The activation of CD99 inhibits cell-extracellular matrix adhesion by suppressing β1 integrin affinity

BMB Reports

Sun-Hee Lee^1¹  Birendra Kumar Yadav^1²  Kyoung-Jin Lee^1³ 

[1] Anatomy and Cell Biology, School of Medicine^2;Biochemistry, 3Biological Sciences, College of Natural Sciences, Kangwon National University, Chunchon 200-701, Korea^3;Departments of^1

关键词: β1 integrin;   

DOI  :  

学科分类：生物化学/生物物理

来源: Korean Society for Biochemistry and Molecular Biology

【 摘 要 】

CD99 is known to be involved in the regulation of cell-cell adhesion. However, it remains unclear whether CD99 controls cell-extracellular matrix adhesion. In this study, the effects of CD99 activation on cell-extracellular matrix adhesion were investigated. It was found that engagement of CD99 with the stimulating antibody YG32 downregulated the adhesion of MCF-7 cells to fibronectin, laminin and collagen IV in a dose-dependent manner. The CD99 effect on cell-ECM adhesion was inhibited by overexpression of the dominant negative form of CD99 or CD99 siRNA transfection. Treatment of cells with Mn(2+) or by β(1) integrin-stimulating antibody restored the inhibitory effect of CD99 on cell-ECM adhesion. Cross-linking CD99 inactivated β(1) integrin through conformational change. CD99 activation caused dephosphorylation at Tyr-397 in FAK, which was restored by the β(1) stimulating antibody. Taken together, these results provide the first evidence that CD99 inhibits cell-extracellular matrix adhesion by suppressing β(1) integrin affinity.

【 授权许可】

Unknown