Tyrosine phosphorylation and activation of pp60c-src and pp125FAK in bradykinin-stimulated fibroblasts.
Tyrosine phosphorylation and activation of pp60c-src and pp125FAK in bradykinin-stimulated fibroblasts.
复制标题
缓激肽刺激的成纤维细胞中酪氨酸磷酸化以及 pp60c-src 和 pp125FAK 的激活。
DOI:
10.1152/ajpcell.1996.270.5.c1430
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发表时间:
1996
期刊:
影响因子:
--
通讯作者:
Villereal,ML
中科院分区:
文献类型:
--
作者:
Lee,KM;Villereal,ML
Bradykinin (BK) stimulates protein tyrosine phosphorylation in human foreskin fibroblasts (K.-M. Lee, K. Toscas, and M. L. Villereal, J. Biol. Chem. 268:9945-9948, 1993). The major tyrosine phosphorylation occurs in proteins of a molecular mass of 130 and 70 kDa. In this report, we demonstrate that focal adhesion-associated tyrosine kinase, pp125FAK, is one component of the 130-kDa phosphotyrosine band. The BK-stimulated pp125FAK tyrosine phosphorylation level is well correlated with increased kinase activity, as assessed by in vitro immune complex kinase assays. We have identified paxillin, a protein that is localized in focal adhesions, as a component of the 70-kDa phosphotyrosine band. In addition to identifying the two proteins responsible for the major phosphotyrosine bands, we also report that pp60c-src is tyrosine phosphorylated and activated in response to BK, as analyzed by immunoblotting and in vitro kinase assays, respectively. These findings indicate, for the first time, that the BK receptor is coupled to the important protooncogene c-src and that the src pathway may mediate some of the events downstream from BK binding.
DOI:
--
发表时间:
1993
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Lee,KM;Toscas,K;Villereal,ML
通讯作者:
Villereal,ML