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Molecular & Cellular Proteomics 1:509-516, 2002.
© 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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Geneva Proteomics Center, Central Clinical Chemistry Laboratory, Geneva University Hospital, 1211 Geneva 14, Switzerland
¶ Clore Laboratory, School of Science, University of Buckingham, Buckingham MK18 1EG, United Kingdom
The insulin sensitizer drug, rosiglitazone, has been shown to have a protective effect on pancreatic islet cell structure and function in animal models of type 2 diabetes. The identification of new molecular targets associated both with islet cell dysfunction and protection is a crucial research goal. In the present study, a proteomics approach has been used to identify such targets. Obese C57Bl/6J lep/lep mice and lean littermates were given the insulin sensitizer drug BRL49653, rosiglitazone. It normalized the impaired glucose tolerance in lep/lep mice but had no significant effect on glucose tolerance in the lean mice. Pancreatic islet polypeptides were arrayed by a two-dimensional gel electrophoresis system that separated more than 2500 individual spots. Three overexpressed and six underexpressed proteins were significant (p < 0.05) between lep/lep and lean mice, and four were modulated significantly (p < 0.05) by the rosiglitazone treatment of the obese mice. The identity of these differentially expressed proteins was made using mass spectrometric analysis and provided evidence that differential expression of actin-binding proteins may be an important aspect of defective islet function. Rosiglitazone increased carboxypeptidase B expression in both lep/lep and normal mice suggesting that this might be an independent effect of rosiglitazone that contributes to improved insulin processing.
To whom correspondence should be addressed: Geneva Proteomics Center, Central Clinical Chemistry Laboratory, Geneva University Hospital, 24 rue Micheli-du-Crest, 1211 Geneva 14, Switzerland. Tel.: 41-22-372-73-74; Fax: 41-22-372-73-99; E-mail: sanchez{at}dim.hcuge.ch
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