Platelet endothelial cell adhesion molecule-1 is a major SH-PTP2 binding protein in vascular endothelial cells

被引:88
|
作者
Masuda, M [1 ]
Osawa, M [1 ]
Shigematsu, H [1 ]
Harada, N [1 ]
Fujiwara, K [1 ]
机构
[1] ASAHI CHEM IND CO LTD, LIFE SCI RES INST, CHEM LAB, FUJI, SHIZUOKA 416, JAPAN
来源
FEBS LETTERS | 1997年 / 408卷 / 03期
基金
日本科学技术振兴机构;
关键词
PECAM-1; SH-PTP2; tyrosine phosphorylation; osmotic shock; mechanical stimuli; endothelial cell; TYROSINE-PHOSPHATASE; FLUID-FLOW; KINASE; INSULIN; STIMULATION; CLONING; DOMAINS; CD31;
D O I
10.1016/S0014-5793(97)00457-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Platelet endothelial cell adhesion molecule-1 (PECAM-1, CD31) is rapidly tyrosine phosphorylated in mechanically stimulated vascular endothelial cells (ECs), A 65-kDa protein from ECs specifically bound to the c-Src phosphorylated PECAM-1 cytoplasmic domain and was identified as a protein tyrosine phosphatase SH-PTP2 (SHP2, Syp), PECAM-1 was coimmunoprecipitated by anti-SH-PTP2 from EC extracts as a major binding protein, and the level of association increased when PECAM-1 was tyrosine phosphorylated, This association was mediated by SH2 domains of SH-PTP2. A rapid translocation of SH-PTP2 into cell-cell adhesion sites, where PECAM-1 was localized, occurred in mechanically stimulated cells, Our results suggest that PECAM-1 is a component of a mechanosensing machinery acting upstream of SH-PTP2. (C) 1997 Federation of European Biochemical Societies.
引用
收藏
页码:331 / 336
页数:6
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