The activation of CD99 inhibits cell-extracellular matrix adhesion by suppressing β(1) integrin affinity

BMB Rep. 2012 Mar;45(3):159-64. doi: 10.5483/BMBRep.2012.45.3.159.

Abstract

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. [BMB reports 2012; 45(3): 159-164].

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 12E7 Antigen
  • Antigens, CD / metabolism*
  • Cell Adhesion / drug effects
  • Cell Adhesion Molecules / agonists*
  • Cell Adhesion Molecules / metabolism*
  • Extracellular Matrix / drug effects*
  • Extracellular Matrix / metabolism*
  • Humans
  • Integrin beta1 / metabolism*
  • MCF-7 Cells
  • Tumor Cells, Cultured

Substances

  • 12E7 Antigen
  • Antigens, CD
  • CD99 protein, human
  • Cell Adhesion Molecules
  • Integrin beta1