pubmed-article:9726983 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9726983 | lifeskim:mentions | umls-concept:C0600431 | lld:lifeskim |
pubmed-article:9726983 | lifeskim:mentions | umls-concept:C0031621 | lld:lifeskim |
pubmed-article:9726983 | lifeskim:mentions | umls-concept:C0031671 | lld:lifeskim |
pubmed-article:9726983 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:9726983 | pubmed:issue | 37 | lld:pubmed |
pubmed-article:9726983 | pubmed:dateCreated | 1998-10-13 | lld:pubmed |
pubmed-article:9726983 | pubmed:abstractText | It has been demonstrated that the lipid products of the phosphoinositide 3-kinase (PI3K) can associate with the Src homology 2 (SH2) domains of specific signaling molecules and modify their actions. In the current experiments, phosphatidylinositol 3,4, 5-trisphosphate (PtdIns-3,4,5-P3) was found to bind to the C-terminal SH2 domain of phospholipase Cgamma (PLCgamma) with an apparent Kd of 2.4 microM and to displace the C-terminal SH2 domain from the activated platelet-derived growth factor receptor (PDGFR). To investigate the in vivo relevance of this observation, intracellular inositol trisphosphate (IP3) generation and calcium release were examined in HepG2 cells expressing a series of PDGFR mutants that activate PLCgamma with or without receptor association with PI3K. Coactivation of PLCgamma and PI3K resulted in an approximately 40% increase in both intracellular IP3 generation and intracellular calcium release as compared with selective activation of PLCgamma. Similarly, the addition of wortmannin or LY294002 to cells expressing the wild-type PDGFR inhibited the release of intracellular calcium. Thus, generation of PtdIns-3,4,5-P3 by receptor-associated PI3K causes an increase in IP3 production and intracellular calcium release, potentially via enhanced PtdIns-4, 5-P2 substrate availability due to PtdIns-3,4,5-P3-mediated recruitment of PLCgamma to the lipid bilayer. | lld:pubmed |
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pubmed-article:9726983 | pubmed:language | eng | lld:pubmed |
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pubmed-article:9726983 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:9726983 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9726983 | pubmed:month | Sep | lld:pubmed |
pubmed-article:9726983 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:9726983 | pubmed:author | pubmed-author:RheeS GSG | lld:pubmed |
pubmed-article:9726983 | pubmed:author | pubmed-author:CantleyL CLC | lld:pubmed |
pubmed-article:9726983 | pubmed:author | pubmed-author:SpokesKK | lld:pubmed |
pubmed-article:9726983 | pubmed:author | pubmed-author:CantleyL GLG | lld:pubmed |
pubmed-article:9726983 | pubmed:author | pubmed-author:MülerM MMM | lld:pubmed |
pubmed-article:9726983 | pubmed:author | pubmed-author:KazlauskasAA | lld:pubmed |
pubmed-article:9726983 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9726983 | pubmed:day | 11 | lld:pubmed |
pubmed-article:9726983 | pubmed:volume | 273 | lld:pubmed |
pubmed-article:9726983 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9726983 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9726983 | pubmed:pagination | 23750-7 | lld:pubmed |
pubmed-article:9726983 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:9726983 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9726983 | pubmed:articleTitle | Phosphoinositide 3-kinase regulates phospholipase Cgamma-mediated calcium signaling. | lld:pubmed |
pubmed-article:9726983 | pubmed:affiliation | Division of Signal Transduction, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02215, USA. | lld:pubmed |
pubmed-article:9726983 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9726983 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9726983 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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