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Diabetes 53:S179-S185, 2004
© 2004 by the American Diabetes Association, Inc.

Section IV: Lipid Modulators of Islet Function

Islet Complex Lipids

Involvement in the Actions of Group VIA Calcium-Independent Phospholipase A2 in ß-Cells

Sasanka Ramanadham1, Haowei Song1, Shunzhong Bao1, Fong-Fu Hsu1, Sheng Zhang1, Zhongmin Ma2, Chun Jin1, and John Turk1

1 Mass Spectrometry Resource, Division of Endocrinology, Diabetes, and Metabolism, Department of Medicine, Washington University School of Medicine, St. Louis, Missouri
2 Mount Sinai School of Medicine, New York, New York

The ß-isoform of group VIA calcium-independent phospholipase A2 (iPLA2ß) does not require calcium for activation, is stimulated by ATP, and is sensitive to inhibition by a bromoenol lactone suicide substrate. Several potential functions have been proposed for iPLA2ß. Our studies indicate that iPLA2ß is expressed in ß-cells and participates in glucose-stimulated insulin secretion but is not involved in membrane phospholipid remodeling. If iPLA2ß plays a signaling role in glucose-stimulated insulin secretion, then conditions that impair iPLA2ß functions might contribute to the diminished capacity of ß-cells to secrete insulin in response to glucose, which is a prominent characteristic of type 2 diabetes. Our recent studies suggest that iPLA2ß might also participate in ß-cell proliferation and apoptosis and that various phospholipid-derived mediators are involved in these processes. Detailed characterization of the iPLA2ß protein level reveals that ß-cells express multiple isoforms of the enzyme, and our studies involve the hypothesis that different isoforms have different functions.

Address correspondence and reprint requests to Sasanka Ramanadham, Washington University School of Medicine, Department of Medicine, Box 8127, 660 S. Euclid Ave., St. Louis, MO 63110. E-mail: sramanad{at}im.wustl.edu


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Diabetes Diabetes Care Clinical Diabetes Diabetes Spectrum
Copyright © 2004 by the American Diabetes Association.