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2
2
1 but not
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3 AMPK trimeric complex in skeletal muscle during exercise in humans
1 Institute of Exercise and Sport Sciences; Department of Human Physiology, University of Copenhagen, Copenhagen, Denmark
* To whom correspondence should be addressed. E-mail: jwojtaszewski{at}aki.ku.dk.
We investigated time- and intensity-dependent effects of exercise on AS160 phosphorylation in human skeletal muscle. Subjects performed cycle exercise for 1) 90 min (67% VO2peak, n=8), 2) 20 min (80% VO2peak, n=11), 3) two min (110% of peak work rate, n=9), or 4) 30 sec (maximal sprint, n=10). Muscle biopsies were obtained before, during and after exercise. In trial 1, AS160 phosphorylation increased at 60 min (60%, p=0.06) and further at 90 min of exercise (120%, p<0.05).
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2
3 AMPK activity increased significantly to a steady state level after 30 min, whereas
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1 AMPK activity increased after 60 min of exercise with a further significant increase after 90 min.
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1 AMPK activity and AS160 phosphorylation correlated positively (r2=0.55). In exercise trials 2, 3, and 4,
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2
3 AMPK activity but neither AS160 phosphorylation nor
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1 AMPK activity increased. Akt Ser-473 phosphorylation was unchanged in all trials whereas Akt Thr-308 phosphorylation increased significantly in trial 3 and 4 only. These results show that AS160 is phosphorylated in a time but not intensity dependent manner, and suggest that
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2
1 AMPK may act in a pathway responsible for exercise-induced AS160 phosphorylation. Furthermore, we show that AMPK complexes in skeletal muscle are activated differently depending on exercise intensity and duration.
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