gjiogd Flashcards

(27 cards)

1
Q

blood osmolality

A

increased: drink more, release antidiuretic

decreased: not thirsty, no antidiuretic

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2
Q

serum osmolality tests for

A

hydration
hyperglycemia
hypothalamus
ethylene glycol

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3
Q

ethylene glycol

A

kidney + liver try to metabolize -> toxic metabolites -> metabolic acidosis + nephrotoxosis from oxalate forming

TREATMENT: IV (often w sodium bicarbonate) of dilated ethanol competitive inhibitor

restores hydration, electrolytes, kidney function, excretes poison

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4
Q

fluid

A

crystalloid: lots small solutes, cross wall (hypo/iso), hydrating

colloid: large, don’t cross (iso), hold fluid

ISOTONIC: same osmolality as blood eg. 0.9% NaCl

HYPOTONIC: less osmolality than blood (more solutes inside than out)
- cell burst

HYPERTONIC: more osmolality than blood (more solutes outside)
- cell shrinks

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5
Q

solutes

A

electrolytes most common

organic molecules (proteins, phospholipids, cholesterol, triglycerides) large, less, uneven between compartments

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6
Q

diffusion

A

passive
- molecules from high -> low solute concentration
- depends on size, charge, and lipid solubility

FACILITATED
- carrier protein helps
eg. glucose -> muscle/fat

DIALYSIS
- blood circulated through fake kidney-> dialysate in opposite direction -> toxins go from blood to dialysate (lower concentration)

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7
Q

osmosis

A

the movement of water from low -> high solute concentration
- semipermeable membrane
eg. water in stomach -> bloodstream

OSMOTIC PRESSURE
- water comes in because more protein interstitial

ONCOTIC PRESSURE
- pressure difference between in/out, exerted to stop when equilibrium reached

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8
Q

filtration

A

hydrostatic pressure
- fluid moves out of capillaries based on pressure gradient (heartbeat)

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9
Q

membrane potential

A

changes in ion distribution on either side of membrane -> voltage

membrane selective: Na has a harder time moving in than K
- 2 K enter, 3 Na exit

eg. muscle cell contracting.

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10
Q

active transport ions

A

Na, K, Ca2, Mg2
- need ATP + carrier

either symport (same direction) or antiport

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11
Q

ion concentration maintains….

A

irritable cells (cells that create ATP through respiration)

eg. neurons, myofibrils

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12
Q

cytosis

A

nutrients in, waste out

ENDO: into cell
phago: eats solids by phagosome
pino: liquid through membrane folds
eg. small intestine
receptor mediated: cells w/specific proteins in their membrane
- ligabands bind -> coated pit vesicle
eg. insulin

EXO: out
- vesicles in ER and golgi move to cell surface, fuse to membrane, release contents extracellularly
eg. neurons -> acetylcholine.
eg. endothelial cells -> mucus
eg. mast cells -> histamine

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13
Q

carbs

A

glucose
- makes ATP through glycosis
- excess becomes glycogen, stored in liver or becomes fat

starch: rice, nuts, grains, roots

cellulose: all veg

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14
Q

fat

A

liver can convert b/w kinds

triglycerides/neutral fats
- 2x energy of carbs/proteins
- help absorb A D E K
- insulate, protect
- energy for muscle cells, skeletal cells, hepatocytes

fatty acids:
a. saturated: only single C bonds, max H
eg. meat, dairy

b. unsaturated: double bond Cs
eg. plant oils

essential:
linoleic, linolenic, arachidonic acid

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15
Q

protein

A

amino acids (NH2, COOH, R)
- all or nothing to make a protein
essential: taurine, arginine, glycine.

  1. complete: meat, eggs, dairy
  2. complement: legumes, grain

N balance: aminos not stored, used for protein or oxidized for energy or converted to carb/fat
- + = more protein in tissue than makes ATP
- - = protein breakdown more than in tissue
- BUN test (N packaged into urea in liver, excreted by kidney)

  • ruminants digest protein with microbes that improve the quality of protein
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16
Q

water

A

most important.
can also get through oxidizing protein/fat/carbs.
but this makes free radicals (A C E vitamins are antioxidants that disarm)

17
Q

vitamins

A

co-enzymes: keys that activate an enzyme
eg. riboflavin and niacin break down glucose

all from diet except
D (skin)
A (conversion to beta carotene)
K (intestine bacteria)

  1. water soluble
    - absorbed in GIT then peed out
    eg. C, B
  2. fat soluble
    - bind to ingesta, stored in body
    eg. A D E K [not stored]
18
Q

minerals

A

macro
micro
trace

19
Q

metabolism/catabolism

A

stage 1: GIT - hydrolysis
- protein -> amino
- carb -> glucose
- fats -> fatty acids + glycerol

stage 2: cytoplasm (anaerobic).
- pyruvic acid -> acetyl coA

stage 3: mitochondria (aerobic)
- ADP + Po4 = ATP

20
Q

anabolism

A

uses stored energy to make new molecules

metabolic turnover: constant manufacturing of new replacement molecules

energy storage: supplied by catabolism -> released when bonds break
eg. ATP, NADH, FADH2

dehydration synthesis: 2 things bond and extra H2O created
eg. poly = mono + mono
eg. fat = glycerol + fatty
eg. protein = amino + amino

21
Q

reactions

A
  1. redox: electrons removed from oxidation
    - reduction: gains e-, lost O, combines with H.
    - oxidation: lost e- and H, combined with O
  2. synthesis (anabolic)
  3. decomposition (catabolic)
  4. exchange: bonds broken and made
    eg. ATP transfers PO4 to glucose -> glucose-phosphate
22
Q

enzyme

A

act upon a substrate to create a product

co-factor: non-protein that completes for binding side
eg. iron, zinc, mg, K, ca

co-enzyme: nonprotein organic co-factors, often vitamins
- temporarily/permanently binds
eg. NAD, FAD, acetyl-coA

23
Q

enzyme activity factors

A
  1. enzyme concentration
  2. substrate concentration: levels out when saturated
  3. temperature: levels out when enzyme denatured
  4. pH: levels out at extremes (except pepsin which likes 1.5)
24
Q

clinical enzymes

A

only found in cell, in blood if damaged

alkaline phosphatase = liver/bone
amylase = pancreas
lipase = acute pancreatitis
alanine transaminase = hepatitis
aspartate transaminase = heart

assay on isozymes to pinpoint

25
enzyme reversible inhibition
a. competitive similar structure to normal substrate -> the more concentrated one winds - reversed by increasing substrate concentration eg. bacteria needs folic acid -> sulfanilamide resembles and competes -> folic acid stopped -> bacteria died b. non-competitive - no resemblance, binds elsewhere - changes substrate's shape so it doesn't bind to normal substrate anymore eg. isoleucine feedback inhibitor (end product inhibits earlier step)
26
enzyme irreversible inhibition
covalent bond with functional group of enzyme -> inactivates it eg. heavy metals combine to sulfyhydrl groups and cause neurological damage, chelating agents tightly hold on eg. penicillin inhibits enzymes (transpeptidase) bacteria needs to build cell wall
27
enzyme control mechanisms
zymogen: inactive precurose that is stored and released when needed eg. prothrombin -> thrombin genetic: adapt to environment, more enzymes made as needed allosteric regulation: enzyme combines with modulator that either activates or inhibits -> shape changes eg. isoleucine (modulator) binds to threonine deaminase and inhibits it -> total 5 enzyme reactions -> isoleucine levels are lowered, threonine deaminase active again -> more isoleucine made in response