Down-regulation of integrin alpha(M)beta(2) ligand-binding function by the urokinase-type plasminogen activator receptor

作者：Tang Man-Li; Kong Le-Sheng; Law S. K. Alex; Tan Suet-Mien^*

来源：Biochemical and Biophysical Research Communications, 2006, 348(3): 1184-1193.

DOI：10.1016/j.bbrc.2006.07.179

• cell adhesion
• integrins
• urokinase-type plasminogen activator receptor

The cell adhesion molecule integrin alpha(M)beta(2) associates with the urokinase-type plasminogen activator receptor (uPAR) on monocytes and neutrophils. uPAR also associates with members of the beta(1) and beta(3) integrins, and it modulates the ligand-binding function of these integrins. In this study, we showed that co-expressing uPAR with alpha(M)beta(2) in 293 transfectants down-regulated the ligand-binding capacity of alpha(M)beta(2) to denatured protein, fibrinogen, and intercellular adhesion molecule I (ICAM-1). Migration of transfectants on fibrinogen mediated by alpha(M)beta(2) was reduced in the presence of uPAR. In addition, the constitutive ligand-binding property of an alpha(M)beta(2) mutant was attenuated by its association with uPAR. Co-immunoprecipitation analyses using a panel of alpha(M)beta(2)- specific mAbs suggest shielding of the ligand-recognition site Of 942 by uPAR.

• 出版日期2006-9-29
• 单位南阳理工学院