Objective: The purpose of this study was to determine the acute in vivo response of human muscle protein to stress. Summary Background Data; Prior animal and human in vitro studies have suggested that physiologic stress increases muscle protein turnover. In contrast, recent publications using a polyribosomal methodology have demonstrated a reduction in human muscle protein synthesis in vivo after surgery. Methods: Five healthy volunteers were given a stable isotopic infusion of 1,213C leucine that allowed for determination of the fractional rate of muscle protein synthesis by measuring the rate of incorporation of 13C label into vastus lateralis muscle biopsies. Simultaneous infusion of 15N lysine and quantitation of leg blood flow by indocyanine green dye dilution allowed for estimation of leg muscle protein breakdown rate (Lys Ra) and synthesis rate (Lys Rd). These measurements were performed before and then at the conclusion of a 4-hour femoral arterial infusion of the catabolic hormones epinephrine, cortisol, and glucagon. Results: The catabolic hormone infusion elicited a significant (65%) increase in the leg muscle protein breakdown rate and a significant but less marked increase in the rate of muscle protein synthesis, as assessed by both an increase in the fractional rate of muscle protein synthesis of 48.5% and in lysine uptake within the leg of 32%. Conclusions: This study conclusively demonstrates that a hormonally induced stress results in a net catabolism of human muscle protein by increasing the rate of protein breakdown in excess of an increased protein synthetic rate.
|Original language||English (US)|
|Number of pages||6|
|Journal||Annals of Surgery|
|State||Published - Nov 1993|
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