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Research Article Free access | 10.1172/JCI3920

Leptin inhibits insulin secretion by activation of phosphodiesterase 3B.

A Z Zhao, K E Bornfeldt, and J A Beavo

Department of Pharmacology, University of Washington, Seattle, Washington 98195, USA.

Find articles by Zhao, A. in: JCI | PubMed | Google Scholar

Department of Pharmacology, University of Washington, Seattle, Washington 98195, USA.

Find articles by Bornfeldt, K. in: JCI | PubMed | Google Scholar

Department of Pharmacology, University of Washington, Seattle, Washington 98195, USA.

Find articles by Beavo, J. in: JCI | PubMed | Google Scholar

Published September 1, 1998 - More info

Published in Volume 102, Issue 5 on September 1, 1998
J Clin Invest. 1998;102(5):869–873. https://doi.org/10.1172/JCI3920.
© 1998 The American Society for Clinical Investigation
Published September 1, 1998 - Version history
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Abstract

The molecular signaling events by which leptin exerts its functions in vivo are not well delineated. Here, we show a novel leptin signaling mechanism that requires phosphoinositide 3-kinase (PI 3-kinase)-dependent activation of cyclic nucleotide phosphodiesterase 3B (PDE3B) and subsequent suppression of cAMP levels. In pancreatic beta cells, leptin causes the activation of PDE3B, which leads to marked inhibition of glucagon-like peptide-1-stimulated insulin secretion. The effect of leptin is abolished when insulin secretion is induced with cAMP analogues that cannot be hydrolyzed by PDE3B. Selective inhibitors of PDE3B and PI 3-kinase completely prevent the leptin effect on insulin secretion and cAMP accumulation. The results demonstrate that one of the physiological effects of leptin, suppression of insulin secretion, is mediated through activation of PDE3B and suggest PDE3B as a mediator of leptin action in other tissues.

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