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Resistance exercise training induces skeletal muscle hypertrophy, but repeated bouts gradually attenuate this anabolic effect. Attenuation of mechanistic target of rapamycin complex 1 (mTORC1) activation by repetitive resistance exercise is involved in this process, but the mechanism leading to inactivation of mTORC1 remains unclear. In this study, we investigated repetition-dependent changes in mitogen-activated protein kinases (MAPKs) and the 90-kDa ribosomal S6 kinase (p90RSK), upstream regulators of mTORC1, in a rat resistance-exercise model. Resistance exercise was associated with increased phosphorylation of 70-kDa ribosomal protein S6 kinase (Thr389), but its magnitude was decreased with repeated bouts. Additionally, phosphorylation of extracellular signal-regulated kinase (ERK) 1/2 (Thr202/Tyr204) and p38 MAPK (Thr180/Tyr182), which are MAPKs, decreased with repeated bouts. A similar result was also observed for p90RSK phosphorylation (Thr573). These observations indicate that repeated bouts desensitized ERK1/2 and p38 MAPK, subsequently attenuating p90RSK phosphorylation. This reduction in p90RSK phosphorylation may have been partly responsible for the blunting of mTORC1 activation by resistance exercise.
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