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J Appl Physiol (October 11, 2002). doi:10.1152/japplphysiol.00642.2002
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Articles in PresS, published online ahead of print October 11, 2002
J Appl Physiol, 10.1152/jap.00642.2002
Submitted on July 15, 2002
Accepted on October 7, 2002

5'AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle

Jakob N. Nielsen1*, Kirsty J. Mustard2, Drew A. Graham1, Haiyan Yu3, Christopher S. MacDonald1, Henriette Pilegaard4, Laurie J. Goodyear3, D. Grahame Hardie2, Erik A. Richter1, and Jorgen F. Wojtaszewski1

1 Copenhagen Muscle Research Centre, Institute of Exercise and Sport Sciences, University of Copenhagen, Copenhagen, Denmark
2 Wellcome Trust Biocentre, Division of Molecular Physiology, Dundee University, Dundee, United Kingdom
3 Joslin Diabetes Center, Harvard Medical School, Boston, Massachusetts, USA
4 Copenhagen Muscle Research Centre, August Krogh Institute, Copenhagen, Denmark

* To whom correspondence should be addressed. E-mail: jnnielsen{at}aki.ku.dk.

5'AMP-activated protein kinase (AMPK) has been proposed to be a pivotal factor in cellular responses to both acute exercise and exercise training. To investigate whether protein levels and gene expression of catalytic 9{alpha}1, {alpha}2) and regulatory (ß1, ß2, {gamma}1, {gamma}2, {gamma}3) AMPK subunits and exercise-induced AMPK activity are influenced by exercise training status, muscle biopsies were obtained from seven endurance exercise-trained and seven sedentary young healthy men. The {alpha}1 and {alpha}2 AMPK mRNA content in trained subjects were both 117±2 % of that in sedentary subjects (NS) whereas mRNA for {gamma}3 was 61±1% of that in sedentary (NS). The level of {alpha}1AMPK protein in trained subjects was 185±34% of that in sedentary subjects (P<0.05), while the levels of the {alpha}2, ß1, ß2, {gamma}1, {gamma}2 and {gamma}3 subunits were similar in trained and sedentary subjects. At the end of 20 min of cycle exercise at 80% of VO2peak, the increase in phosphorylation of {alpha}AMPK (Thr172) was blunted in the trained group (138±38 % above rest) compared with the sedentary group (353±63 % above rest)(P<0.05). Acetyl CoA-carboxylase (ACC) ß phosphorylation (Ser221), which is a marker for in vivo AMPK activity was increased by exercise in both groups but to a lower level in trained subjects (32±5 arbitrary units) than in sedentary controls (45±1 arbitrary units)(P<0.01). Whereas {alpha}1AMPK activity was unchanged in response to exercise in both groups, {alpha}2AMPK activity increased 110±33 % above rest in trained subjects and 184±31 % above rest in sedentary subjects (NS between trained and sedentary subjects). The phosphocreatine / (phosphocreatine+creatine)-ratio was higher in the trained group than in the sedentary group at the end of exercise (0.38±0.04 versus 0.21±0.04, P<0.05). In conclusion, trained human skeletal muscle has increased {alpha}1AMPK protein levels. Furthermore, AMPK activation during exercise is blunted in trained human skeletal muscle, probably due to a better maintenance of the energy charge, even when exercise is performed at the same relative workload.




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