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Am J Physiol Endocrinol Metab 286: E411-E417, 2004. First published November 12, 2003; doi:10.1152/ajpendo.00317.2003
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5'-AMP-activated protein kinase activity and protein expression are regulated by endurance training in human skeletal muscle

Christian Frøsig,1 Sebastian B. Jørgensen,1 D. Grahame Hardie,2 Erik A. Richter,1 and Jørgen F. P. Wojtaszewski1

1Copenhagen Muscle Research Centre, Institute of Exercise and Sport Sciences, University of Copenhagen, DK-2100 Copenhagen, Denmark; and 2Wellcome Trust Biocentre, Division of Molecular Physiology, Faculty of Life Sciences, University of Dundee, DD1 4HN Dundee, Scotland, United Kingdom

Submitted 10 July 2003 ; accepted in final form 4 November 2003

The 5'-AMP-activated protein kinase (AMPK) is proposed to be involved in signaling pathways leading to adaptations in skeletal muscle in response to both a single exercise bout and exercise training. This study investigated the effect of endurance training on protein content of catalytic ({alpha}1, {alpha}2) and regulatory ({beta}1, {beta}2 and {gamma}1, {gamma}2, {gamma}3) subunit isoforms of AMPK as well as on basal AMPK activity in human skeletal muscle. Eight healthy young men performed supervised one-legged knee extensor endurance training for 3 wk. Muscle biopsies were obtained before and 15 h after training in both legs. In response to training the protein content of {alpha}1, {beta}2 and {gamma}1 increased in the trained leg by 41, 34, and 26%, respectively ({alpha}1 and {beta}2 P < 0.005, {gamma}1 P < 0.05). In contrast, the protein content of the regulatory {gamma}3-isoform decreased by 62% in the trained leg (P = 0.01), whereas no effect of training was seen for {alpha}2, {beta}1, and {gamma}2. AMPK activity associated with the {alpha}1- and the {alpha}2-isoforms increased in the trained leg by 94 and 49%, respectively (both P < 0.005). In agreement with these observations, phosphorylation of {alpha}-AMPK-(Thr172) and of the AMPK target acetyl-CoA carboxylase-{beta}(Ser221) increased by 74 and 180%, respectively (both P < 0.001). Essentially similar results were obtained in four additional subjects studied 55 h after training. This study demonstrates that protein content and basal AMPK activity in human skeletal muscle are highly susceptible to endurance exercise training. Except for the increase in {gamma}1 protein, all observed adaptations to training could be ascribed to local contraction-induced mechanisms, since they did not occur in the contralateral untrained muscle.

5'-adenosine monophosphate; acetyl-coenzyme A carboxylase-{beta}


Address for reprint requests and other correspondence: C. Frøsig, Copenhagen Muscle Research Centre, Dept. of Human Physiology, Institute of Exercise and Sport Sciences, Univ. of Copenhagen, 13 Universitetsparken, DK-2100 Copenhagen, Denmark (E-mail: Cfrosig{at}ifi.ku.dk).




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