pubmed-article:10428803 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10428803 | lifeskim:mentions | umls-concept:C0006675 | lld:lifeskim |
pubmed-article:10428803 | lifeskim:mentions | umls-concept:C0081888 | lld:lifeskim |
pubmed-article:10428803 | lifeskim:mentions | umls-concept:C1418416 | lld:lifeskim |
pubmed-article:10428803 | lifeskim:mentions | umls-concept:C1256369 | lld:lifeskim |
pubmed-article:10428803 | pubmed:issue | 32 | lld:pubmed |
pubmed-article:10428803 | pubmed:dateCreated | 1999-9-2 | lld:pubmed |
pubmed-article:10428803 | pubmed:abstractText | To understand the role cAMP phosphodiesterases (PDEs) play in the regulation of insulin secretion, we analyzed cyclic nucleotide PDEs of a pancreatic beta-cell line and used family and isozyme-specific PDE inhibitors to identify the PDEs that counteract glucose-stimulated insulin secretion. We demonstrate the presence of soluble PDE1C, PDE4A and 4D, a cGMP-specific PDE, and of particulate PDE3, activities in betaTC3 insulinoma cells. Selective inhibition of PDE1C, but not of PDE4, augmented glucose-stimulated insulin secretion in a dose-dependent fashion thus demonstrating that PDE1C is the major PDE counteracting glucose-dependent insulin secretion from betaTC3 cells. In pancreatic islets, inhibition of both PDE1C and PDE3 augmented glucose-dependent insulin secretion. The PDE1C of betaTC3 cells is a novel isozyme possessing a K(m) of 0.47 microM for cAMP and 0.25 microM for cGMP. The PDE1C isozyme of betaTC3 cells is sensitive to 8-methoxymethyl isobutylmethylxanthine and zaprinast (IC(50) = 7.5 and 4.5 microM, respectively) and resistant to vinpocetine (IC(50) > 100 microM). Increased responsiveness of PDE1C activity to calcium/calmodulin is evident upon exposure of cells to glucose. Enhanced cAMP degradation by PDE1C, due to increases in its responsiveness to calcium/calmodulin and in intracellular calcium, constitutes a glucose-dependent feedback mechanism for the control of insulin secretion. | lld:pubmed |
pubmed-article:10428803 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10428803 | pubmed:language | eng | lld:pubmed |
pubmed-article:10428803 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10428803 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10428803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10428803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10428803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10428803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10428803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10428803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10428803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10428803 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10428803 | pubmed:month | Aug | lld:pubmed |
pubmed-article:10428803 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:10428803 | pubmed:author | pubmed-author:FleischerNN | lld:pubmed |
pubmed-article:10428803 | pubmed:author | pubmed-author:HanPP | lld:pubmed |
pubmed-article:10428803 | pubmed:author | pubmed-author:WerberJJ | lld:pubmed |
pubmed-article:10428803 | pubmed:author | pubmed-author:SuranaMM | lld:pubmed |
pubmed-article:10428803 | pubmed:author | pubmed-author:MichaeliTT | lld:pubmed |
pubmed-article:10428803 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10428803 | pubmed:day | 6 | lld:pubmed |
pubmed-article:10428803 | pubmed:volume | 274 | lld:pubmed |
pubmed-article:10428803 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10428803 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10428803 | pubmed:pagination | 22337-44 | lld:pubmed |
pubmed-article:10428803 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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pubmed-article:10428803 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10428803 | pubmed:articleTitle | The calcium/calmodulin-dependent phosphodiesterase PDE1C down-regulates glucose-induced insulin secretion. | lld:pubmed |
pubmed-article:10428803 | pubmed:affiliation | Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, New York 10461, USA. | lld:pubmed |
pubmed-article:10428803 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10428803 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:10428803 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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