Post-prandial protein metabolism

• Published in: Baillière's clinical endocrinology and metabolism 1996-10, Vol.10 (4), p.533-549
• Main Authors: Millward, D. Joe, Fereday, Amelia, Gibson, Neil R., Pacy, Paul J.
• Format: Article
• Language: English
• Subjects: Amino Acids - metabolism; Humans; Postprandial Period - physiology; Proteins - metabolism
• ISSN: 0950-351X; 1878-0881
• DOI: 10.1016/S0950-351X(96)80696-3

Current post-prandial studies of amino acid metabolism and utilization are consistent with a feeding mechanism mediated primarily by insulin and amino acids, with the balance between protein conservation and net deposition dependent on the amino acid supply. [1- 13c]leucine post-prandial kinetic tracer studies of leucine oxidation, non-oxidative disappearance and endogenous appearance allow study of the regulation of whole-body amino acid oxidation, protein synthesis and proteolysis. On the basis of these studies it appears that for leucine oxidation, the main determinant of the efficiency of protein utilization, the overriding regulatory influence is substrate availability rather than insulin. Such substrate sensitivity is manifest throughout the physiological range of insulin down to the lowest insulin levels observed suggesting that a basal insulin need is not an important part of regulation of this important catabolic pathway. The key protein turnover response is an inhibition of proteolysis sufficient to limit any increases in amino acid levels thus limiting any increase in amino acid oxidation. It appears that the influences of amino acids and insulin on proteolysis are separate and additive and may both be receptor mediated so that extracellular amino acid levels can regulate intracellular levels. It is likely that protein synthesis is regulated by intracellular amino acid levels but post-prandial stimulation through increases in amino acid levels appears to be unhelpful because of parallel increases in amino acid oxidation. Evidence for any influence of insulin on protein synthesis has yet to be unequivocally identified.