Objective The purpose of this study was to determine the acute in vivo
response of human muscle protein to stress. Summary Background Data P
rior animal and human in vitro studies have suggested that physiologic
stress increases muscle protein turnover. In contrast, recent publica
tions 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 1,2C-13 le
ucine that allowed for determination of the fractional rate of muscle
protein synthesis by measuring the rate of incorporation of C-13 label
into vastus lateralis muscle biopsies. Simultaneous infusion of N-15
lysine and quantitation of leg blood flow by indocyanine green dye dil
ution allowed for estimation of leg muscle protein breakdown rate (Lys
Ra) and synthesis rate (Lys Rd). These measurements were performed be
fore 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 ma
rked 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 st
udy 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.