pubmed-article:2467744 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2467744 | lifeskim:mentions | umls-concept:C0682538 | lld:lifeskim |
pubmed-article:2467744 | lifeskim:mentions | umls-concept:C0071655 | lld:lifeskim |
pubmed-article:2467744 | lifeskim:mentions | umls-concept:C1519726 | lld:lifeskim |
pubmed-article:2467744 | lifeskim:mentions | umls-concept:C0033268 | lld:lifeskim |
pubmed-article:2467744 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:2467744 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:2467744 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:2467744 | pubmed:dateCreated | 1989-5-23 | lld:pubmed |
pubmed-article:2467744 | pubmed:abstractText | A phosphatidylinositol (PI) kinase activity associated with certain protein tyrosine kinases important in cell proliferation phosphorylates the 3' hydroxyl position of PI to produce phosphatidylinositol-3-phosphate (PI-3-P). Here we report that, in addition to PI-3' kinase activity, anti-phosphotyrosine (alpha-P-tyr) immunoprecipitates from platelet-derived growth factor (PDGF)-stimulated smooth muscle cells (SMC) contain lipid kinase activities that utilize the substrates phosphatidylinositol-4-phosphate (PI-4-P) and phosphatidylinositol-4,5-bisphosphate (PI-4,5-P2). These activities are absent in alpha-P-tyr immunoprecipitates from quiescent SMC. The product of PI-4-P phosphorylation appears to be phosphatidylinositol-3,4-bisphosphate (PI-3,4-P2), a lipid not previously reported. The product of PI-4,5-P2 phosphorylation is phosphatidylinositol-trisphosphate (PIP3). PI-3-P was detected in quiescent SMC and increased only slightly in response to PDGF. PIP3 and the putative PI-3,4-P2 appeared only after the addition of mitogen. Both the temporal production of these novel phospholipids after PDGF stimulation and the observation of the enzymatic activities that produce them in alpha-P-tyr immunoprecipitates suggest that these phospholipids are excellent candidates for mediators of the PDGF mitogenic response. | lld:pubmed |
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pubmed-article:2467744 | pubmed:language | eng | lld:pubmed |
pubmed-article:2467744 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2467744 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:2467744 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2467744 | pubmed:month | Apr | lld:pubmed |
pubmed-article:2467744 | pubmed:issn | 0092-8674 | lld:pubmed |
pubmed-article:2467744 | pubmed:author | pubmed-author:SerunianL ALA | lld:pubmed |
pubmed-article:2467744 | pubmed:author | pubmed-author:CantleyL CLC | lld:pubmed |
pubmed-article:2467744 | pubmed:author | pubmed-author:LibbyPP | lld:pubmed |
pubmed-article:2467744 | pubmed:author | pubmed-author:SoltoffS PSP | lld:pubmed |
pubmed-article:2467744 | pubmed:author | pubmed-author:AugerK RKR | lld:pubmed |
pubmed-article:2467744 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2467744 | pubmed:day | 7 | lld:pubmed |
pubmed-article:2467744 | pubmed:volume | 57 | lld:pubmed |
pubmed-article:2467744 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2467744 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2467744 | pubmed:pagination | 167-75 | lld:pubmed |
pubmed-article:2467744 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:2467744 | pubmed:meshHeading | pubmed-meshheading:2467744-... | lld:pubmed |
pubmed-article:2467744 | pubmed:year | 1989 | lld:pubmed |
pubmed-article:2467744 | pubmed:articleTitle | PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells. | lld:pubmed |
pubmed-article:2467744 | pubmed:affiliation | Department of Cellular and Molecular Physiology, Tufts University School of Medicine, Boston, Massachusetts 02111. | lld:pubmed |
pubmed-article:2467744 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2467744 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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