liver physiology Flashcards

1
Q

how much bile is secreted per day?

A

250ml-1000ml

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2
Q

what are the functions of ITO cells?

A

secretion of the extracellular matrix of the space of disse. storage of fat and fat soluble vitamins.

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3
Q

name some of the channels involved in canaliculi secretion.

A

MDR1-MDR3 cMOAT

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4
Q

describe the journey of bile salts.

A

produced in the liver, released in bile, reabsorbed by gut in jejunum but mainly terminal ileum and then conjugated in liver to amino acids.

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5
Q

what is bile made of?

A

water, bile salts, cholesterol + lecithin and bilirubin.

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6
Q

how are bile salts kept in the gallbladder?

A

arranged in micelles so that they don’t damage the gallbladder.

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7
Q

what increases bile viscosity?

A

mucin.

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8
Q

describe the metabolism of amino acids?

A

cannot be stored because ineffective energy source. they are deaminated to form a-keto acids. glutamate is deaminated for form a-ketoglutarate and fed into the krebs cycle. NH4+ gets excreted

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9
Q

how is a-ketoglutamate formed?

A

deamination of glutamate.

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10
Q

how is pyruvate formed?

A

deamination of alanine from muscle.

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11
Q

describe the glucose alanine cycle.

A

in muscle, glucose in converted to pyruvate via glycolysis. glycolysis is aminated to form alanine. in this process, glutamate is deaminated to a-ketoglutarate in the presence of the enzyme alanine aminotransferase, and the NH4+ is transferred to pyruvate to form alanine. alanine then travels in the blood to the liver where it is deaminated to form pyruvate again. during this process a-ketoglutarate is aminated to form glutamate, this process also uses alanine aminotransferase. the NH4+ is then put into the urea cycle. the pyruvate formed undergoes gluconeogenesis to form glucose again which gets transported to muscle.

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12
Q

how much albumin is produced per day? where does it go?

A

10g. it travels in the interstitium into lymph and into the thoracic duct to be empties into the left subclavian vein.

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13
Q

what is albumins half life? how many binding sites does it have?

A

16-18 hours. 4, all with difference specific binding sites.

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14
Q

which clotting factors are produced by the liver?

A

all but von willebrand.

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15
Q

what are microsomal enzymes? where are they found?

A

monooxydases. they can oxidise, reduce, or hydrolyse, and glucuronidation. CP450. smooth ER

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16
Q

what are nonmicrosomal enzymes? where are they found?

A

cytoplasm/mitochondria of hepatocytes. protein oxidases, esterases or conjugates.

17
Q

what is phase 1 of detoxification?

A

phase 1 - cytochrome p450. xenobiotic is oxidised. results in some loss of function of the drug, can still be active. the reaction is non-synthetic. end result is a new/modified functional group.

18
Q

what is phase 2 of detoxification?

A

conjugation. this reaction is synthetic. it is the attachment of an ionised group to completely inactivate the molecule e.g. methyl or acetyl group. makes it more soluble.

19
Q

what does it mean to say that a reaction is synthetic?

A

produces a soluble compound that can be excreted in urine/faeces.

20
Q

what is glucuronisation?

A

most common conjugation reaction in which glucuronic acid is added to the xenobiotic. BILIRUBIN!!!!!

21
Q

what are vitamin A, C, B, D used for/deficiency?

A

A = retanoids, for seeing in dark. C = for synthesis of neurotransmitters. B = nucleic acid production. D = calcium metabolism.

22
Q

what is BMR equivalent to? how is it measured?

A

ATP useage. O2 uptake

23
Q

what do the brain, RBCs and liver use for energy?

A

brain = ketone bodies and glucose. RBCs use glucose. liver uses glucose, fatty acids, alcohol, AAs.

24
Q

what is the total energy expenditure?

A

60% resting, 30% activity induced and 10% dietary. 70% is from fats and 30% is from carbs.

25
Q

how mud protein do adults turn over per day? secrete? how much reabsorbed?

A

1-2% of total body weight. 20-30g. 80% reabsorbed, 20% excreted.

26
Q

what are the two types of degradation of proteins?

A

lysosomal/nonlysosomal.

27
Q

describe lysosomal degradation of proteins.

A

reticuloendothelial system of the liver. protein diffuses through the fenestrations of the capillaries and kupffer cells engulf and degrade by releasing hydrolytic enzymes.

28
Q

describe nonlysosomal degradation of proteins.

A

when proteins have reached their half life or have been part of a catalytic reaction, part of the protein called a PEST sequence may be exposed. this exposure causes ubiquitin to bin, a process called ubiquitinisation. this protein is then ‘tagged’ for protein degradation. the protein is taken to a proteasome where it is degraded by proteases. a pest sequence contains proline, glutamic acid, serene and threonine.