Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 이서구 | * |
dc.date.accessioned | 2018-05-02T08:15:32Z | - |
dc.date.available | 2018-05-02T08:15:32Z | - |
dc.date.issued | 2004 | * |
dc.identifier.issn | 0021-9258 | * |
dc.identifier.other | OAK-2273 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/242728 | - |
dc.description.abstract | Phospholipase C-γ1 (PLC-γ1) is phosphorylated on three tyrosine residues: Tyr-771, Tyr-783, and Tyr-1253. With the use of antibodies specific for each of these phosphorylation sites, we have now determined the kinetics and magnitude of phosphorylation at each site. Phosphorylation of Tyr-783, which is essential for lipase activation, was observed in all stimulated cell types examined. The extent of phosphorylation of Tyr-1253 was ∼50 to 70% of that of Tyr-783 in cells stimulated with platelet-derived growth factor (PDGF) or epidermal growth factor (EGF), but Tyr-1253 phosphorylation was not detected in B or T cell lines stimulated through B- and T-cell antigen receptors, respectively. Tyr-771 was phosphorylated only at a low level in all cells studied. In cells stimulated with PDGF, phosphorylation and dephosphorylaiion of Tyr-783 and of Tyr-1253 occurred with similar kinetics; the receptor kinase appeared to phosphorylate both sites, albeit with Tyr-783 favored over Tyr-1253, before the bound PLC-γ1 was released, and phosphorylation at the two sites occurred independently. PDGF and EGF induced similar levels of phosphorylation of Tyr-783 and of Tyr-1253 in a cell line that expressed receptors for both growth factors. However, only PDGF, not EGF, elicited substantial PLC activity, suggesting that Tyr-783 phosphorylation was not sufficient for enzyme activation. Finally, concurrent production of phosphatidylinositol 3,4,5-trisphosphate was found to contribute to the activation of phosphorylated PLC-γ1. | * |
dc.language | English | * |
dc.title | Mechanism of tyrosine phosphorylation and activation of phospholipase c-γ1. Tyrosine 783 phosphorylation is not sufficient for lipase activation | * |
dc.type | Article | * |
dc.relation.issue | 31 | * |
dc.relation.volume | 279 | * |
dc.relation.index | SCI | * |
dc.relation.index | SCIE | * |
dc.relation.index | SCOPUS | * |
dc.relation.startpage | 32181 | * |
dc.relation.lastpage | 32190 | * |
dc.relation.journaltitle | Journal of Biological Chemistry | * |
dc.identifier.doi | 10.1074/jbc.M405116200 | * |
dc.identifier.wosid | WOS:000222849700024 | * |
dc.identifier.scopusid | 2-s2.0-3543026271 | * |
dc.author.google | Sekiya F. | * |
dc.author.google | Poulin B. | * |
dc.author.google | Kim Y.J. | * |
dc.author.google | Rhee S.G. | * |
dc.contributor.scopusid | 이서구(7401852092) | * |
dc.date.modifydate | 20240423081003 | * |