Whole-body leucine and muscle protein kinetics in rats fed varying protein intakes.

Whole-body leucine kinetics and rectus muscle synthetic rates were evaluated in postabsorptive rats fed semipurified diets that varied in the casein content. Rats were allowed to consume ad libitum a 2% casein diet or were pair-fed or ad libitum-fed 6, 20, or 40% casein diets for 14 days. After overnight starvation, rates of whole-body leucine kinetics and rectus muscle synthetic rates were determined with a 2-h constant intravenous infusion of L-[1-14C]leucine. The postabsorptive response to inadequate protein intakes included a significant reduction in the release of leucine from whole-body protein degradation as well as subsequent reutilization for protein synthesis. In contrast, dietary protein intake at levels greater than required for maximal growth were not associated with any increases in leucine incorporation into whole-body protein or muscle fractional synthetic rates. Rates of whole-body leucine oxidation based on plasma leucine specific radioactivities underestimated total oxidation by 22-27%, and this was relatively constant as the protein component of the diet was varied. In addition, the muscle acid-soluble leucine specific radioactivity was similar to the plasma alpha-ketoisocaproate enrichment, regardless of dietary protein intake.