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1 Department of Human Biology, Nutrition and Toxicology Research Institute Maastricht (NUTRIM), Maastricht University, Maastricht, The Netherlands
2 School of Exercise and Nutrition Sciences, Deakin University, Burwood, Victoria, Australia
3 Department of Human Biology, Nutrition and Toxicology Research Institute Maastricht (NUTRIM), Maastricht University, Maastricht, The Netherlands; Department of Movement Sciences, Nutrition and Toxicology Research Institute Maastricht (NUTRIM), Maastricht University, Maastricht, The Netherlands
* To whom correspondence should be addressed. E-mail: R.Koopman{at}Hb.unimaas.nl.
To investigate the in vivo effects of resistance exercise on translational control in human skeletal muscle, we determined the phosphorylation of AMP activated kinase (AMPK), eukaryotic initiation factor 4E-binding protein (4E-BP1), p70/p85-S6 protein kinase (S6K1) and ribosomal S6 protein (S6). Furthermore, we investigated whether changes in the phosphorylation of S6K1 are muscle fiber-type specific. Eight male subjects performed a single high-intensity resistance exercise session. Muscle biopsies were collected before, immediately after exercise, and following 30 and 120 min of post-exercise recovery. The phosphorylation status of AMPK, 4E-BP1, S6K1 and S6 was determined by western blotting with phospho-specific and pan antibodies. To determine fiber-type specific changes in the phosphorylation status of S6K1, (immuno)fluorescence microscopy was applied. AMPK phosphorylation was increased ~3 fold immediately following resistance exercise, while 4E-BP1 phosphorylation was reduced to 27±6% of pre-exercise values. Phosphorylation of S6K1 at Thr421/Ser424 was increased 2-2.5 fold during recovery, but did not induce a significant change in S6 phosphorylation. Phosphorylation of S6K1 was more pronounced in the type II vs. type I muscle fibers. Before exercise, phosphorylated S6K1 was predominantly located in the nuclei. After 2 h of post-exercise recovery, phospho-S6K1 was primarily located in the cytosol of type II muscle fibers. We conclude that resistance exercise effectively increases the phosphorylation of S6K1 on Thr421/Ser424, which is not associated with a substantial increase in S6 phosphorylation in a fasted state.
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