Branched-chain amino acids administration suppresses endurance exercise-related activation of ubiquitin proteasome signaling in trained human skeletal muscle

Evgeny A. Lysenko, Tatiana F. Vepkhvadze, Egor M. Lednev, Olga L. Vinogradova, Daniil V. Popov

We tested whether post exercise ingestion of branched-chain amino acids (BCAA < 10 g) is sufficient to activate signaling associated with muscle protein synthesis and suppress exercise-induced activation of mechanisms associated with proteolysis in endurance-trained human skeletal muscle. Nine endurance-trained athletes performed a cycling bout with and without BCAA ingestion (0.1 g/kg). Post exercise ACC(Ser79/222) phosphorylation (endogenous marker of AMPK activity) was increased (~3-fold, P < 0.05) in both sessions. No changes were observed in IGF1 mRNA isoform expression or phosphorylation of the key anabolic markers - p70S6K1(Thr389) and eEF2(Thr56) - between the sessions. BCAA administration suppressed exercise-induced expression of mTORC1 inhibitor DDIT4 mRNA, eliminated activation of the ubiquitin proteasome system, detected in the control session as decreased FOXO1(Ser256) phosphorylation (0.83-fold change, P < 0.05) and increased TRIM63 (MURF1) expression (2.4-fold, P < 0.05). Therefore, in endurance-trained human skeletal muscle, post exercise BCAA ingestion partially suppresses exercise-induced expression of PGC-1a mRNA, activation of ubiquitin proteasome signaling, and suppresses DDIT4 mRNA expression.