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KMID : 0624620120450030159
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BMB Reports
2012 Volume.45 No. 3 p.159 ~ p.164
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The activation of CD99 inhibits cell-extracellular matrix adhesion by suppressing β1 integrin affinity
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Lee Kyoung-Jin
Lee Sun-Hee
Yadav Birendra Kumar
Ju Hyun-Mi
Kim Min-Seo
Park Jeong-Hyun
Jeoung Doo-Il
Lee Han-Soo
Hahn Jang-Hee
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Abstract
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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.
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KEYWORD
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β1 integrin, CD99, Cell-ECM adhesion, Conformational change, FAK
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