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Skeletal muscle and exercise |
2/ß2/
3 AMPK activation during exercise in human skeletal muscle
1 Copenhagen Muscle Research Centre, Department of Human Physiology, Institute of Exercise and Sport Sciences, University of Copenhagen, Denmark
5'AMP-activated protein kinase (AMPK) is a key regulator of cellular metabolism and is regulated in muscle during exercise. We have previously established that only three of 12 possible AMPK 
/ß/
-heterotrimers are present in human skeletal muscle. Previous studies describe discrepancies between total AMPK activity and regulation of its target acetyl-CoA-carboxylase (ACC)ß. Also, exercise training decreases expression of the regulatory 3 AMPK subunit and attenuates 2 AMPK activity during exercise. We hypothesize that these observations reflect a differential regulation of the AMPK heterotrimers. We provide evidence here that only the 2/ß2/3 subunit is phosphorylated and activated during high-intensity exercise in vivo. The activity associated with the remaining two AMPK heterotrimers, 1/ß2/1 and 2/ß2/1, is either unchanged (20 min, 80% maximal oxygen uptake 
) or decreased (30 or 120 s sprint-exercise). The differential activity of the heterotrimers leads to a total -AMPK activity, that is decreased (30 s trial), unchanged (120 s trial) and increased (20 min trial). AMPK activity associated with the 2/ß2/3 heterotrimer was strongly correlated to 3-associated -Thr-172 AMPK phosphorylation (r2
= 0.84, P < 0.001) and to ACCß Ser-221 phosphorylation (r2
= 0.65, P < 0.001). These data single out the 2/ß2/3 heterotrimer as an important actor in exercise-regulated AMPK signalling in human skeletal muscle, probably mediating phosphorylation of ACCß.
(Received 12 September 2006;
accepted after revision 8 October 2006;
first published online 12 October 2006)
Corresponding author J. B Birk: Copenhagen Muscle Research Centre, Department of Human Physiology, Institute of Exercise and Sport Sciences, University of Copenhagen, 13 Universitetsparken, 2100 Copenhagen Ø, Denmark. Email: jbirk{at}ifi.ku.dk
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