Association between myosin heavy chain protein isoforms and intramuscular anabolic signaling following resistance exercise in trained men

训练有素的男性进行抗阻运动后,肌球蛋白重链蛋白亚型与肌内合成代谢信号之间的关联

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Abstract

Resistance exercise stimulates an increase in muscle protein synthesis regulated by intracellular anabolic signaling molecules in a mammalian/mechanistic target of rapamycin (mTOR)-dependent pathway. The purpose of this study was to investigate acute anabolic signaling responses in experienced, resistance-trained men, and to examine the association between myosin heavy chain (MHC) isoform composition and the magnitude of anabolic signaling. Eight resistance-trained men (24.9 ± 4.3 years; 91.2 ± 12.4 kg; 176.7 ± 8.0 cm; 13.3 ± 3.9 body fat %) performed a whole body, high-volume resistance exercise protocol (REX) and a control protocol (CTL) in a balanced, randomized order. Participants were provided a standardized breakfast, recovery drink, and meal during each protocol. Fine needle muscle biopsies were completed at baseline (BL), 2 h (2H) and 6 h post-exercise (6H). BL biopsies were analyzed for MHC isoform composition. Phosphorylation of proteins specific to the Akt/mTOR signaling pathway and MHC mRNA expression was quantified. Phosphorylation of p70S6k was significantly greater in REX compared to CTL at 2H (P = 0.04). MHC mRNA expression and other targets in the Akt/mTOR pathway were not significantly influenced by REX. The percentage of type IIX isoform was inversely correlated (P < 0.05) with type I and type IIA MHC mRNA expression (r = -0.69 to -0.93). Maximal strength was also observed to be inversely correlated (P < 0.05) with Type I and Type IIA MHC mRNA expression (r = -0.75 to -0.77) and p70S6k phosphorylation (r = -0.75). Results indicate that activation of p70S6k occurs within 2-h following REX in experienced, resistance-trained men. Further, results also suggest that highly trained, stronger individuals have an attenuated acute anabolic response.

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