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79 Cards in this Set

  • Front
  • Back
Physiology
Study of normal body functions
Primary tissues
1. Muscle- contraction, generation of force
2. Nerve- initiate, transmit electrical impulses
3. Epithelial- barrier between body and external environment; exchange
4. Connective- connect, anchor, support
Organs
collection of 2 or more types of tissues put together into structure that performs specific function
Organ Systems
collection of organs that work together to accomplish a particular task
Body fluid compartments
1. Total body water= 70% BW
2. Intracellular fluid = 2/3 TBW
3. Extracellular fluid = 1/3 TBW
4. Plasma = 1/5 ECF
5. Interstitial fluid
Negative feedback control in homeostasis
-Primary mechanism for maintaining homeostasis (aka homeostatic control mech.)
-3 basic components: sensors (nerve receptors), control center (brain/spinal cord), effectors (muscles/glands)
-Mechanisms: set point, sensors send input to integrating center which compares to set point then error signal goes to IC which sends output to brings level back to set point
-inhibitory, i.e. final corrective action is opposite to the initial deviation from the normal value (or condition).
Positive feedback
-loops cause rapid change (ex: ovulation)
-ex: upstroke of action potential in nerve and muscle
-body uses it to bring a physiological process to a quick completion (ex: childbirth, ovulation)
-does not lead to stability or regulation, but the opposite: a progressive change in one direction.
Feedforward control
Term referring to an animal's ability to predict an upcoming disturbance to the homeostatic state, and to take the necessary corrective action. It is anticipatory- does not require error signals. Learned responses to known cues.
Homeothermic
of birds and mammals; having constant and relatively high body temp. (aka: warm-blooded)
Poikilothermic
of animals except birds and mammals; having body temp that varies with the environment (aka cold-blooded)
Hypothermia
subnormal body temp
Hyperthermia
abnormally high body temp (fever)
above 41 C (105.8 F), dangerous
above 43 C (109.4 F), deadly
Mechanisms of heat transfer between body and external environment
-radiation- thermal energy as electromagnetic waves
-conduction- thermal energy through direct contact
-evaporation- heat loss through evaporation of water (insensible water loss, sweating)
-convection- heat transfer by movement of fluid or air
Fever
-accompanies infections
-MOs and WBCs secrete pyrogens
-body temp set point increases (fever does NOT result from a failure of the thermoregulatory system)
-due to the resetting of the set point in the body's thermostat (hypothalamus)
-low fever enhances immune response; but fever that is too high and occurs too fast is dangerous
Pyrogens
fever-inducing agents produced by bacteria, viruses, molds, and yeasts, or produced endogenously by WBC/macrophages
Heat stroke
an acute hyperthermia resulting from excessive exposure to heat, natural or artificial. The temp regulatory mechanisms become overwhelmed and unable to effectively deal with the heat, and body temp climbs uncontrollably
Symptoms of heat stroke
dry skin
vertigo
headache
thirst
nausea
muscular cramps
body temp may be subnormal
Heat exhaustion
effect of excessive exposure to heat, occurring among workers in hot places (i.e. furnaces, sun's heat, foundries)
Symptoms of heat exhaustion
normal/subnormal temp
dizziness
headache
nausea
weakness
profuse sweating
sometimes delirium or collapse
Thermoneutral zone
range of ambient temp over which the organism is able to maintain a constant body temp without the use of metabolically demanding mechanisms (such as more fat burning, more muscle contractions, more sweating, etc.)
Pathology
study of diseases;
branch of medical science that studies the causes, nature and effects of diseases and esp of the structural and functional changes produced by them
Symptoms
subjective abnormalities felt by the patients
Signs
objective abnormalities perceptible to the examining physician
Syndrome
collection of symptoms and signs
Etiology
study or theory of all factors that cause disease and the method of their introduction to the host; the causes or origin of a disease or disorder
Remission
a diminution or abatement of the symptoms of a disease; also the period during which such diminution occurs
Relapse
the return of a disease after its apparent cessation
Epidemiology
the study of diseases (occurrence, distribution, and transmission) in populations
Endemic diseases
disease in population that is restricted to a local region
Epidemic disease
it has spread to many individuals at the same time in a larger region
Pandemic disease
an epidemic that is geographically widespread; occurring throughout a very large region, a continent, or even throughout the world
Properties of water
-high heat capacity
-high heat of vaporization
-solvent
-molecules are cohesive and adhesive (high surface tension and capillary action)
-pure water freezes at 0 C but is most dense at 4 C. That is, solid water (ice) is less dense than cold liquid water
-polar molecules dissolve in water
Acids and bases
-An acid is a proton donor and a base is a proton acceptor
-strong acids dissociate totally, and the anions formed (like Cl- from HCl) are not bases because they do not associate with protons in solution. Only weak acids, mostly organic, dissociate partially.
pK' of an acid
the pH at which the acid is half dissociated, when [A-]=[HA]
Buffer system
-simply a mixture of a weak acid (e.g. acetic acid) and its conjugate base (e.g. acetate ion, an anion) or a weak base (e.g. ammonia, NH3) and its conjugate acid (NH4+, a cation)
-works by reacting with any added acid or base to control the pH, as the strong acid or base is changed to a weak one
Definition of buffering
ability of a solution to resist a change in pH when acid or base is added
More effective buffer:
make sure that the concentration of the buffering agents is large in comparison to the added acid or base
Biomolecules
Carbon-based (organic) molecules synthesized by living organisms.
Including carbohydrates, lipids, proteins/amino acids, and nucleic acids/nucleotides
Atoms
an atom is the smallest part of an element which can take part in a chemical reaction; they are the basic building blocks of ordinary matter and can join together to form molecules
Element
substance made entirely from one type of atom
Which 4 elements make up 98% of atoms in the body?
H, O, C, N
(other 2%: P and S, etc.)
Common functional groups in biomolecules
hydroxyl
sulfhydryl
phosphate
carboxyl
amino
Carbohydrates (sugars)
C,H,O in proportion of 1:2:1
Cn(H2O)n = (CH2O)n
Monosaccharides
glucose, fructose, galactose, ribose, 2-deoxyribose

notice hydroxyl groups which make carbs polar
Disaccharides
sucrose, lactose

formed by dehydration synth. from monosaccharides
(sucrose = glucose + fructose)
joined by glycosidic linkage
Sweetest carb?
fructose
Polysaccharides
starch (from plants)
glycogen (animal starch)
Lipids
composed of primarily hydrogen and carbon atoms

non-polar/hydrophobic (poor solubility in water)
Classes of Lipids
Triglycerides
Phospholipids
Eicosanoids
Steroids
Triglycerides
glycerol + 3 fatty acids
What makes triglycerides hydrophobic?
Fatty acid chains
Triglyceride is produced by
dehydration synthesis from glycerol and fatty acids
Phospholipids
one -OH of glycerol linked to phosphate

amphipathic (amphiphilic) molecules

phosphatidyl choline = lecithin
Amphipathic (Amphiphilic) means
polar (hydrophilic)- phosphate group (Head)

nonpolar (hydrophobic)- FA chains (Tails)
Eicosanoids
group of 20-C fatty acids with a cyclopentane ring

(prostaglandine, thromboxanes, leukotrienes)
Steroids
Ring structure made of 4 C rings derived from cholesterol

Hydrophobic (NOT water soluble)
Sex steroids
estradiol
testosterone
progesterone
Adrenal steroids
cortisol
aldosterone
Proteins/Amino acids
proteins = polymers of amino acids

20 aa's are building blocks of proteins

macromolecules of thousands of atoms

function as receptors, enzymes, ion channels, antibodies, etc.
Basic structure of aa's
R = side chain that can vary in property (polar, nonpolar, ionized)
20 diff aa's due to 20 diff R's.
peptide bond
covalent bond between carboxyl group of one aa and amino group of another aa
peptides
generally 2-50 aa's (smaller)
proteins
greater than 50 aa's (huge)
How are peptide bonds produced?
dehydration synthesis
Primary protein structure
sequence of aa's
Secondary protein structure
H-bonding between amino hydrogen of 1 aa and carboxyl oxygen of another aa

(alpha helixes and beta pleated sheets)
Tertiary protein structure
formation of bends and loops in polypeptide chain due to interactions between R groups

*overall shape (folding) of protein*
Interactions causing tertiary structure
-electrostatic interactions (ionic bonds)
-van der waals forces
-hydrogen bonds
-covalent bonds (disulfide bridge)
Quaternary protein structure
formation of proteins with more than one polypeptide (2 or more chains/subunits) linked by disulfide bonds
glycoproteins
contains sugar units, i.e. FSH
lipoproteins
contains lipids, i.e. LDL, HDL
Nucleic acids/nucleotides
Functions: storage, expression, and transmission of genetic info

basic subunit = nucleotide = sugar + phosphate + nitrogenous base
Purines (double rings)
A and G
Pyrimidines (single ring)
C, T, and U
ATP and ADP
-high energy phosphate bonds
-major molecules for transferring energy
-muscle contraction
-active transport across membranes
-synth. of organic molecules
what are cAMP and cGMP?
messengers
what are NAD and FAD?
other energy-transferring nucleotides
A-T or A-U
two H-bonds
G-C
three H-bonds