Protein Metabolism in Insulin-Dependent Diabetes Mellitus

Endocrine Research Unit, Mayo Clinic and Foundation, Rochester, MN

Patients with insulin-dependent diabetes are in a catabolic state without insulin replacement. The mechanism of insulin's anticatabolic effect has been investigated in whole-body and regional tracer kinetic studies. Whole-body studies have demonstrated that there are increases in both protein breakdown and protein synthesis during insulin deprivation. Because the magnitude of the increase in protein breakdown is greater than the magnitude of the increase in protein synthesis, there is a net protein loss during insulin deprivation. Regional studies have shown that insulin replacement inhibits protein breakdown and synthesis in splanchnic tissue but only inhibits protein breakdown in skeletal muscle. Because the increase in protein synthesis in splanchnic tissues is greater than the increase in protein breakdown, insulin deprivation results in a net accretion of protein in the splanchnic bed. In contrast, in skeletal muscle, there is a net increase in protein breakdown during insulin deprivation, resulting in a net release of amino acids. There are no human data concerning the site of protein accretion in the splanchnic bed or the specific protein whose synthesis is increased during insulin deprivation. It appears that insulin exerts its overall anticatabolic effect in insulin-dependent diabetes mainly through the inhibition of muscle protein breakdown.

The Journal of Nutrition Vol. 128 No. 2 February 1998, pp. 323S-327S
Copyright ©1998 by the American Society for Nutritional Sciences

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