Expression and regulation of cyclic nucleotide phosphodiesterases in human and rat pancreatic islets.

As shown by transgenic mouse models and by using phosphodiesterase 3 (PDE3) inhibitors, PDE3B has an important role in the regulation of insulin secretion in pancreatic β-cells. However, very little is known about the regulation of the enzyme. Here, we show that PDE3B is activated in response to hig...

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Main Authors: Emilia Heimann, Helena A Jones, Svante Resjö, Vincent C Manganiello, Lena Stenson, Eva Degerman
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2010-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC2995729?pdf=render
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spelling doaj-8cc7946781f34417b2248ac3b121c8122020-11-25T02:36:25ZengPublic Library of Science (PLoS)PLoS ONE1932-62032010-01-01512e1419110.1371/journal.pone.0014191Expression and regulation of cyclic nucleotide phosphodiesterases in human and rat pancreatic islets.Emilia HeimannHelena A JonesSvante ResjöVincent C ManganielloLena StensonEva DegermanAs shown by transgenic mouse models and by using phosphodiesterase 3 (PDE3) inhibitors, PDE3B has an important role in the regulation of insulin secretion in pancreatic β-cells. However, very little is known about the regulation of the enzyme. Here, we show that PDE3B is activated in response to high glucose, insulin and cAMP elevation in rat pancreatic islets and INS-1 (832/13) cells. Activation by glucose was not affected by the presence of diazoxide. PDE3B activation was coupled to an increase as well as a decrease in total phosphorylation of the enzyme. In addition to PDE3B, several other PDEs were detected in human pancreatic islets: PDE1, PDE3, PDE4C, PDE7A, PDE8A and PDE10A. We conclude that PDE3B is activated in response to agents relevant for β-cell function and that activation is linked to increased as well as decreased phosphorylation of the enzyme. Moreover, we conclude that several PDEs are present in human pancreatic islets.http://europepmc.org/articles/PMC2995729?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Emilia Heimann
Helena A Jones
Svante Resjö
Vincent C Manganiello
Lena Stenson
Eva Degerman
spellingShingle Emilia Heimann
Helena A Jones
Svante Resjö
Vincent C Manganiello
Lena Stenson
Eva Degerman
Expression and regulation of cyclic nucleotide phosphodiesterases in human and rat pancreatic islets.
PLoS ONE
author_facet Emilia Heimann
Helena A Jones
Svante Resjö
Vincent C Manganiello
Lena Stenson
Eva Degerman
author_sort Emilia Heimann
title Expression and regulation of cyclic nucleotide phosphodiesterases in human and rat pancreatic islets.
title_short Expression and regulation of cyclic nucleotide phosphodiesterases in human and rat pancreatic islets.
title_full Expression and regulation of cyclic nucleotide phosphodiesterases in human and rat pancreatic islets.
title_fullStr Expression and regulation of cyclic nucleotide phosphodiesterases in human and rat pancreatic islets.
title_full_unstemmed Expression and regulation of cyclic nucleotide phosphodiesterases in human and rat pancreatic islets.
title_sort expression and regulation of cyclic nucleotide phosphodiesterases in human and rat pancreatic islets.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2010-01-01
description As shown by transgenic mouse models and by using phosphodiesterase 3 (PDE3) inhibitors, PDE3B has an important role in the regulation of insulin secretion in pancreatic β-cells. However, very little is known about the regulation of the enzyme. Here, we show that PDE3B is activated in response to high glucose, insulin and cAMP elevation in rat pancreatic islets and INS-1 (832/13) cells. Activation by glucose was not affected by the presence of diazoxide. PDE3B activation was coupled to an increase as well as a decrease in total phosphorylation of the enzyme. In addition to PDE3B, several other PDEs were detected in human pancreatic islets: PDE1, PDE3, PDE4C, PDE7A, PDE8A and PDE10A. We conclude that PDE3B is activated in response to agents relevant for β-cell function and that activation is linked to increased as well as decreased phosphorylation of the enzyme. Moreover, we conclude that several PDEs are present in human pancreatic islets.
url http://europepmc.org/articles/PMC2995729?pdf=render
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