Protein metabolism Flashcards

1
Q

ureagenesis

A

formation of urea from amino acids

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2
Q

atrophy

A

muscle reduction/loss

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3
Q

order of processing dietary proteins

A
  1. Stomach (hydrolysed & denatured)
    o Pepsin & hydrochloric acid initiate protein digestion
  2. Small intestine (denatured & neutralised)
    o Trypsin, Chymotrypsin, Aminopeptidase & carboxypeptidase
    o Pancreas secretes pancreatic proteases & enterocyte proteases
    o Secretin = triggers release of bicarbonate (HCO3)
    o Peptide fragments & free amino acids absorbed
  3. Liver (transportation)
    o Remaining amino acids enter hepatic portal vein & transported to the liver
    o ~40% used for ureagenesis for energy
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4
Q

rough % of protein in men vs women

A

14-16%

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5
Q

what is mTOR?

A
  • mandilion target of rapamycin
  • master controller of protein synthesis
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6
Q

function of mTOR

A

high conc. = promotes muscle growth in the body
low conc. = repair & maintenance

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7
Q

autophagy

A

recycling of damaged proteins into amino acids

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8
Q

mTOR pathway

A
  1. Amino acids sensed by muscle cell
  2. Transported across cell membrane via SNAT2 & LAT1 (membrane proteins)
  3. Amino acids stimulate protein signalling & phosphorylation via Sestrin-2 (protein)
  4. mTOR activated & translocate to the lysosome to become ‘active’
  5. mTOR phosphorylates several proteins
    o S6K1
    o RPS6
    o 4E-BP1
  6. Initiate protein translation at ribosome (mRNA) & increases protein synthesis
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9
Q

p-p70S6 Kinase

A
  • downstream regulator of mTOR post-exercise
  • essential for increasing translation
  • inducting muscle protein synthesis
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10
Q

protein muscle breakdown is driven by…

A

MuRF1 & MAFbx

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11
Q

function of MuRF1 & MAFbx

A
  • directs tagged proteins to the proteasome for degradation
  • promotion of muscular atrophy
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12
Q

net balance during fasted (during exercise) state

A
  • muscle protein breakdown > protein synthesis
  • negative net balance
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13
Q

net balance during fed (post exercise) state

A
  • protein synthesis > muscle protein breakdown
  • positive net balance
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14
Q

role of amino acids during Krebs/Citric Acid Cycle

A
  • maintain levels of specific substrates
  • maintain glucose levels
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15
Q

Transamination

A

transfer of 1 amino group from 1 molecule to another

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16
Q

enzymes used in transamination

A
  • aminotransferase = catalyses transamination
  • alpha-ketoglutarate = involved in transamination
17
Q

Deamination

A

amino acid removal & loss of its amino group

18
Q

what is produced from deamination?

A

ammonia (toxic)

19
Q

what happens to ammonia after deamination?

A

ammonia is converted into urea in the liver

20
Q

3 amino acids which bypass degradation by the liver

A
  • leucine
  • isoleucine
  • valine
21
Q

Cori Cycle (lactate)

A
  1. Lactate produced by anaerobic glycolysis in muscles
  2. Transported to the liver & converted to glucose
  3. Returns to the muscles & cyclically metabolized back to lactate
22
Q

The Glucose-Alanine Cycle (Alanine)

A
  1. Pyruvate forms amino acid acceptor (transamination)  forms alanine
  2. Alanine transported to the liver & converted to pyruvate & glutamate (used via citric acid cycle)
  3. Glucose then transported back to the muscle
23
Q

4 steps in the conversion of ammonia to carbamoyl phophate

A
  1. Ammonia + Ornithine  Citrulline
  2. Citrulline converted to arginine succinate
  3. Arginine succinate  arginine + fumarate
  4. Arginine hydrolysed via arginase  urea