Insulin action on protein metabolism.
On the basis of the preceding observations, the following sequence of events can be postulated during insulin deficiency or excess. The main feature of insulin deficiency is the disruption of protein balance in muscle that rapidly leads to emaciation and wasting. Muscle protein degradation is greatly enhanced while increased amino acid availability maintains protein synthesis. In splanchnic tissues, both degradation and synthesis are increased but with an altered pattern, so that the levels of some proteins are increased (e.g. proteins of the acute-phase response), while those of others are decreased (e.g. albumin). As a result, intracellular protein content in liver is maintained but secretion of plasma proteins is abnormal. In healthy subjects, an acute increase in insulin concentration, as occurs after a meal, leads to a rapid suppression of protein breakdown in the splanchnic area. If hyperinsulinaemia is not supported by an exogenous amino acid supply, as might occur during a protein-free meal or experimentally during euglycaemic hyperinsulinaemic clamping, the plasma as well as muscle free amino acid concentration drops, owing to reduced splanchnic release. With reduced amino acid availability, insulin is not anabolic in muscle. If amino acid concentrations are maintained at normal or high levels, e.g. following a mixed meal, a net protein deposition in muscle may occur, primarily because of a stimulation of synthesis and possibly owing to inhibition of breakdown.
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Shriners Burns Institute, Galveston, TX 77550.
Wolfe
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D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D001692:Biological Transport; D003920:Diabetes Mellitus / Q000503:physiopathology; D006801:Humans; D007328:Insulin / Q000502:physiology*; D007333:Insulin Resistance; D009132:Muscles / Q000502:physiology; D011506:Proteins / Q000378:metabolism*; D051381:Rats
D000596:Amino Acids; D007328:Insulin; D011506:Proteins