Overnight branched-chain amino acid infusion causes sustained suppression of muscle proteolysis

Protective effect of branched chain amino acids on hindlimb suspension-induced muscle atrophy in growing rats

“…In this study, we found that BCAA did not increase the Akt1 and mTOR mRNA levels compared to the hindlimb suspension group. This result agrees with some human studies showing that infusion of BCAA suppressed muscle protein breakdown without increasing protein synthesis, although species differences may be present [39][40]. In contrast with our results, leucine increased the phosphorylation of Akt and mTOR against denervation induced muscle atrophy in middle aged rats [29].…”

A leucine-supplemented diet improved protein content of skeletal muscle in young tumor-bearing rats

“…The trigger for the increased leucine oxidation remains unknown. Interestingly, diets containing different proportions of BCAA have shown important beneficial effects on the metabolic changes associated with muscle protein wasting (6). The use of BCAA-enriched total parenteral nutrition in patients with intra-abdominal adenocarcinomas showed an increase in whole body protein synthesis or improved leucine kinetics, fractional albumin synthesis rates, and leucine balance, indicating a favorable influence on protein metabolism (18).…”

“…Louard et al (6) showed that different proportions of dietary BCAA had important beneficial effects on the metabolic changes associated with muscle wasting.…”

Possible Involvement of Calcium Signaling Pathways inL-Leucine-Stimulated Protein Synthesis in L6 Myotubes

“…Among these regulatory factors, amino acids, in particular the branched-chain amino acids (BCAAs: leucine, isoleucine, and valine), are known to exert powerful regulatory influences on protein turnover. [1][2][3] We have reported that L-leucine stimulated protein synthesis in RLC-16 hepatocytes 4) and L6 myotubes cultured in L-leucine-deficient media. 5) Under L-leucine-deficient conditions, D-leucine did not exert such an effect.…”