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Originally published In Press as doi:10.1074/jbc.M212881200 on January 16, 2003

J. Biol. Chem., Vol. 278, Issue 12, 10436-10442, March 21, 2003
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Proteome Analysis Reveals Phosphorylation of ATP Synthase beta -Subunit in Human Skeletal Muscle and Proteins with Potential Roles in Type 2 Diabetes*

Kurt HøjlundDagger , Krzysztof Wrzesinski§, Peter Mose Larsen§, Stephen J. Fey§, Peter Roepstorff, Aase HandbergDagger , Flemming Dela||, Jørgen Vinten**, James G. McCormackDagger Dagger , Christine ReynetDagger Dagger , and Henning Beck-NielsenDagger §§

From the Dagger  Diabetes Research Centre, Department of Endocrinology, Odense University Hospital, DK-5000 Odense C § Centre for Proteome Analysis and  Department of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense M, || Copenhagen Muscle Research Centre, Department of Medical Physiology and ** Department of Physiology, Panum Institute, University of Copenhagen, N DK-2200 Copenhagen N, and Dagger Dagger  Novo Nordisk A/S, DK-2880 Bagsværd, Denmark

Insulin resistance in skeletal muscle is a hallmark feature of type 2 diabetes. An increasing number of enzymes and metabolic pathways have been implicated in the development of insulin resistance. However, the primary cellular cause of insulin resistance remains uncertain. Proteome analysis can quantitate a large number of proteins and their post-translational modifications simultaneously and is a powerful tool to study polygenic diseases like type 2 diabetes. Using this approach on human skeletal muscle biopsies, we have identified eight potential protein markers for type 2 diabetes in the fasting state. The observed changes in protein expression indicate increased cellular stress, e.g. up-regulation of two heat shock proteins, and perturbations in ATP (re)synthesis and mitochondrial metabolism, e.g. down-regulation of ATP synthase beta -subunit and creatine kinase B, in skeletal muscle of patients with type 2 diabetes. Phosphorylation appears to play a key, potentially coordinating role for most of the proteins identified in this study. In particular, we demonstrated that the catalytic beta -subunit of ATP synthase is phosphorylated in vivo and that the levels of a down-regulated ATP synthase beta -subunit phosphoisoform in diabetic muscle correlated inversely with fasting plasma glucose levels. These data suggest a role for phosphorylation of ATP synthase beta -subunit in the regulation of ATP synthesis and that alterations in the regulation of ATP synthesis and cellular stress proteins may contribute to the pathogenesis of type 2 diabetes.

* This work was supported in part by grants from the Danish Research Agency (Technology by Highly Oriented Research) (9700893), the Danish Diabetes Association, the Institute of Clinical Research, University of Southern Denmark, and the Danish National Research Foundation (504-14). Part of this work was performed in the frame of the Danish Biotechnology Instrument Centre.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§§ To whom correspondence should be addressed: Diabetes Research Centre, Dept. of Endocrinology, Odense University Hospital, Kloevervaenget 6, Odense C DK-5000, Denmark. Tel.: 45-65-41-34-44; Fax: 45-65-91-96-53; E-mail: henning.beck-nielsen@ouh.fyns-amt.dk.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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