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Am J Physiol Endocrinol Metab 286: E239-E244, 2004. First published October 7, 2003; doi:10.1152/ajpendo.00326.2003
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AMPK activity and isoform protein expression are similar in muscle of obese subjects with and without type 2 diabetes

Kurt Højlund,2,* Kirsty J. Mustard,3,* Peter Stæhr,2 D. Grahame Hardie,3 Henning Beck-Nielsen,2 Erik A. Richter,1 and Jørgen F. P. Wojtaszewski1

1Department of Human Physiology, Copenhagen Muscle Research Centre, Institute of Exercise and Sport Sciences, University of Copenhagen, DK-2100 Copenhagen; 2Diabetes Research Centre, University of Southern Denmark and Department of Endocrinology, Odense University Hospital, DK-5000 Odense, Denmark; and 3Division of Molecular Physiology, School of Life Sciences, Wellcome Trust Biocentre, Dundee University, Dundee, DD1 5EH Scotland, United Kingdom

Submitted 14 July 2003 ; accepted in final form 2 October 2003

Acute or chronic activation of AMP-activated protein kinase (AMPK) increases insulin sensitivity. Conversely, reduced expression and/or function of AMPK might play a role in insulin resistance in type 2 diabetes. Thus protein expression of the seven subunit isoforms of AMPK and activities and/or phosphorylation of AMPK and acetyl-CoA carboxylase-{beta} (ACC{beta}) was measured in skeletal muscle from obese type 2 diabetic and well-matched control subjects during euglycemic-hyperinsulinemic clamps. Protein expression of all AMPK subunit isoforms ({alpha}1, {alpha}2, {beta}1, {beta}2, {gamma}1, {gamma}2, and {gamma}3) in muscle of obese type 2 diabetic subjects was similar to that of control subjects. In addition, {alpha}1- and {alpha}2-associated activities of AMPK, phosphorylation of {alpha}-AMPK subunits at Thr172, and phosphorylation of ACC{beta} at Ser221 showed no difference between the two groups and were not regulated by physiological concentrations of insulin. These data suggest that impaired insulin action on glycogen synthesis and lipid oxidation in skeletal muscle of obese type 2 diabetic subjects is unlikely to involve changes in AMPK expression and activity.

adenosine 5'-monophosphate-activated protein kinase (EC 2.7.1.109); acetyl-CoA carboxylase-{beta} (EC 6.4.1.2); glycogen synthase (EC 2.4.1.11); protein phosphorylation


Address for reprint requests and other correspondence: J. F. P. Wojtaszewski, Copenhagen Muscle Research Centre, Dept. of Human Physiology, Institute of Exercise and Sport Sciences, Univ. of Copenhagen, 13 Universitetsparken, Copenhagen DK-2100, Denmark (E-mail: Jwojtaszewski{at}aki.ku.dk).




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