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Am J Physiol Endocrinol Metab (January 24, 2006). doi:10.1152/ajpendo.00530.2005
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Submitted on November 2, 2005
Accepted on January 17, 2006

The increase in S6K1 phosphorylation in human skeletal muscle following resistance exercise occurs mainly in type II muscle fibers

Rene Koopman1*, Antoine H.G. Zorenc1, Rudy J.J. Gransier1, David Cameron-Smith2, and Luc J.C. van Loon3

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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