Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 348, Issue 3, Pages 1184-1193Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2006.07.179
Keywords
cell adhesion; integrins; urokinase-type plasminogen activator receptor
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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. (c) 2006 Elsevier Inc. All rights reserved.
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