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

FEBS Letters

Masuda, Michitaka²  Fujiwara, Keigi²  Osawa, Masaki²  Harada, Noboru²  Shigematsu, Hiroki¹ 

[1] Laboratory for Chemistry, Institute for Life Science Research, Asahi Chemical Industry Co., Ltd., Fuji, Shizuoka 416, Japan;Department of Structural Analysis, National Cardiovascular Center Research Institute, Suita, Osaka 565, Japan

关键词: PECAM-1;    SH-PTP2;    Tyrosine phosphorylation;    Osmotic shock;    Mechanical stimuli;    Endothelial cell;   

DOI  :  10.1016/S0014-5793(97)00457-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown