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1 Diabetes Research Centre & Department of Endocrinology, University of Southern Denmark & Odense University Hospital, Odense, Denmark
2 Wellcome Trust Biocentre, Division of Molecular Physiology, School of Life Sciences, Dundee University, Dundee, Skotland, United Kingdom
3 Copenhagen Muscle Research Centre, Institute of Exercise and Sport Sciences, Department of Human Physiology, University of Copehagen, Copehagen, Denmark
* To whom correspondence should be addressed. E-mail: Jwojtaszewski{at}aki.ku.dk.
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-
(ACC-) were 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 (
1, 2, 1, 2, 
1, 2 and 3) in muscle of obese type 2 diabetic subjects was similar to that of control subjects. In addition, 1- and 2-associated activities of AMPK, phosphorylation of -AMPK subunits at Thr172, and phosphorylation of ACC- 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.
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