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1 Copenhagen Muscle Research Centre, Institute of Exercise and Sport Sciences, University of Copenhagen, Copenhagen, Denmark
2 Wellcome Trust Biocentre, Division of Molecular Physiology, Faculty of Life Sciences, University of Dundee, Dundee, Scotland, United Kingdom
* To whom correspondence should be addressed. E-mail: Cfrosig{at}ifi.ku.dk.
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 (
1,
2) and regulatory (
1,
2 and
1,
2,
3) subunit isoforms of
AMPK as well as on basal AMPK activity in human skeletal muscle. Eight young healthy
men performed supervised one-legged knee extensor endurance training for three weeks.
Muscle biopsies were obtained before and 15 hours after training in both legs. In
response to training the protein content of
1,
2 and
1 increased in the trained leg by
41%, 34% and 26%, respectively (
1 and
2 P<0.005;
1 P<0.05). In contrast, the protein
content of the regulatory
3 isoform decreased by 62% in the trained leg (P=0.01), while no
effect of training was seen for
2,
1 and
2. AMPK activity associated with the
1 and the
2 isoforms increased in the trained leg by 94% and 49%, respectively (both, P<0.05 ). In
agreement with these observations, phosphorylation of
-AMPK(Thr172) and of the known
AMPK target acetyl-CoA carboxylase-
(Ser221) increased by 74% and 180%, respectively
(both, P<0.001). This study demonstrates that protein content and basal AMPK activity in
human skeletal muscle is highly susceptible to endurance exercise training. Except for the
increase in
1 protein, all observed adaptations to training could be ascribed to local
contraction-induced mechanisms, since they did not occur in the contra-lateral untrained
muscle.
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