rdf:type |
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lifeskim:mentions |
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pubmed:issue |
14
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pubmed:dateCreated |
2000-5-8
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pubmed:abstractText |
Phosphatidylinositol 3-kinase mediates several actions of insulin including its antilipolytic effect. This effect is elicited by the insulin-stimulated serine phosphorylation and activation of cGMP-inhibited phosphodiesterase (PDE3B). In human adipocytes, we found that insulin differentially stimulated phosphatidylinositol 3-kinase activity; the lipid kinase activity was associated with IRS-1, whereas the serine kinase activity was associated with the insulin receptor and phosphorylated a number of proteins including p85, p110, and a 135-kDa protein identified as PDE3B. PDE3B phosphorylation was associated with enzyme activation, thus initiating the antilipolytic effect of insulin. These results show a novel pathway for intracellular signaling through the insulin receptor leading to the serine phosphorylation of key proteins involved in insulin action.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3',5'-Cyclic-AMP Phosphodiesterases,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic Nucleotide...,
http://linkedlifedata.com/resource/pubmed/chemical/IRS1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin Receptor Substrate Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PDE3B protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Insulin
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10093-8
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10744689-3',5'-Cyclic-AMP Phosphodiesterases,
pubmed-meshheading:10744689-Adipose Tissue,
pubmed-meshheading:10744689-Cells, Cultured,
pubmed-meshheading:10744689-Cyclic Nucleotide Phosphodiesterases, Type 3,
pubmed-meshheading:10744689-Enzyme Activation,
pubmed-meshheading:10744689-Humans,
pubmed-meshheading:10744689-Insulin,
pubmed-meshheading:10744689-Insulin Receptor Substrate Proteins,
pubmed-meshheading:10744689-Molecular Weight,
pubmed-meshheading:10744689-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:10744689-Phosphoproteins,
pubmed-meshheading:10744689-Phosphorylation,
pubmed-meshheading:10744689-Protein-Serine-Threonine Kinases,
pubmed-meshheading:10744689-Receptor, Insulin,
pubmed-meshheading:10744689-Signal Transduction
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pubmed:year |
2000
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pubmed:articleTitle |
Phosphorylation of PDE3B by phosphatidylinositol 3-kinase associated with the insulin receptor.
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pubmed:affiliation |
Lundberg Laboratory for Diabetes Research, Department of Internal Medicine, Goteborg University, Sahlgrenska University Hospital, Goteborg S-413 45, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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