Decreased myofibrillar proteolysis after refeeding requires dietary protein or amino acids.

Abstract

Previous studies have demonstrated that brief fasting augments and refeeding a complete diet diminishes the breakdown of myofibrillar proteins in rat skeletal muscle. The purpose of the present study was to determine which dietary component(s) was responsible for this effect and to determine the role of insulin and amino acids. Myofibrillar proteolysis was evaluated by measuring the release of 3-methylhistidine by perfused rat muscle of 1-day fasted rats and 1-day fasted rats refed for 4-24 h with a complete, protein-free, or lipid meal. For comparison, tyrosine release by perfused muscle was measured in the absence and presence of cycloheximide to evaluate net and total proteolysis, respectively. Refeeding of either diet increased plasma insulin. Despite this, myofibrillar proteolysis decreased only when protein or amino acids was included in the test meal. On the other hand, the complete or protein-free meal decreased tyrosine release in the absence but not in the presence of cycloheximide, suggesting that either diet enhanced muscle protein synthesis. Most amino acids in plasma and muscle decreased after refeeding the protein-free meal, whereas after the complete meal some amino acids in plasma and muscle increased, whereas other decreased or changed little. These results indicate that decreased myofibrillar proteolysis in muscle after refeeding of food-deprived rats requires dietary protein or amino acids. They also suggest that hormonal and/or nutritional factors other than insulin and amino acids may orchestrate this response. However, a role of amino acids cannot yet be excluded, because it is conceivable that changes in specific amino acids in plasma instead of muscle may signal diminished proteolysis.