Protein metabolism Flashcards
ureagenesis
formation of urea from amino acids
atrophy
muscle reduction/loss
order of processing dietary proteins
- Stomach (hydrolysed & denatured)
o Pepsin & hydrochloric acid initiate protein digestion - 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 - Liver (transportation)
o Remaining amino acids enter hepatic portal vein & transported to the liver
o ~40% used for ureagenesis for energy
rough % of protein in men vs women
14-16%
what is mTOR?
- mandilion target of rapamycin
- master controller of protein synthesis
function of mTOR
high conc. = promotes muscle growth in the body
low conc. = repair & maintenance
autophagy
recycling of damaged proteins into amino acids
mTOR pathway
- Amino acids sensed by muscle cell
- Transported across cell membrane via SNAT2 & LAT1 (membrane proteins)
- Amino acids stimulate protein signalling & phosphorylation via Sestrin-2 (protein)
- mTOR activated & translocate to the lysosome to become ‘active’
- mTOR phosphorylates several proteins
o S6K1
o RPS6
o 4E-BP1 - Initiate protein translation at ribosome (mRNA) & increases protein synthesis
p-p70S6 Kinase
- downstream regulator of mTOR post-exercise
- essential for increasing translation
- inducting muscle protein synthesis
protein muscle breakdown is driven by…
MuRF1 & MAFbx
function of MuRF1 & MAFbx
- directs tagged proteins to the proteasome for degradation
- promotion of muscular atrophy
net balance during fasted (during exercise) state
- muscle protein breakdown > protein synthesis
- negative net balance
net balance during fed (post exercise) state
- protein synthesis > muscle protein breakdown
- positive net balance
role of amino acids during Krebs/Citric Acid Cycle
- maintain levels of specific substrates
- maintain glucose levels
Transamination
transfer of 1 amino group from 1 molecule to another
enzymes used in transamination
- aminotransferase = catalyses transamination
- alpha-ketoglutarate = involved in transamination
Deamination
amino acid removal & loss of its amino group
what is produced from deamination?
ammonia (toxic)
what happens to ammonia after deamination?
ammonia is converted into urea in the liver
3 amino acids which bypass degradation by the liver
- leucine
- isoleucine
- valine
Cori Cycle (lactate)
- Lactate produced by anaerobic glycolysis in muscles
- Transported to the liver & converted to glucose
- Returns to the muscles & cyclically metabolized back to lactate
The Glucose-Alanine Cycle (Alanine)
- Pyruvate forms amino acid acceptor (transamination) forms alanine
- Alanine transported to the liver & converted to pyruvate & glutamate (used via citric acid cycle)
- Glucose then transported back to the muscle
4 steps in the conversion of ammonia to carbamoyl phophate
- Ammonia + Ornithine Citrulline
- Citrulline converted to arginine succinate
- Arginine succinate arginine + fumarate
- Arginine hydrolysed via arginase urea