
–immune response
–treatment – metronidazole

Front 743

[Parasites]

Case Study!

Back 743

–Your patient is a 5–year–old female accompanied by her mother.
–The chief complaint is nausea, vomiting, and foul–smelling diarrhea for several days.
–The mother states that the watery stool looks greasy. The child has had little appetite.
–The patient attends a pre–school this year, and had been in day care since she was 2–years–old.
–Physical exam reveals moderate epigastric tenderness. The child is slightly below normal weight.

Front 744

[DS – Intro to Antimicrobial Pharm]

Describe bacteriostatic

Back 744

inhibits/stops growth & reproduction of bacteria but do not kill them

works with the immune system to remove organisms from the body

*tetracycline

Front 745

[DS – Intro to Antimicrobial Pharm]

Describe bactericidal

Back 745

kill bacteria
– interference w a process essential for life

–useful with endocarditis, meningitis, & neutropenic cancer patients


*PCN

Front 746

[DS – Intro to Antimicrobial Pharm]

Describe Time–dependent killing

Back 746

killing effect is directly proportional to the amount of time the drug concentration at the site of infection is above the MIC of the organism

Front 747

[DS – Intro to Antimicrobial Pharm]

Define MIC

Back 747

minimum inhibitory concentration

Front 748

[DS – Intro to Antimicrobial Pharm]

Are beta–lactam antibiotics time or concentration dependent?

Back 748

time–dependent killers

Front 749

[DS – Intro to Antimicrobial Pharm]

Describe concentration dependent antibiotics

Back 749

bacterial kill increases with increasing levels of the drug

concentration is not important

Aminoglycosides & fluoroquinlones

Front 750

[DS – Intro to Antimicrobial Pharm]

Describe selective toxicity

Back 750

adversely affect only type of cell & spare normal human cells

Front 751

[DS – Intro to Antimicrobial Pharm]

What are the 5 MoA of antibiotics

Back 751

1. inhibition of cell wall synthesis
2. Disruption of cell membrane function
3. Inhibitors of protein synthesis
4. Inhibition of Nucleic Acid synthesis
5. Inhibition of synthesis of Essential Metabolites

Front 752

[DS – Intro to Antimicrobial Pharm]

What antibiotics inhibit cell wall synthesis

Names & targets

Back 752

b–lactam – targets TG
Vancomycin – targets TP
Bacitracin – stop dephosphorylation of bactoprenol
Cycloserine – stop the addition of d–ala
fosfomycin – inhibit nam

Front 753

[DS – Intro to Antimicrobial Pharm]

Beta–lactam antibiotics: names

Back 753

PCN
Cephalosporins
Carbapenem
Monobactams

Front 754

[DS – Intro to Antimicrobial Pharm]

List the types of PCN

Back 754

Natural PCN – PCN G
Extended–Spectrum PCN – amoxicillin

Front 755

[DS – Intro to Antimicrobial Pharm]

List the generations & specific names of the Cephalosporins

Back 755

1 – cephalexin
2 – cefoxitin
3 – ceftriaxone
4 – cefepime

Front 756

[DS – Intro to Antimicrobial Pharm]

What are the benefits of the higher generation cephalosporins

Back 756

– increased ability to cross the BBB
– increased resistance to b–lactamases
– increased activity vs. gram negative

Front 757

[DS – Intro to Antimicrobial Pharm]

Carbapenem: names

Back 757

Imipenem

Front 758

[DS – Intro to Antimicrobial Pharm]

Monobactams: names

Back 758

Aztreonam

Front 759

[DS – Intro to Antimicrobial Pharm]

Describe the Beta–lactam ring, uses, makeup, & limits

Back 759

–consists of b–lactam bonds
–can be cleaved by b–lactamases
– inhibits PBPs inducing cell wall bursting

Front 760

[DS – Intro to Antimicrobial Pharm]

Names of antibiotics that disrupt cell membrane function

Back 760

–Cidal & concentration–dependent

Amphotericin
Ketoconazole
Polymyxin
Daptomycin

Amy Keeps Pooping D***it

Front 761

[DS – Intro to Antimicrobial Pharm]

Target & Names of the antibiotics that inhibit the synthesis of essential metabolites

Back 761

Target: mostly folic acid

Trimethoprim
sulfonamides > sulfamethoxazole

Front 762

[DS – Intro to Antimicrobial Pharm]

Target & names of antibiotics that affect nucleic acid metabolism

Back 762

Bactericidal –
DNA Gyrase inhibitor
* Fluoroquinolones – Ciproflaxin
RNA Polymerase
* Rifampin

Front 763

[DS – Intro to Antimicrobial Pharm]

Names of antibiotics that inhibit bacterial protein synthesis

Back 763

Aminoglycosides – Gentamycin ******
Tetracyclines – Doxycyclin
Macrolides – Erythromycin
Chloramphenicol
Clindamycin
Mupirocin
Streptogramins

Front 764

[DS – Intro to Antimicrobial Pharm]

Attributes of antibiotics that inhibit bacterial protein synthesis

Back 764

Bacteriostatic (except AG=cidal)

target 30s/50s

Front 765

[DS – Intro to Antimicrobial Pharm]

resistance factors for antibiotics that inhibit bacterial protein synthesis

Back 765

Microbial Enzymes > AGs, alter enzyme, reduce binding
Ribosome protection > tetracyclines & Macrolides= compete for or alter binding site
Efflux pumps > Macrolides & Tetracyclines
Update reduced > Cephalosporins
Natural Selection –

Front 766

[DS – Intro to Antimicrobial Pharm]

Define PBPs

Back 766

peptidoglycan binding proteins

Front 767

[DS – Microbial Genetics & Drug Res]

Discuss the misuses of antibiotics

Back 767

–Given when they are not needed (according to CDC up to 50% of antimicrobial use in hospitals are inappropriate) (Outpatient prescriptions are often unnecessary particularly when treating URI)
–Continued when they are no longer necessary
–Given at the wrong dosage
–Wrong antibiotic is used to treat the infection
–In many countries antibiotics can be purchased over the counter which leads to even more indiscriminate use
– Antibiotic use and misuse has led to incr. in selective pressure

Front 768

[DS – Microbial Genetics & Drug Res]

List the ways bacteria can resist antibiotics

Back 768

–Degrade or alter antibiotic (splitting of the Beta–Lactam ring) (Modify aminoglycosides)
–Efflux Pump (Tetracycline) (Macrolides)
–Uptake reduced (Cephalosporins)
–Overproduction of target metabolic bypass (Sulfonamides) (Timethoprim) – produces enzymes that breakdown the drug
– Alteration of target (Penicillin binding proteins “transpeptidases”: Beta–Lactams) (50S ribosomal subunit modified so that it still functions but macrolide can no longer bind) (DNA gyrase and topoisomerase interferes with fluoroquinolones)
– Pathogens develop resistance through natural selection (When bacteria are exposed to an antibiotic, more susceptible organisms will be killed leaving behind the more resistant bacteria to grow and multiply)

Front 769

[DS – Microbial Genetics & Drug Res]

Explain Spontaneous Mutations

Back 769

Despite effective repair systems, mistakes in normal replication occur about 1 per 10^6 & 10^9 cells

Front 770

[DS – Microbial Genetics & Drug Res]

Explain Induced Mutations

Back 770

caused by mutagens

Front 771

[DS – Microbial Genetics & Drug Res]

Explain Mutations resulting in antibiotic resistance

Back 771

May arise prior to or in the absence of selective pressure; most antibiotic resistance occurs by point mutations

Front 772

[DS – Microbial Genetics & Drug Res]

Explain point mutations:

Back 772

substitution, deletion, or change of nucleotide base sequence

Front 773

[DS – Microbial Genetics & Drug Res]

List three methods of intracellular DNA transfer

Back 773

Transformation
Transduction
Conjugation

Front 774

[DS – Microbial Genetics & Drug Res]

Explain Transformation

Back 774

direct uptake & incorporation of exogenous genetic material (exogenous DNA) from its surrounding & taken up through the cell membranes

Front 775

[DS – Microbial Genetics & Drug Res]

Explain Transduction

Back 775

transfer of genetic material from one bacterium to another by means of a bacteriophage (virus)

Front 776

[DS – Microbial Genetics & Drug Res]

Explain Conjugation

********

Back 776

transfer of DNA between bacterial cells by direct cell to cell contact (sex pilus)

F+ to F– only = unidirectional

Front 777

[DS – Microbial Genetics & Drug Res]

Explain the importance of R–plasmids

Back 777

Conjugative Resistance R–plasmids

found in many gram–negative bacteria
Contain the "F" factor (replication & transfer Gene)

Contains resistant genes often coding for multiple resistances

Front 778

[DS – Microbial Genetics & Drug Res]

Explain Transposons

Back 778

Mobile Genetic Elements
–can move from place to place on the chromosomes & into/out of the plasmids
–carry both insertion sequences plus other genes often those coding for resistances
–if transposons insert into a functional gene, it will be destroyed = cell death
transposons are biological mutagens

Front 779

[Drug Metabolism]

4. Discuss the major pathways of Drug metabolism:

Phase I only

Back 779

–add group to molecule (OH, SH, COOH, NH2)
–alters drug to a more polar metabolite
– more water soluble

Front 780

[Drug Metabolism]

4. Discuss the major pathways of Drug metabolism:

Phase II only

Back 780

–conjugation: endogenous substrate added to the drug by acetylation, sulfonation, or glucuronidation
–usually forms a highly polar, inactive metabolite that is excreted via kidneys
–Phase 1 addition prep's the molecule for Phase 2 addition
– large change in structure, biological activity, LS, etc

Front 781

[Drug Metabolism]

5. Recall the basic types of Phase I metabolism

Back 781

Oxidations

Reductions

Hydrolysis

goal: add or change the molecule to make it more polar thus less LS & more water–soluble

Front 782

[Drug Metabolism]

6. What are the top three CYP450s involved in drug metabolism in humans?

Back 782

CYP3A4

CYP2d6

CYP2c9

Front 783

[Drug Metabolism]

6. What food product inhibits intestinal CYP3A4

Back 783

Grapefruit juice

Front 784

[Drug Metabolism]

6. Which transporter works in cooperation with CYP450s to limit systemic exposure to drugs

Back 784

P–glycoproteins

Front 785

[Drug Metabolism]

7. Recall the different types of Phase II metabolisms & discuss its role in drug elimination & excretion

Back 785

Glucuronidation, Acetylation, Sulfation
– attaches an endogenous substrate that usually increases the polarity, inactivates it, and makes it less LS

Front 786

[Drug Metabolism]

8. Predict potential effects of a drug acting as an inducer or inhibitor of an enzyme that is responsible for the metabolism of another drug.

Back 786

Induction: cause an increase in the expression of an enzyme, increasing the speed at which a SPECIFIC drug is metabolized and removed from the body.

Inhibitor: cause the suppression of the enzymes that metabolize a SPECIFIC drug, increasing the time the drug stays in the body.

Front 787

[Drug Metabolism]

consequences of drug metabolism

Back 787

1. less lipid soluble, now kidney can excrete it
2. less stored in fat
3. more water soluble
4. more ionized at physiological pH
5. less bound to plasma proteins
6. less able to penetrate cell membranes
7. more readily excreted in urine by the kidneys

Front 788

[Drug Metabolism]

general characteristics of drug metabolites

Back 788

1. more water soluble
2. more easily excreted by kidneys
3. frequently inactivates a drug (inactivated by liver)
4. metabolism MAY activate a drug (bioactivation)
5. Prodrug concept à prodrug (precursor) is not active, metabolite is active may have no, <, =, or > pharmacological activity than parent drug can sometimes be toxic

Front 789

[Drug Metabolism]

Explain the functional importance of drug metabolism as it relates to the elimination and excretion of drugs

Back 789

1. Biotransformation makes drugs more lipid soluble, more water soluble, more ionized, less bound to plasma proteins, etc (see above). This allows the metabolites to be more easily eliminated and excreted through the kidneys.
2. Significance of metabolism: Termination of a drug's pharmacological effect(s) & enhancement of its excretion. This allows intermediates to become polar, non–toxic, metabolites which can then be excreted.

Front 790

[Drug Metabolism]

Discuss the role of metabolism in acetaminophen toxicity

Back 790

Metabolism allows acetaminophen to be turned into non–toxic metabolites. The major pathway (95%, phase 2) uses glucoronidation & sulfation to create inactive, non–toxic metabolites, which can then be excreted in the urine. The minor pathway (5%, phase creates reactive toxic intermediates, but these can be neutralized into non–toxic metabolites through glutathione conjugation.

Front 791

[Drug Metabolism]

Describe the implications of an intermediary drug metabolite being more reactive than the parent compound

Back 791

1. the reactive toxic intermediates are actually more reactive than the parent compound (acetaminophen) so the MUST be converted to non–toxic metabolites in order for them to be excreted
2. glutathione conjugation converts the toxic metabolites to the non–toxic form
3. happens when there is more drug present than the metabolic enzymes can handle
4. enzymes become saturated in the major pathway (phase 2) and so excess drug is metabolized by the minor pathway (CYP450 enzyme)
5. in this case the glutathione becomes depleted à drug cannot be converted to non–toxic metabolite so the toxic metabolic becomes reactive à hepatotoxicity cellular necrosis

Front 792

[Drug Metabolism]

Discuss Phase I of drug metabolism

Back 792

1. adds hydroxyl (OH) or some other group (SH, COOH, NH2)
2. more polar means more H2O soluble
3. if polar enough, may be excreted
4. many phase I products not eliminated rapidly
5. metabolites may be inactive
6. over ½ of all drugs are metabolized by a group of P450 enzymes
7. usually prepares a molecule for phase II
8. usually produces minor changes in chemical structure, LS, and biological activity

Front 793

[Drug Metabolism]

Discuss Phase II of drug metabolism

Back 793

1. conjugation an adds "something" to the drug; big water soluble drugs
2. glucuronic acid, sulfate, glutathione, acetyl groups
3. usually forms a highly polar, inactive metabolite that is renal excreted
4. Phase I metabolite may be needed as a substrate for phase II metabolism
5. Glucuronidation – hooks glucuronite groups; most important
6. Acetylation
7. Glutathione conjugation
8. Glycine conjugation
9. Methylation
10. produce large changes in structure, biological activity and LS (big decreases)

Front 794

[Intro to Metabolism]

2. Describe the relationship between oxygen consumption & resting metabolic rate

Back 794

–the amount of oxygen intake can be used to estimate metabolic rate
–measurement of the amount of energy needed to maintain normal function
–because energy prod. requires O2, oxygen consumption can be measured & used to estimate RMR/BMR
higher intake = higher Metabolic Rate

Front 795

[Intro to Metabolism]

List the 3 phases in aerobic respiration

Back 795

Phase 1: oxide fuels

Phase 2: Make ATP

Phase 3: Use ATP

Front 796

[Intro to Metabolism]

Describe Phase 1 of aerobic respirations

Back 796

turn everything into acetyl CoA
Oxidize acetyl CoA in the TCA
fuels oxidized to CO2
NAD & FAD reduced to NADH / FADH2

Front 797

[Intro to Metabolism]

Describe Phase 2 of Aerobic Respiration

Back 797

Oxidative Phosphorylation
– make ATP through the electron transport chain
– uses oxygen as the final electron acceptor
– FADH2 & NADH are re–oxidized back to
FAD / NAD

Front 798

[Intro to Metabolism]

Describe Phase 3 of Aerobic Respiration

Back 798

Using ATP will generate ADP

cycle starts over

Front 799

[Intro to Metabolism]

1. Cellular carriers of Energy

Back 799

ATP – Adenine Triphosphate
GTP – Guanine Triphosphate
CTP – Creatine Triphosphate
UTP – Uridine triphosphate

Front 800

[Intro to Metabolism]

Glycolysis

Explain why the pathway exists & in which tissues it occurs

Back 800

Pathway: glucose ––> pyruvate + 2 ATP

Where:
RBCs only use glucose for energy
– (no mitochondria)
Brain doesn't absorb lactate (unless forced) so will always use glucose & ketones
– (if forced w extended fasting)

Front 801

[Intro to Metabolism]

TCA Cycle

Explain why the pathway exists & in which tissues it occurs

Back 801

(aerobic respiration phase 1)

pathway: acetyl CoA converted to CO2, H2O, ATP

Front 802

[Intro to Metabolism]

Oxidative phosphorylation

Explain why the pathway exists & in which tissues it occurs

Back 802

(aerobic respiration phase 2)

pathway: makes ATP through the electron transport chain, FADH2 & NADH donate electrons to the process
– depends on oxygen

Where: inside the mitochondria

Front 803

[Intro to Metabolism]

Fatty Acid synthesis

Explain why the pathway exists & in which tissues it occurs

Back 803

pathway: acetyl CoA –––> Fatty acids
– NADPH oxidized to NADP
– pentose phosphate pathway reduces NADP to NADPH

Where: Liver

Front 804

[Intro to Metabolism]

Triglyceride synthesis

Explain why the pathway exists & in which tissues it occurs

Back 804

pathway: fatty acids ––> triglycerides

where: made in the liver, transported to the adipose via lipoproteins
– Dietary triglycerides are transported via
chylomicrons

Front 805

[Intro to Metabolism]

Lipolysis

Explain why the pathway exists & in which tissues it occurs

Back 805

pathway: triacylglycerols broken down into fatty acids & glycerols
– glycerol goes right into gluconeogenesis

Where: adipose tissues

Front 806

[Intro to Metabolism]

Beta–oxidation

Explain why the pathway exists & in which tissues it occurs

Back 806

pathway: fatty acids (oxidized) ––> acetyl CoA
– NADH & FADH2 are generated

where: muscle, liver, & "other tissues"

Front 807

[Intro to Metabolism]

Gluconeogenesis

Explain why the pathway exists & in which tissues it occurs

Back 807

pathway: converting lactate, certain amino acids, or glycerol into glucose
– glycerol comes straight from lypolysis
where:
– liver (during fasting state)
– kidneys (slight)

Front 808

[Intro to Metabolism]


6. Explain the difference between aerobic & anaerobic metabolism

Back 808

Aerobic metabolism: oxygen is available as the final electron acceptor
– acetyl CoA is used in the TCA cycle to produce ATP, CO2, H2O

Anaerobic metabolism: occurs where no O2 available. Pyruvate is converted to lactate
– cannot generate acetyl CoA, thus no TCA (no oxidative phosphorylation)
– primary metabolism of RBCs

Front 809

[Intro to Metabolism]

6. Describe the uses of lactate in the fed & fasted states

Back 809

Fasting: lactate is the product of glycolysis in RBC's & exercising muscles

Fed: RBCs primary metabolism is glycolysis whose result is lactate.

Front 810

[Intro to Metabolism]

7. Indicate the metabolic process that will provide the cell with the energy during Fed & Fasted states.

Red Blood Cells

Back 810

Fed: glycolysis

Fasted: glycolysis still
– only method available to RBCs

Front 811

[Intro to Metabolism]

7. Indicate the metabolic process that will provide the cell with the energy during Fed & Fasted states.

Adipose Cells

Back 811

Fed: glycolysis

Fasted: lipolysis

Front 812

[Intro to Metabolism]

7. Indicate the metabolic process that will provide the cell with the energy during Fed & Fasted states.

Brain Cells

Back 812

Fed: glycolysis, TCA, Oxydative Phosphorylation

Fasted: if extended: ketogenesis + whatever stores of glucose can be produced

Front 813

[Intro to Metabolism]

7. Indicate the metabolic process that will provide the cell with the energy during Fed & Fasted states.

Muscle Cells

Back 813

Fed: glycolysis (glucose = lactate)

Fasted: glycogenolysis + ketones

Front 814

[Intro to Metabolism]

7. Indicate the metabolic process that will provide the cell with the energy during Fed & Fasted states.

Liver Cells

Back 814

Fed: glycolysis

Fasted: B–oxidation, Amino Acids

Front 815

[Intro to Metabolism]

8. Explain how the liver works with the other systems to maintain homeostatic blood glucose during a prolonged fast.

Back 815

– continues to convert fatty acids to ketone bodies
– since the brain continues to use a limited amount of glucose, the liver needs to produce less glucose per hour during prolonged fasting than during shorter periods of fasting.
– because the stores of glycogen in the liver are depleted by ~30 hours of fasting, gluconeogenesis is the only process by which the liver can supply glucose to the blood

Front 816

[Intro to Metabolism]

8. Explain how the Adipose Tissue works with the other systems to maintain homeostatic blood glucose during a prolonged fast.

Back 816

– as blood insulin decreases or blood glucagon increases, adipose triacylglycerols are mobilized by lipolysis
– most fatty acids cannot provide carbon for gluconeogenesis ––> fatty acids serve as a fuel for muscle, kidney, & most other tissues and are oxidized to acetyl CoA & subsequently to CO2, H2O in the TCA cycle
– supplies the blood with its major source of fuel via the glycerol portion of the triglyceride

Front 817

[Intro to Metabolism]

8. Explain how the RBCs works with the other systems to maintain homeostatic blood glucose during a prolonged fast.

Back 817

transfer lactate to the blood so that it can be reconverted back to glucose

Front 818

[Intro to Metabolism]

8. Explain how the Muscle works with the other systems to maintain homeostatic blood glucose during a prolonged fast.

Back 818

– breakdown proteins to amino acids = transferred back to the liver to produce glucose
– acetyl CoA used in TCA cycle to generate ATP, CO2, H2O
– muscle use of ketones decreases
– brain use of ketones increases
– brain use of glucose decreases
– liver gluconeogenesis decreases
– muscle protein degradation decreases
– liver production of urea decreases

Front 819

[DS – Metabolism]

1. What metabolic processes is insulin going to stimulate?

Back 819

Insulin: increases the breakdown of glucose when blood glucose levels are high

Stimulates: glycolysis, TCA cycle, Oxidative Phosphorylation, Triglyceride Synthesis, Glycogenesis, Fatty Acid Synthesis

Front 820

[DS – Metabolism]

1. What metabolic processes is glucagon going to stimulate?

Back 820

Glucagon: increases during the fasted state, signals the liver to utilize shared carbohydrates to release glucose into circulation. Signals adipose to degrade triacylglycerols into fatty acids(energy via b–oxydation) & glycerol(gluconeogenesis)
Stimulates: TCA Cycle, Oxidative Phosphorylation, Lipolysis, Beta–oxidation, gluconeogenesis, glycogenolysis

Front 821

[DS – Metabolism]

2. Name the primary regulator of insulin

Back 821

Pancreas in response to a high–carbohydrate meal / serum glucose concentration

Front 822

[DS – Metabolism]

2. Describe the mechanism through which the release of insulin occurs

Back 822

–insulin is rapidly removed from circulation & degraded by the liver, so blood insulin levels decrease rapidly once the rate of secretion slows.
–neural signals from ANS help to coordinate insulin release with the secretory signals initiated by the ingestion of fuels
– certain amino acids can stimulate insulin secretion
– gut hormones in response to food intake can aid in onset of insulin release
–epinephrine decreases the release of insulin

Front 823

[DS – Metabolism]

2. Name the primary regulator of glucagon

Back 823

suppressed by insulin & glucose

Front 824

[DS – Metabolism]

2. Describe the mechanism through which the release of glucagon occurs

Back 824

– certain hormones stimulate glucagon secretion (cortisol & epinephrine)

– many amino acids also stimulate glucagon release

Front 825

[DS – Metabolism]

4. Describe the effects of epinephrine on energy metabolism

[big picture]

Back 825

–mobilize fuels during acute stress
–stimulate glucose production from glycogen

Front 826

[DS – Metabolism]

4. Describe the effects of cortisol on energy metabolism

[big picture]

Back 826

– provides for changing requirements over the long term
–stimulates glucagon secretion
–stimulates amino acid mobilization from muscle protein
–stimulates gluconeogensis
–stimulates fatty acid release from adipose tissues

Front 827

[DS – Metabolism]

5. What class of receptor/signal transduction pathway does Glucagon exert its effect.

Back 827

* binds to GPCRs to stimulate synthesis of cAMP

–activates glucose production from glycogen in the liver but not in the skeletal muscles
–glucagon–stimulated phosphorylation of enzymes simultaneously activates gl;ycogen degradation, inhibits glycogen synthesis, & inhibits glycolysis in the liver

Front 828

[DS – Metabolism]

5. What class of receptor/signal transduction pathway does Insulin exert its effect.

Back 828

* uses tyrosine–kinase receptors for signal transduction

–reverses glucagon–stimulated phosphorylation
–stimulates the phosphorylation of several enzymes
–induces & represses the synthesis of specific enzymes
–acts as a growth factor & has general stimulatory effects on protein synthesis
–stimulates glucose & amino acid transport into cells

Front 829

[DS – Metabolism]

5. What class of receptor/signal transduction pathway does Cortisol exert its effect.

Back 829

* bind intracellular receptors or binding proteins

– move to the nucleus & interact with chromatin
– change the rate of gene transcription on the target cell
–stress hormone

Front 830

[DS – Metabolism]

5. What class of receptor/signal transduction pathway does NE/Epi exert its effect.

Back 830

* act as neurotransmitter or hormone

– bind to adrenergic receptors
– work through the cAMP system (GPCRs)

Front 831

[DS – Metabolism]

6. Which hormone would be secreted during:

An Overnight Fast

Back 831

Decreased insulin

increased glucagon

Front 832

[DS – Metabolism]

6. Which hormone would be secreted during:

Prolonged Starvation

Back 832

Decreased insulin

increased glucagon

Front 833

[DS – Metabolism]

6. Which hormone would be secreted during:

Exercise

Back 833

increased glucagon

Front 834

[DS – Metabolism]

6. Which hormone would be secreted during:

Surgery, trauma, or severe infection

Back 834

increased Cortisol

Front 835

[DS – Metabolism]

6. Which hormone would be secreted during:

A carbohydrate rich meal

Back 835

increased insulin

Front 836

[DS – Metabolism]

6. Which hormone would be secreted during:

A protein rich meal

Back 836

increased insulin

Front 837

[DS – Metabolism]

6. Which hormone would be secreted during:

a "fight or flight" situation

Back 837

epinephrine

Front 838

[Intro to Metabolism]

What is the main anabolic hormone?

Back 838

Insulin

Front 839

[Intro to Metabolism]

Which is considered the "fasted state" hormone?

Back 839

Glucagon

Front 840

[Intro to Metabolism]

How many days (about) before the brain begins to utilize Ketones & whatever glucose is available?

Back 840

~4 days

Front 841

[Intro to Metabolism]

When will the liver produce Ketones?

Back 841

only when fasted & only when there is excess acetyl CoA

Front 842

[Intro to Metabolism]

This is an important source of Amino Acids during the fasted state

Back 842

Skeletal Muscle

Front 843

[Intro to Metabolism]

What systems can export glucose into the blood stream?

Back 843

Liver [& kidney]

Front 844

[Intro to Metabolism]

The pathway that reduces NADP back to NADPH

Back 844

Pentose Phosphate Pathway

Front 845

[Intro to Metabolism]

Are important for energy storage & the transport of dietary fat

Back 845

Triglycerides

Front 846

[Intro to Metabolism]

What tissues can make glycogen?

Back 846

liver
muscles
* all tissues in very small quantities

Front 847

[Intro to Metabolism]

What tissues can make fatty acids

Back 847

Liver
* a little in the adipose tissue

Front 848

[Intro to Metabolism]

What tissues are only capable of using glucose

Back 848

Red Blood Cells

Brain (until starvation, then Ketones + glucose)

Front 849

[Intro to Metabolism]

Oxidative phosphorylation requires these:

Back 849

Mitochondria & Oxygen

Front 850

[Intro to Metabolism]

The end result of metabolism without oxygen

Back 850

Lactate

Front 851

[Intro to Metabolism]

Glucose can be metabolized into:

Back 851

glucose–6–p

Front 852

[Intro to Metabolism]

Glucose–6–p can be metabolized into:

Back 852

Glucose
Glycogen (glycogenesis)
Pyruvate (glycolysis)
Reduces NADPH via PPP

Front 853

[Intro to Metabolism]

What is the function of the pentose phosphate pathway

Back 853

recycle NADPH

Front 854

[Intro to Metabolism]

Glycogen can be metabolized into:

Back 854

glucose–6–p (glycogenolysis)

Front 855

[Intro to Metabolism]

Pyruvate can be metabolized into:

Back 855

Glucose–6–p (gluconeogenesis)
Lactate
Acetyl CoA

Front 856

[Intro to Metabolism]

Lactate can be metabolized into:

Back 856

Pyruvate

Front 857

[Intro to Metabolism]

Amino Acids can be metabolized into:

Back 857

Pyruvate

Acetyl CoA

Front 858

[Intro to Metabolism]

Ethanol can be metabolized into:

Back 858

Acetyl CoA

Front 859

[Intro to Metabolism]

Triacylglycerols can be metabolized into:

Back 859

Fatty Acids [lipolysis] (+ glycerols)

Front 860

[Intro to Metabolism]

Fatty Acids can be metabolized into:

Back 860

Triacylglycerols (synthesis w glycerol)

Acetyl CoA (B–Oxidation)

Front 861

[Intro to Metabolism]

Ketones can be metabolized into:

Back 861

Acetyl CoA

Front 862

[Intro to Metabolism]

Acetyl CoA can be metabolized into:

Back 862

Fatty Acids (Fatty Acid Synthesis)

Ketones

utilized by TCA cycle to Oxidative phosphorylation

Front 863

[Intro to Metabolism]

Describe RMR

Back 863

– Resting Metabolic Rate

– measurement of the amount of energy needed to maintain normal function

– energy production requires Oxygen, thus Oxygen can be measured to calculate RMR/BMR

Front 864

[Intro to Metabolism]

Define Digestion

Back 864

breaking food down into absorbable components

Front 865

[Intro to Metabolism]

Define Absorption

Back 865

transfer of digested components from the gut to the blood

Front 866

[Intro to Metabolism]

Define Metabolism

Back 866

What happens after the molecule has been absorbed

Front 867

[DS – Byproducts of Metabolism]

Describe the benefits of lactate and ketone production

Back 867

lactate can be used for energy or in gluconeogenesis. Ketones can be used as a source of fuel and is a normal production by the liver.

Front 868

[DS – Byproducts of Metabolism]

Recall that amino acid catabolism generates ammonia and name the process through which the ammonia is detoxified and eliminated. Name the organ in which this occurs

Back 868

the ammonia is turned into urea in a process called the urea cycle which occurs primarily in the liver

Front 869

[DS – Byproducts of Metabolism]

Interpret BUN lab results

Back 869

urea in the blood is measured by blood urea nitrogen (BUN)

Front 870

[DS – Byproducts of Metabolism]

Describe the importance of the glutathione peroxidase system in neutralizing reactive oxygen species including the role of NADPH and the pentose phosphate pathway

Back 870

it neutralizes ROS by acting as a reducing agent in a process catalyzed by glutathione peroxidase. NADPH is an electron donor used to regenerate reduced glutathione which can then neutralize another molecule of peroxide. Pentose phosphate pathway is the ONLY pathway that can produce NADPH in red blood cells.

Front 871

[DS – Byproducts of Metabolism]

Define the term methemoglobin and explain the roles of the glutathione peroxidase system and methemoglobin reductase in preventing it from forming and regenerating ferrous hemoglobin

Back 871

Methemoglobin is when the iron in heme is oxidized from its ferrous (Fe2+) to its ferric state (Fe3+). Methemoglobin reductase uses NADH to re–reduce the heme iron back into the ferrous state.

Front 872

[DS – Byproducts of Metabolism]

Explain how bilirubin is eliminated and interpret bilirubin lab results

Back 872

Bilirubin will travel to the liver on albumin and once it's there, the liver will convert it to bilirubin diglucuronide via an enzyme called glucuronyl transferase. It will then be excreted in the bile. Bilirubin diglucuronide is called conjugated bilirubin because it has been conjugated to something else. Indirect bilirubin is not conjugated and if there is a problem with the bile duct then the excess bilirubin will go into the blood.

Front 873

[DS – Byproducts of Metabolism]

Alanine and aspartate aminotransferase (ALT and AST)

Back 873

Enzymes that are important for amino acid and nitrogen metabolism. Present at high concentrations in the liver.

Front 874

[DS – Byproducts of Metabolism]

Alkaline phosphatase

Back 874

disorders affecting the bile duct can result in elevated serum levels of this enzyme

Front 875

[DS – Byproducts of Metabolism]

Bilirubin (direct and indirect)

Back 875

if a bile duct is blocked then you will find bilirubin in the blood and indirect bilirubin would be elevated if you have a genetic defect in glucuronyl transferase or if the liver is damaged

Front 876

[DS – Byproducts of Metabolism]

Albumin

Back 876

albumin is produced by the liver, it will often be present at reduced amounts in patients with suboptimal liver function

Front 877

[Intro to Bacteria I & II]

Nucleoid

Back 877

Bacterial chromosome of coiled DNA (~2000–4000 genes)

Front 878

[Intro to Bacteria I & II]

Plasmid

Back 878

Smaller circle of DNA
Carries genes for antibiotic resistance, toxin production, etc.
~5–100 genes

Front 879

[Intro to Bacteria I & II]

Cytoplasm

Back 879

PACKED with ribosomes (most: polysomes)
Ribosomes (50S and 30S) are sites for some antibiotics
Also has Inclusion Bodies (storage granules and gas vacuoles)

Front 880

[Intro to Bacteria I & II]

Cytoplasmic Membrane

Back 880

Osmotic barrier
Specific transport (nutrients)
generates ATP through respiration
Senses environmental changes

Front 881

[Intro to Bacteria I & II]

Cell Wall

Back 881

Peptidoglycan (aka murien)
Site for lysozyme (tears)
Synthesis is site for many antibiotics
Strength and shape to the cell

Front 882

[Intro to Bacteria I & II]

Outer Membrane

Back 882

Gram Negative ONLY
Contain Porins (entry of nutrient molecules)
Lipoprotein (anchors outer membrane to cell wall)
Composed of Lipopolysaccharides (specific O–side chain, core polysaccharide)

Front 883

[Intro to Bacteria I & II]

Periplasmic Space

Back 883

Space between outer and inner membrane
Gel contains loose network of murien ("cell wall")
Hydrolytic and degradative enzymes
Other enzymes involved in peptidoglycan synthesis, nullification of toxins, etc.

Front 884

[Intro to Bacteria I & II]

Cell Envelope

Back 884

Entire outer complex (cell wall, inner and outer membranes)

Front 885

[Intro to Bacteria I & II]

Bacterial Capsule

Back 885

aka Glycocalyx
Composed of polysaccharides
Viscous, fibrous matrix
Antiphagocytic
*Encapsulated bacteria = smooth, nonencapsulated = rough

Front 886

[Intro to Bacteria I & II]

Pili (fimbriae)

Back 886

Responsible for attachment to specific cell types (e.g. Streptococcus to throat cells)
Used in sexual genetic transfer

Front 887

[Intro to Bacteria I & II]

Flagella

Back 887

Motility via proton motive force
Long helical filament, flexible hook, basal body
Spins counterclockwise (straight); clockwise (tumbles)

Front 888

[Intro to Bacteria I & II]

Spores

Back 888

Metabolically inactive bacteria
Survive literally almost everything

Front 889

[Intro to Bacteria I & II]

Gram +

Back 889

Thick peptidoglycan layer over cell membrane

Front 890

[Intro to Bacteria I & II]

Gram –

Back 890

Outer membrane, thin peptodiglycan layer, inner membrane

Front 891

[Intro to Bacteria I & II]

Difference between prokaryotes and eukaryotes?

Back 891

Eukaryotes have membrane–bound organelles; prokaryotes do not

Front 892

[Intro to Bacteria I & II]

Main targets for antimicrobial activity

Back 892

Cytoplasm
Peptidoglycan cell wall

Front 893

[Intro to Bacteria I & II]

Symbiosis

Back 893

An association between two organisms that live together

Front 894

[Intro to Bacteria I & II]

Mutualism

Back 894

Mutually beneficial association

Front 895

[Intro to Bacteria I & II]

Commensalism

Back 895

One organism benefits, but neither is harmed

Front 896

[Intro to Bacteria I & II]

Parasitism

Back 896

One organism benefits at the expense of the other

Front 897

[Intro to Bacteria I & II]

Actions of normal human flora

Back 897

–Occupy tissue receptors
–Antagonize other bacteria (bacteriocins)
–Synthesize vitamins and growth factors (B complex, K, E)
–Help assimilate ruffage from glycosidase production
–metabolize cholesterol and bile acids
–Stimulate proliferation of Gut–Associated Lymphoid Tissue (GALT)

Front 898

[Intro to Bacteria I & II]

athogenicity

Back 898

Ability to inflict damage

Front 899

[Intro to Bacteria I & II]

Invasiveness

Back 899

–Colonization
–Ability to bypass or overcome host defenses
–Production of extracellular substances that facilitate invasion

Front 900

[Intro to Bacteria I & II]

Toxigenesis

Back 900

–Soluble
–Transported by blood and lymph
–Cause cytotoxic effects at tissue sites

Front 901

[Intro to Bacteria I & II]

Gram + Cocci

Back 901

–Staphylococcus
–Streptococcus

Front 902

[Intro to Bacteria I & II]

Gram + Rods

Back 902

–Corynebacteria
–Bacillus
–Listeria

Front 903

[Intro to Bacteria I & II]

Gram + Spiral

Back 903

None! HAHAHAHAHA

Front 904

[Intro to Bacteria I & II]

Gram – Spiral

Back 904

–Treponoma
–Borrelia

Front 905

[Intro to Bacteria I & II]

Gram – Rods

Back 905

–Pseudomonas
–E. coli
–Haemophilus
–Bacteroides

Front 906

[Intro to Bacteria I & II]

Gram – Cocci

Back 906

Neisseria

Front 907

[Intro to Bacteria I & II]

Acid Fast Organisms

Back 907

Mycobacteria

Front 908

[Intro to Bacteria I & II]

Intracellular (obligate parasites)

Back 908

–Chlamydia
–Rickettsia

Front 909

[Intro to Bacteria I & II]

Wall–less

Back 909

–Mycoplasma

Front 910

[Intro to Bacteria I & II]

Bacterial Metabolism

Back 910

–HIGHLY efficient
–Building blocks synthesized in amounts proportional to the needs of making macromolecules
–Toxic intermediates don't accumulate
–Optimal levels of enzymes and cellular organelles are available
–Unnecessary enzymes are not made
–Cell senses and responds to environment
–Cell grows at maximum growth rate allowed by environmental conditions

Front 911

[Intro to Bacteria I & II]

How is Proton Motive Force (pmf) generated?

Back 911

Reducing power (ability to donate electrons) forces electrons to pass through Electron Transport Chain located in cytoplasmic membrane; protons are ejected, forming a concentration gradient of protons known as the proton motive force (pmf) (respiration)

Pmf is used for cellular work

Front 912

[Intro to Bacteria I & II]

How is ATP generated?
Substrate level phosphorylation

Back 912

A phosphorylated intermediate is converted to a high energy phosphate bond, which reacts with ADP to produce ATP

Front 913

[Intro to Bacteria I & II]

How is ATP generated?
Chemiosmosis

Back 913

Pmf drives protons back into cell through ATPase generating ATP from ADP

Front 914

[Intro to Bacteria I & II]

What happens when reducing power is in short supply?

Back 914

ATP is hydrolyzed to ADP, expelling protons from the cell and creates pmf, driving electrons in opposite direction along ETC.

Front 915

[Intro to Bacteria I & II]

Nutrient energy mechanisms

Back 915

–Active transport
–Group translocation (phosphorylation)–most common
–Facilitated diffusion (metabolism of nutrients)– less common

Front 916

[Intro to Bacteria I & II]

Binary Fission

Back 916

–Cell grows to twice their size
–Divide by binary fusion
–Begins at origin and proceeds in both directions
–Takes ~40 mins at 37 degrees C
–In culture doubling every 20 mins, DNA replication must initiate every 20 mins
–Multifork replication used to accomplish this (already beginning second replication as first is completed)

Front 917

[Intro to Bacteria I & II]

Phases of growth in bacteria

Back 917

–Lag: Senses the environment and makes enzymes necessary to start growth
–Exponential: (log) rapid growth occurs
–Stationary: Growth halts as resources are used up from the environment
–Death: (log)

Front 918

[Intro to Bacteria I & II]

Nutrition Requirements

Back 918

–ALL cells are heterotrophic: need performed hydrocarbons like sugars in order to grow (gets from host)
–Some (ex E.coli) need only inorganic salts and a nitrogen source
–Others (streptococcus) require more complex media (vitamins, amino acids, purines, etc.)
–Others require VERY enriched medium––Fastidious

Front 919

[Intro to Bacteria I & II]

Oxygen requirements
Strict Anaerobes

Back 919

–Neisseria or Pseudomonas
–Respiration occurs via electron transport chain, with Oxygen as final e acceptor
–Cytochrome oxidase enzyme

Front 920

[Intro to Bacteria I & II]

Oxygen requirements
Obligate anaerobes

Back 920

–Clostridium
–Only grow in absence of CO2
–Fermentation: terminal e acceptor is an organic metabolic intermediate –> organic acids (lactic acids)
–Usually lack superoxide dismutase, catalase, Catalast, and peroxidase

Front 921

[Intro to Bacteria I & II]

Oxygen requirements
Facultative

Back 921

–E. coli (most pathogenic bacteria)
–Bacteria grow aerobically in presence of oxygen, anaerobically in absence

Front 922

[Intro to Bacteria I & II]

Oxygen requirements
Aerotolerant

Back 922

–tolerate oxygen, but grow fermentatively

Front 923

[Intro to Bacteria I & II]

Iron Uptake

Back 923

–Necessary for bacterial growth
–Free iron scarce in blood and tissue––bound
–Bacteria create siderophores: iron chelating compounds

Front 924

[Intro to Bacteria I & II]

Difference between fermentation and aerobic respiration

Back 924

Ferm: w/o O
Aerobic: w/ O

Front 925

[Intro to Bacteria I & II]

Steps in Peptidoglycan synthesis

Back 925

1. Uridine diphosphate (UDP) carrier activates N–acetylmuranic acid (NAM) and N–acetylglucosame (NAG)
2. Pentapeptide added to UDP–NAM
3. UDP–NAM–PEP transfers to bactroprenol phosphate
4. UDP–NAG added to UDP–NAM–PEP (peptidoglycan monomer)
5. bactroprenol phosphate transports monomer through cell membrane
6. Autolysins break glycosidic bond b/w peptidoglycan and peptide cross–linkages of existing cell wall
7. Transglycosidase (TG) enzyme inserts and links monomers into new ppg
8. Transpeptidases (TP) reform peptide cross–links

Front 926

[Intro to Bacteria I & II]

Fosfomycin

Back 926

Inhibits phosphoenopyruvate transferase; prevents formation of NAM

Front 927

[Intro to Bacteria I & II]

Cycloserine

Back 927

Analogue of D–ala; blocks addition of dipeptide to UDP–NAM

Front 928

[Intro to Bacteria I & II]

Bacitracin

Back 928

Blocks dephosphorylation of bactroprenol phosphate (prevents transport of ppg monomer across cell membrane

Front 929

[Intro to Bacteria I & II]

Vancomycin:

Back 929

binds to peptides of ppg monomers and blocks (TG)

Front 930

[Intro to Bacteria I & II]

Beta–lactams

Back 930

–Penicillins, Cephalosporins, Carbepenems
–bind to TP

Front 931

[Intro to Bacteria I & II]

Linezolid

Back 931

Blocks initiating complex (translation)
–30S inhibitors:
–Tetracycline, Aminoglycosides
–50S inhibitors:
–Macrolides, Chloramphenicol

Front 932

[Intro to Bacteria I & II]

Fluoroquinolones

Back 932

Inhibits DNA gyrase or topoisomerase

Front 933

[Intro to Bacteria I & II]

Metronidazole

Back 933

Disrupts DNA helical structure under anaerobic conditions

Front 934

[Intro to Bacteria I & II]

Rifampin

Back 934

Binds to RNA polymerase

Front 935

[Intro to Bacteria I & II]

Sulfonamides

Back 935

Blocks synthesis of dihydropteroic acid

Front 936

[Intro to Bacteria I & II]

Trimethoprim

Back 936

Blocks synthesis of tetrahydrofolate

Front 937

[Intro to Bacteria I & II]

Polymyxins

Back 937

Interact with with phospholipids

Front 938

Name the 4 major dietary sources of fuel

Back 938

Carbohydrates
Fats
Proteins
? unknown, clarify

Front 939

Explain: Catabolism vs. Anabolism

Back 939

Catabolism: breaking down for energy

Anabolism: constructing a molecule, requires

Front 940

Monosaccharides

Back 940

Glucose

Galactose

Fructose

Front 941

Disaccharides

Back 941

Lactose

Maltose

Sucrose

Front 942

Sucrose is made up of what saccharides

Back 942

glucose + fructose

Front 943

Maltose is made up of what saccharides

Back 943

glucose + glucose

Front 944

Lactose is made up of what saccharides

Back 944

glucose + galactose

Front 945

Polysaccharides

Back 945

Cellulose
Hemicelluloses
Pectin
beta–glucans
Fructans

Front 946

The portion of the reducing sugar that is oxidized in a cupric compound

Back 946

Aldehyde group

Front 947

What color will the glucose or galactose oxidase tests turn in the presence of a reducing sugar?

Back 947

Blue

Front 948

What is the difference between an unsaturated & polyunsaturated fatty acid?

Back 948

1 double bond vs. >1 double bond

Front 949

Results from partial hydrogenation of vegetable oils

Back 949

trans

Front 950

Most abundant double bond arrangement in fatty acids

Back 950

CIS

Front 951

used to make vegetable oils more solid at room temperature

Back 951

hydrogenation

Front 952

structure of triglycerides

Back 952

3 fatty acids
one glycerol

Front 953

Importance of Triglycerides

Back 953

energy storage

transport of dietary fats

Front 954

Three main body fuel stores

Back 954

proteins

carbohydrates

fats

Front 955

[Fungal]

Describe fungal pathogenesis

{think definition, not process}

Back 955

basic mechanism of fungal pathogenicity is the ability to adapt to tissue environment & temperature (body & fever range) & withstand the lytic activity of host cellular defenses

Front 956

[Fates of a Cell]

Describe Oxygen-derived free Radicals,

specifically: Superoxide Ion

*boards only

Back 956

production: incomplete reduction of O2 during oxidative phosphorylation; by phagocyte oxidase in leukocytes

inactivation: conversion of H2O2 & O2 by superoxide dismutase

path. effects: stimulates production of degradative enzymes in leukocytes & other cells; may directly damage lipids, proteins, DNA, acts close to site of production

Front 957

[Fates of a Cell]

Describe Oxygen-derived free Radicals,

specifically: Hydrogen Peroxide

*boards only

Back 957

production: generated by SOD from O2 and by oxidases in peroxisomes

inactivation: conversion to H2O & O2 by catalase (peroxisomes), glutathione peroxidase (cytosol, mitochondria)

path. effects:can be converted to *OH & OCL- ; which destroy microbes & cells; can act distant from site of production

Front 958

[Fates of a Cell]

Describe Oxygen-derived free Radicals,

specifically: Hydroxyl Radical

*boards only

Back 958

production: generated by H2O by hydrolysis (radiation) ; from H2O2 by Fenton Reaction; From superoxide ion

inactivation: conversion to H2O by glutathione Peroxidase

path. effects: most reactive oxygen-derived free radical; principal ROS responsible for damaging lipids, proteins & DNA

Front 959

[Fates of a Cell]

Describe Oxygen-derived free Radicals,

specifically: Peroxynitrate

*boards only

Back 959

production: produced by interaction of superoxide ion & NO generated by NO synthase in many cell types (endothelial cells, leukocytes, neurons, etc)

inactivation: conversion to HNO2 by peroxiredoxins (cytosol, mitochondria)

path. effects: damages lipids, proteins, DNA

Front 960

[Fates of a Cell]

What is the most reactive oxygen derived free radical responsible for the most damage?

Back 960

Hydroxyl Radical