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Diabetes 53:53-60, 2004
© 2004 by the American Diabetes Association, Inc.

PKC{alpha} Is Activated But Not Required During Glucose-Induced Insulin Secretion From Rat Pancreatic Islets

Lee Carpenter1, Christopher J. Mitchell1, Zheng Z. Xu2, Philip Poronnik3, Gerald W. Both2, and Trevor J. Biden1

1 Garvan Institute of Medical Research, St. Vincents Hospital, and Department of Medicine, University of New South Wales, Sydney, Australia
2 CSIRO Molecular Science, North Ryde, Sydney, Australia
3 Department of Physiology, University of Sydney, and School of Biomedical Sciences, University of Queensland, Australia

The role of protein kinase C (PKC) in glucose-stimulated insulin secretion (GSIS) is controversial. Using recombinant adenoviruses for overexpression of PKC{alpha} and PKC{delta}, in both wild-type (WT) and kinase-dead (KD) forms, we here demonstrate that activation of these two PKCs is neither necessary nor sufficient for GSIS from batch-incubated, rat pancreatic islets. In contrast, responses to the pharmacologic activator 12-O-tetradecanoylphorbol-13-acetate (TPA) were reciprocally modulated by overexpression of the PKC{alpha}WT or PKC{alpha}KD but not the corresponding PKC{delta} adenoviruses. The kinetics of the secretory response to glucose (monitored by perifusion) were not altered in either cultured islets overexpressing PKC{alpha}KD or freshly isolated islets stimulated in the presence of the conventional PKC (cPKC) inhibitor Go6976. However, the latter did inhibit the secretory response to TPA. Using phosphorylation state-specific antisera for consensus PKC phosphorylation sites, we also showed that (compared with TPA) glucose causes only a modest and transient functional activation of PKC (maximal at 2–5 min). However, glucose did promote a prolonged (15 min) phosphorylation of PKC substrates in the presence of the phosphatase inhibitor okadaic acid. Overall, the results demonstrate that glucose does stimulate PKC{alpha} in pancreatic islets but that this makes little overall contribution to GSIS.

Address correspondence and reprint requests to Dr. Trevor Biden, Cell Signalling Group, Garvan Institute of Medical Research, 384 Victoria St., Darlinghurst, Sydney 2010, Australia. E-mail: t.biden{at}garvan.org.au


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