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Papers In Press, published online ahead of print December 22, 2004
Department of Cellular and Molecular Physiology, Pennsylvania State University, Hershey, PA 17033
Corresponding Author: jjefferson{at}psu.edu
The contribution of mTOR signaling to the resistance exercise-induced stimulation of skeletal muscle protein synthesis was assessed by administering rapamycin to Sprague-Dawley rats 2 h prior to a bout of resistance exercise. Animals were sacrificed 16 h post-exercise and gastrocnemius protein synthesis, mTOR signaling, and biomarkers of translation initiation were assessed. Exercise stimulated the rate of protein synthesis, however this effect was prevented by pre-treatment with rapamycin. The stimulation of protein synthesis was mediated by an increase in translation initiation, as exercise caused an increase in polysome aggregation that was abrogated by rapamycin administration. Taken together the data suggest the effect of rapamycin was not mediated by reduced phosphorylation of eukaryotic initiation factor (eIF) 4E binding protein (BP) 1, because exercise did not cause a significant change in 4E-BP1(Thr-70) phosphorylation, 4E-BP1-eIF4E association, or eIF4F complex assembly concomitant with increased protein synthetic rates. Alternatively, there was a rapamycin-sensitive decrease in relative eIF2B
J. Biol. Chem, 10.1074/jbc.M413732200
Submitted on December 6, 2004
Revised on December 22, 2004
Accepted on December 10, 2004
Resistance exercise increases muscle protein synthesis and translation of eukaryotic initiation factor 2B
mRNA in a mammalian target of rapamycin-dependent manner
(Ser-535) phosphorylation that was explained by a significant increase in the expression of eIF2B protein. The proportion of eIF2B mRNA in polysomes was increased following exercise, an effect that was prevented by rapamycin treatment, suggesting that the increase in eIF2B protein expression was mediated by an mTOR-dependent increase in translation of the mRNA encoding the protein. The increase in eIF2B mRNA translation and protein abundance occurred independent of similar changes in other eIF2B subunits. These data suggest a novel link between mTOR signaling and eIF2B mRNA translation that could contribute to the stimulation of protein synthesis following acute resistance exercise.
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