{Reference Type}: Journal Article
{Title}: The Effects of Branched-Chain Amino Acids on the Akt/mTOR Pathway and Nebulin Protein in Joint Fixation-Induced Muscle Atrophy.
{Author}: Nishikawa A;Nishikawa A;Kamajiri N;Okada K;Imagita H;
{Journal}: J Nutr Sci Vitaminol (Tokyo)
{Volume}: 68
{Issue}: 2
{Year}: 2022
{Factor}: 2.032
{DOI}: 10.3177/jnsv.68.112
{Abstract}: It is well known that branched-chain amino acids (BCAAs) promote protein synthesis in skeletal muscle and can cause muscle hypertrophy. However, it has also been reported that they may inhibit muscle atrophy induced by load-bearing and age-related changes. In this study, we investigated the effects of BCAA intake during joint fixation on the levels of protein kinase B (Akt), mammalian target of rapamycin (mTOR), and nebulin in a rat model of joint fixation. Akt and mTOR are signal factors of protein synthesis, whereas nebulin is a structural protein in the muscle. The effects of BCAAs on muscle atrophy were also investigated. The phosphorylation rate of mTOR was higher than that of Akt and increased with BCAA intake in the rat hind limb muscles (soleus) when the ankle joint was fixed. The relative level of nebulin and the phosphorylation rate of Neural Wiskott-Aldrich syndrome protein (N-WASP) also increased as a result of BCAA intake during fixation. This is important because nebulin and N-WASP are involved in the formation of the structure of sarcomere thin filaments. Furthermore, when the cross-sectional areas (CSAs) of different types of muscle fibers were measured during histological evaluation of muscle atrophy, it was found that the inhibitory effect of BCAA on muscle atrophy was higher in Type 1 fibers. Additionally, a positive correlation was found between nebulin level and the CSAs of the muscle fibers. It was found that there is a close relationship between the content of structural proteins and muscle atrophy.