N503 Biomedical Foundations

Front 1

Eukaryotes and Prokaryotes:

Name 4 differences

Back 1

1. Eukaryotes = higher plants and animals, Prokaryotes = bacteria

2. Eukaryotes have a well defined nucleus and membrane-bound intracellular compartments, Prokaryotes do not have a lack of any distinct nucleus

3. Eukaryotes are much larger than Prokaryotes

4. Eukaryotes have several distinct chromosomes, Prokaryotes have only one chromosome

Front 2

"Building blocks of life" molecules within cells

4 of them

Back 2

1. CHO, or carbohydrates
2. Proteins
3. Lipids
4. Nucleic Acids

Front 3

Functions of Carbohydrates

5 of them

Back 3

1. Fuel to satisfy metabolic requirements, stored as glycogen in liver and muscle

2. Stored as triglycerides and converted to fatty acids when taken in excess

3. Glycoproteins

4. Protein-sparing effect

5. Marker for glucose control - HbA1c

Front 4

Functions of Proteins

5 of them

Back 4

1. Fuel (not very efficient)

2. Enzymes

3. Antigens

4. Clotting factors (prothrombin, fibrinogen)

5. Carriers - Albumin, TBG, SHBG

Front 5

Functions of Lipids

4 of them

Back 5

1. Fuels - fatty acids

2. Triglycerides - made from fatty acids and stored in adipose

3. Phospholipids - major component of cell membranes

4. Circulating lipoproteins are important contributors to heart disease LDL (bad) and HDL (good)

Front 6

Nucleic acids

Name two main types and NA function

Back 6

1. DNA
2. RNA

Main function is for information storage and transmission

Front 7

Chromosomes

How many pairs

Back 7

Humans have 23 pairs of chromosomes, 22 autosomes and 1 pair of sex chromosomes

Front 8

Types of Membrane Transport

2 types

Back 8

1. Passive transport
a. simple diffusion
b. passive mediated transport

2. Active transport
a. Nacl / K pump (maintains concentration gradient and membrane potential in cells by sending Na out of cell and K back into cell

Front 9

Name 4 Eukaryotic organelles

Back 9

1. Golgi complex
2. Lysosomes
3. Mitochondria
4. Peroxisomes

Front 10

Name 4 Carbohydrates

Back 10

1. Clucose (C6 H12 O6)
2. Fructose
3. Sucrose
4. Lactose

Front 11

Name 7 important enzymes that are usually only found in cells

Back 11

1. Hexokinase: muscle enzyme, makes G6P (yeast)

2. Lactate dehydrogenase (LDH) catalyzes oxidation of lactate to pyruvate

3. Creatine phosphokinase (CPK): released from heart cells post MI

4. Aspartate aminotransferase (AST): liver, moves amino acid from aspartic acid to oxaloacetic acid (SGOT)

5. alanine amino transferase (ALT): liver, helps form pyruvate (SPGT)

6. Glucokinase - liver, glucose phosphorolation

7. ACTH – adrenocorticotropic hormone – growth of adrenal gland, secretes corticosteroids

Clinical point: when cells break these leak out and can be measured in the blood plasma

Front 12

Four functions associated with the cell membrane

Back 12

1. Contact inhibition: keeps cells from growing out of control (cancers)

2. Transduction: messages from extracellular space to intracellular space begins here

3. Immune surveillance: recognition of a substance and activation of immune cells if necessary

4. Transport: the cell membrane is an effective diffusion barrier (Na/K pump)

Front 13

Kreb's Cycle formula

Back 13

Acetyle Co A + FAD + NAD + O2 → Co2 + ATP + NADH + FADH + H2O

Front 14

Henderson-Hasselbach Equation

Back 14

pH = pKa (6.1) + log base (HCO3 – Kidney) / log acid (CO2 - lung)

Front 15

Name types of acidosis & alkolosis; the organs and chemicals involved and

Back 15

Kidney:
Metabolic alkalosis = vomiting (up HCO3)
Metabolic acidosis = Type 1 Diabetes (down HCO3)

Lungs:
Respiratory acidosis = poor ventilation (COPD) (up CO2)
Respiratory alkalosis = hyperventilation (down CO2)

Front 16

Acid phosphatase

Back 16

A type of enzyme used to free attached phosphate groups from other molecules during digestion. It is stored in lysosomes and functions when these fuse with endosomes, which are acidified while they function; therefore, it has an acid pH optimum.

Front 17

Alkaline phosphatase

Back 17

A hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. Most effective in an alkaline environment. Mainly found in the liver.

Front 18

Adenosine Deaminase (ADA)

Back 18

Adenosine deaminase (also known as ADA) is an enzyme involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. ADA2 is the predominant form present in human blood plasma and is increased in many diseases, particularly those associated with the immune system; for example rheumatoid arthritis, psoriasis and sarcoidosis. The plasma AD2 isoform is also increased in most cancers.

Front 19

Microsomal enzymes

Back 19

found in high concentration in the liver, but also in all cells. These are inducible enzymes, inducible by drugs, elcohol, herbal supplements, etc. (CyP450)

Front 20

Reverse Transcriptase

Back 20

makes DNA from RNA (AIDS infects the cells of its host and uses those cells to create DNA from the disease’s RNA for replication)

Front 21

Protease enzymes

Back 21

help to assemble viruses and protease inhibitors are used to prevent viral duplication.

Front 22

Somatotropin

Back 22

A protein hormone which stimulates growth and cell reproduction in humans and other animals. It is a 191-amino acid, single chain polypeptide hormone which is synthesized, stored, and secreted by the somatotroph cells within the lateral wings of the anterior pituitary gland.

Front 23

Somatostatin

Back 23

Also known as growth hormone inhibiting hormone (GHIH) or somatotropin release-inhibiting hormone (SRIF), is a peptide hormone that regulates the endocrine system and affects neurotransmission and cell proliferation via interaction with G-protein-coupled somatostatin receptors and inhibition of the release of numerous secondary hormones.

Front 24

Hormone Receptor

Back 24

A hormone receptor is a receptor protein on the surface of a cell or in its interior that binds to a specific hormone. The hormone causes many changes to take place in the cell.
Binding of hormones to hormone receptors often trigger the start of a biophysical signal that can lead to further signal transduction pathways, or trigger the activation or inhibition of genes.

Front 25

Lipids: 3 types

Back 25

1. Fatty acids (fatty acids can be saturated or unsaturated)
Steatorrhea – increase fat in stool due to gall bladder disease 70% of heart energy is from fatty acids
Palmitic (C14), Oleic (C16), Stearic (C18)

2. Phospholipids: cell membrane composed of glycerol and 2 fatty acids + C and one carbon/phosphate group (serine, choline, inositol), break down into second messengers

3. Lipoproteins: (VLDL, LDL, HDL – highly desirerable), Cholesterol, Steroid hormones, Vitamin

4. Triglycerides: three fatty acids stuck together with glycerol. LDL found here

Front 26

Eukaryotes and Prokaryotes:

Explain difference

Back 26

Eukaryotes: mammalian cells that have defined structure with different functions of each element

Prokaryotes: genetic information exists freely in the cytoplasm (no nucleus, mitochondria). These are really the bacterial cells.

Front 27

Apoptosis and the role of p53

Back 27

Apoptosis is programmed cell death. P53 is the guardian of the genome. It stops mutated cells from dividing and replicating. P53 tells cell to do apoptosis, linked to BRCA 1 and 2 and HPV. They are highly over expressed in cancer cells, they stop cells from entering synthetic stage of life cycle, and mutations and inactivation lead to more S phase and more cell growth

Front 28

Gram Staining

Back 28

The cell wall of most microorganisms contains variable amounts of peptidoglycan. The significance of this is that the Gram stain sticks to the thick peptidoglycan layer which characterizes some bacterial organisms and this classifies the microorganism as Gram positive. Those microorganisms with thin peptidoglycan layers are Gram negative.

Our tears and saliva contain an enzyme called lysozyme that hydrolyzes and destroys peptidoglycan.

Front 29

Cell Membrane or plasmalemma:

Back 29

A lipid bilayer composed of phospholipid, cholesterol, proteins and glycoproteins.

Front 30

Peptidoglycan

Back 30

Peptidoglycan, also known as murein, is a polymer consisting of sugars and amino acids that forms a mesh-like layer outside the plasma membrane of eubacteria. The sugar component consists of alternating residues of β-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid residues. Attached to the N-acetylmuramic acid is a peptide chain of three to five amino acids. The peptide chain can be cross-linked to the peptide chain of another strand forming the 3D mesh-like layer. Some Archaea have a similar layer of pseudopeptidoglycan. Peptidoglycan serves a structural role in the bacterial cell wall, giving structural strength, as well as counteracting the osmotic pressure of the cytoplasm. A common misconception is that peptidoglycan gives the cell it's shape, however, while peptidoglycan helps maintain the structure of the cell, it is actually the MreB protein that facilitates cell shape. Peptidoglycan is also involved in binary fission during bacterial cell reproduction.

Front 31

Cell membrane: what's it made of?

Back 31

lipid bilayer with phospholipids, cholesterol, proteins, and glycoproteins

Front 32

Give 3 types of transport used in the cell

Back 32

Passive diffusion – no energy used to move a molecule from higher to lower concentration

Facilitated diffusion – no energy used but carrier molecules help a molecule move from higher to lower concentration

Active transport – energy used to move AGAINST a concentration gradient

Front 33

Antiport Transport

Back 33

opposite direction Na/K pump – Na diffuses down the gradient into the cell and K diffuses down the gradient out of the cell, so the cell pumps out Na and reclaims K thus maintaining concentration difference to insure membrane potential
Digoxin, cardiac glycoside, inhibit the pump, increase Na in cell
Na/Ca exchange – result from Digoxin
Na increases inside cell, which is pumped out in exchange for Ca. Ca increases inside the cell therefore causing an increase in cardiac contraction (positive ionotropic effect)

Front 34

Symport Transport

Back 34

Move in same direction. Kidney tubules filter Na and glucose out of urine back into cells ORT (oral rehydration therapy) – gives Na and glucose (Cholera)S

Front 35

Endoplasmic Reticulum structure and function

Back 35

Makes cell membrane, makes proteins for export (with ribosomes), processing of secretory proteins, cholesterol synthesis, mixed function oxygenases (triglyceride synthesis)

Front 36

Golgi Complex structure and function

Back 36

Golgi Complex – develops secretory cells called granules, sorts lysosomal enzymes to be sent to lysosome.

Cysitic fibrosis: chloride containing cells get killed in lysosome so H2O goes up

Front 37

Role, structure, and function of Lysosomes

Back 37

intracellular digestion, 40 different enzymes, WBC! Very acidic. They:
1. destroy worn out organelles, macromolecules, cells
2. destroy engulfed bacteria (antigen-antibody complexes for presentation)
3. cleave cholesterol from LDL
4. important in immune response too, presents antigen

Tay-Sachs – absence of BN hexosaminidase, so no gangliosides are metabolized and the cell dies (trash never taken out)

Gout – accumulation of uric acid in lysosomes so they die and cause inflammation and leak out enzymes

Mycobacterium tuberculosis – engulfed by lysosome and secretes chemical which prevent fusion in phagosomes

Legionella pmeumophila – inhibits acidification because of capsule

Myco leprae – capsules of bacterium not digestible by cell

Front 38

Role, structure, and function of Mitochondrion

Back 38

arvests energy form ingested nutrients. Provides oxidative phosphorolation – O2 last electron acceptor, electron transport, and ATP production
regulation of apoptosis (Alzherimer’s disease), have own DNA, not found in bacteria
Bilrubin – mitochondrial disturbance across blood brain barrier, can lead to mental retardation if light therapy is not given

Front 39

Metabolism of glucose, glycolysis

Back 39

Glucose enters the cell via facilitated diffusion or active transport, determined by Insulin induced signals, receptors, and PI3K

Phosphorlation – via hexokinase or glucokinase (liver and pancrease). This traps glucose and is the first step to breakdown hexose into glucose 6 phosphate

Glycogen storage, Glycolysis, Pentose Cycle, Fatty acid

Glycogen storage – liver and muscle do glycogenesis in response to insulin stimulating glycogen synthase

Opposite = glycogenolysis triggered by epinephrine of glucagons

cAMP – first documented 2nd massager in liver during glycolysis

Glycolysis – glucose becomes lactic acid (anaerobic) or pyruvate (aerobic)

Glucose + NAD+ → pyruvate + NADH + H + ATP

NADH + Fe3+ → Fe2+ (good!)

Anaerobic = pyruvate + NADH → lactate + NAD+

Aerobic = pyruvate

Front 40

What is the role of surfactant

Back 40

The surface tension (ST) of the alveolus, which is where gas exchange occurs, is quite high. This is due to the fact that surface tension is inversely proportional to the radius of a sphere (alveolus in this case). Inflating the alveolus is much like blowing up a very, very small balloon. Surfactant, a term that describes a number of complex phospholipids composed primarily of lecithin or phosphatidylcholine, lowers surface tension and makes it easier to expand and inflate the lungs and to ventilate them. Surfactants also appear to be part of the innate immune system, helping the lungs to clear infectious organisms.

Front 41

plasminogen activators

Back 41

A circulating protein referred to as plasminogen is cleaved to plasmin which dissolves
clots. The conversion of plasminogen to plasmin is accomplished by a group of poorly defined substances classified more by their actions than by their structure-called plasminogen activators and a lot of it is in lung tissue. Helps dissolve clots trapped there. The clot filtering abilities of the lungs is quite important.

Front 42

Tidal Volume

Back 42

the amount of air moving into and out of the lungs during each respiratory cycle- about 500 ml of which about 350 ml actually get to where gas exchange can occur. The remaining air often referred to as dead space is about 150 ml.

Front 43

Minute Volume

Back 43

the respiratory rate x tidal volume or 15-17 times 500 ml or about 7.5L.

Front 44

Vital Capacity and Forced Vital Capacity

VC and FVC

Back 44

after a maximal inspiration the amount of air that can be forcibly expelled is about 5L and this is the VC.

Front 45

FEV1

Back 45

One lung function test is the forced expiratory volume in one second (FEV1) divided by the forced vital capacity (FVC) usually measured over 5 seconds. A normal individual will expel four fifths or 80% of their FVC in 1 second.

Front 46

Functional Residual Capacity (FRC)

Back 46

After a normal passive expiration the amount of air left in the lings is the FRC or functional residual capacity.

Front 47

Total Lung Capacity (TLC)

Back 47

total lung capacity =VC plus RV.

Front 48

Gas Exchange

Back 48

This is about the movement of O2. The atmosphere at sea level exerts a barometric or air pressure of 760 mm Hg or 760 Torr (after Torricelli). Per ml of air there are approximately 1 times 1019 molecules, and air pressure is the direct result of the many molecules present in the air.

Front 49

Total Lung Capacity (TLC)

Back 49

total lung capacity = VC plus RV

Front 50

Gas Exchange

Back 50

this is about the movement of O2. The atmosphere at sea level exerts a barometric or air pressure of 760 mm Hg or 760 Torr (after Torricelli). Per ml of air there are approximately 1 times 1019 molecules, and air pressure is the direct result of the many molecules present in the air.

Front 51

Cardiac Output formula

Back 51

heart rate/minute X volume/beat

Front 52

What is the role of hemoglobin? Why is it important?

Back 52

Hemoglobin is responsible for transporting O2 throughout the circulatory systems of organisms. Organisms that do not rely on hemoglobin to transport O2 use simple diffusion of the oxygen molecule to supply their organs.

Front 53

What are the fates of CO2?
Name 5 of them

Back 53

1. used at rest (10% lungs, 60% HCO3, 30% carbamino compound)
2. Dissolves in plasma
3. Carbonic anhydrase makes CO2 into HCO3 CO2 + H2O → H2CO3 → H+ + HCO3-
4. HCO3- exchanged with Cl-
5. CO2 + Hb → carbamino compound HbCO2

Front 54

Hemoglobin: function of

Back 54

Hb is what carries the majority of O2 throughout the blood. 4 O2 per Hb. Increases O2 capacity by 65x - 195mL/L or 975mL/5L

Front 55

Phrenic Nerve

Back 55

responsible for producing contractions in the diaphragm. Irritation of this nerve leads to hiccups

Front 56

Respiratory rate: CNS systems involved

Back 56

Medullary center – initiation and maintanence

Apneustic center and Pneumotaxic center – complementary systems that self regulated
breathing and make it regular

pCO2 – decrease sensitivity of receptors (hypoventilation due to barbiturates, morphine)

hypercapnea – increase CO2 in blood

pO2 – decrease in p50 activate aortic and carotid receptors
H+ - acid base balance

Front 57

Ambient VS alveolar air: % and concentrations of elements

Back 57

Ambient Alveolar
pO2 159 104
PN2 597 569
PCO2 0.3 40
PH2O 3.7 47
Total 760 760

Front 58

Pulmonary ventilation involves three different pressures:

Back 58

1. Atmospheric pressure: the pressure of the air outside the body

2. Intraalveolar (intrapulmonary) pressure: the pressure inside the alveoli of the lungs

3. Intrapleural pressure: the pressure within the pleural cavity.

These three pressures are responsible for pulmonary ventilation.

Front 59

Name the 4 biologically important molecules

Back 59

1. Carbohydrates (Glucose, Fructose, Sucrose, Lactose)

2. Proteins: Amino Acids (essential, gluconeogenic, ketogenic) and Enzymes (AST, LDH, HDH, CPK, ALT, SGPT) also hormones, antigens, antibodies, clotting factors

3. Lipids: Fatty Acids, Triglycerides, Phospholipids, Lipoproteins, Cholesterol, Steroids

4. Nucleic Acids: DNA and RNA

Front 60

What is the structure and function of each biologically important molecule?

Back 60

1. Carbohydrates: fuel reserve, measure of body’s ability to tolerate elevations in sugar levels (HbA1c)

2. Proteins: provide fuel, catalyze chemical reactions (enzymes), provide basis for all the functions listed above

3. Lipids: major component of cell membranes

4. Nucleic Acids: provide framework for building blocks of life in cell

Front 61

What hormones mediate/control the four biologically important molecules?

Back 61

1. Carbohydrate storage controlled by insulin and epinephrine

2. Proteins - Human Growth Hormone

3. Lipids: steroids and cholesterol, cortisol

4. Nucleic Acids: N/A