Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/68305
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dc.contributor.authorLai, J.F.en_US
dc.contributor.author陳鴻震zh_TW
dc.contributor.authorKao, S.C.en_US
dc.contributor.authorJiang, S.T.en_US
dc.contributor.authorTang, M.J.en_US
dc.contributor.authorChan, P.C.en_US
dc.contributor.authorChen, H.C.en_US
dc.date2000zh_TW
dc.date.accessioned2014-06-11T05:56:36Z-
dc.date.available2014-06-11T05:56:36Z-
dc.identifier.issn0021-9258zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/68305-
dc.description.abstractFocal adhesion kinase (FAK) has been implicated to play a critical role in integrin-mediated control of cell behavior. However, it is unclear whether FAK also participates in the regulation of growth factor-elicited. cellular functions. In this study, we have demonstrated that although overexpression of FAK in Madin-Dardy canine kidney cells did not alter their growth property or ability to form tubules within collagen gel upon hepatocyte growth factor (HGF) stimulation, it apparently enhanced HGF-induced cell scattering This enhancement was largely because of an increase in the third phase (i.e. cell migration) of cell scattering rather than the first two phases (i.e. cell spreading and cell-cell dissociation). Conversely, the expression of FAR-related nonkinase significantly (similar to 60%) inhibited HGF-induced cell migration. Moreover, we have found that the effect of FAK on promoting HGF-induced cell motility was greatly dependent on cell-matrix interactions. We showed that HGF treatment selectively increased the expression of integrins alpha(2) and, to a lesser extent, alpha(3) in Madin-Dardy canine kidney cells and that a monoclonal antibody against integrin alpha(2) efficiently blocked HGF-enhanced cell migration on collagen. In our efforts to determine the mechanism. by which FAK promotes HGF-induced cell migration, we found that FAK mutants deficient in phosphatidylinositol 3-kinase or p130(Cas) binding failed to promote HGF-induced cell migration, Interestingly, cells expressing a FAK mutant defective in Grb2 binding exhibited a rate of migration similar to 50% lower than that of cells expressing wild type FAK in response to HGF stimulation, Taken together, our results suggest a link between HGF-increased integrin expression, FAK activation, and enhanced cell motility and implicate a role for FAK in the facilitation of growth factor-induced cell motility.en_US
dc.language.isoen_USzh_TW
dc.relationJournal of Biological Chemistryen_US
dc.relation.ispartofseriesJournal of Biological Chemistry, Volume 275, Issue 11, Page(s) 7474-7480.en_US
dc.relation.urihttp://dx.doi.org/10.1074/jbc.275.11.7474en_US
dc.subjectreceptor tyrosine kinaseen_US
dc.subjectphosphatidylinositol 3-kinaseen_US
dc.subjectepithelial-cellsen_US
dc.subjectc-meten_US
dc.subjectintegrin expressionen_US
dc.subjectprotein-kinaseen_US
dc.subjectgrb2en_US
dc.subjectbindingen_US
dc.subjectmdck cellsen_US
dc.subject3t3 cellsen_US
dc.subjectv-srcen_US
dc.titleInvolvement of focal adhesion kinase in hepatocyte growth factor-induced scatter of Madin-Darby canine kidney cellsen_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1074/jbc.275.11.7474zh_TW
item.languageiso639-1en_US-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.openairetypeJournal Article-
item.fulltextno fulltext-
item.grantfulltextnone-
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