Protein Synthesis and Degradation Change Rapidly in Response to Food Intake in Muscle of Food-Deprived Mice ,

Abstract

The short-term changes in muscle protein synthesis and degradation after food intake are unclear. We investigated muscle protein metabolism after food intake in mice that were starved for 18 h and refed for 1 h. Protein synthesis activity was estimated by the polysome profiles, and protein degradation was estimated by plasma Nτ-methylhistidine (MeHis) concentration, reflecting translational activity and myofibrillar protein degradation, respectively. MeHis is an index of myofibrillar protein degradation because it is not reused for protein synthesis and it is not metabolized. Stimulation of protein synthesis (polysome profile) and the reduction of protein degradation (plasma Nτ-methylhistidine concentration) were observed immediately after feeding began. Protein synthesis returned to the prefeeding level by 6 h after refeeding, whereas protein degradation remained at a low level. The decreased plasma MeHis concentration after refeeding was not due to a decrease in MeHis release from muscle cells and an increase in the free MeHis pool size, because the changes in free MeHis concentration in muscle were similar to that of plasma. Plasma insulin concentration immediately rose with feeding and it returned to the prefeeding level by 3 h after refeeding. These results suggest that responses of postprandial protein metabolism are very rapid and that protein synthesis is regulated by insulin, whereas degradation is regulated by insulin and other dietary factors. Thus the ability of skeletal muscle to use nutrients more effectively by stimulating protein synthesis and reducing protein degradation may cause the accelerated rate of protein accretion in skeletal muscle during the short postprandial period.