| pubmed-article:8636414 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8636414 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:8636414 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:8636414 | lifeskim:mentions | umls-concept:C1512199 | lld:lifeskim |
| pubmed-article:8636414 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8636414 | lifeskim:mentions | umls-concept:C0018321 | lld:lifeskim |
| pubmed-article:8636414 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
| pubmed-article:8636414 | lifeskim:mentions | umls-concept:C1519726 | lld:lifeskim |
| pubmed-article:8636414 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:8636414 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:8636414 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:8636414 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:8636414 | pubmed:dateCreated | 1996-7-11 | lld:pubmed |
| pubmed-article:8636414 | pubmed:abstractText | We investigated the signaling pathways mediating 1-pS Ca2+ channel activation by PDGF in cultured rat mesangial cells. In cell-attached patches, intrapipette PDGF-BB (PDGF B chain homodimer isoform) (50 ng/ml) dramatically stimulates channel activity (P < 0.003, n = 6). Tyrosine kinase inhibition (100 microM genistein or 10 microM tryphostin 9) abolished PDGF-induced channel activation (P < 0.02, n = 6). In excised patches, the effect of tyrosine kinase inhibition could be reversed by 200 microM GTPgammaS (P < 0.02, n = 4). In contrast, 200 microM GDPbetaS inhibited PDGF-induced channel activity (P < 0.04, n = 6). Pertussis toxin (250 ng/ml) had no effect on PDGF-induced channel activity (P = 0.45, n = 6). When excised patches were exposed to anti-Ras antibody (5 microg/ml), PDGF-induced channel activity was abolished (P < 0.002, n = 11). Western immunoblots revealed that PDGF-BB binding stimulates the formation of a membrane-bound complex consisting of growth factor receptor-binding protein 2, son of sevenless, and the PDGF-beta receptor. Complex formation was abolished by genistein. In mesangial cells, the intrinsic tyrosine kinase activity of the PDGF-beta receptor stimulates the formation of a membrane-bound growth factor receptor-binding protein 2/son of sevenless/PDGF-beta receptor complex and activation of the pertussis toxin-insensitive GTP-binding protein, p21-Ras, which leads to the opening of 1-pS Ca2+ channels. | lld:pubmed |
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| pubmed-article:8636414 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8636414 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8636414 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:8636414 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8636414 | pubmed:month | May | lld:pubmed |
| pubmed-article:8636414 | pubmed:issn | 0021-9738 | lld:pubmed |
| pubmed-article:8636414 | pubmed:author | pubmed-author:MatsunagaHH | lld:pubmed |
| pubmed-article:8636414 | pubmed:author | pubmed-author:MICC | lld:pubmed |
| pubmed-article:8636414 | pubmed:author | pubmed-author:LingB NBN | lld:pubmed |
| pubmed-article:8636414 | pubmed:author | pubmed-author:ILLH MHM | lld:pubmed |
| pubmed-article:8636414 | pubmed:author | pubmed-author:SchiefferBB | lld:pubmed |
| pubmed-article:8636414 | pubmed:author | pubmed-author:MarreroM BMB | lld:pubmed |
| pubmed-article:8636414 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8636414 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8636414 | pubmed:volume | 97 | lld:pubmed |
| pubmed-article:8636414 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8636414 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8636414 | pubmed:pagination | 2332-41 | lld:pubmed |
| pubmed-article:8636414 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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