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

Abstract：

:The cell adhesion molecule integrin alphaMbeta2 associates with the urokinase-type plasminogen activator receptor (uPAR) on monocytes and neutrophils. uPAR also associates with members of the beta1 and beta3 integrins, and it modulates the ligand-binding function of these integrins. In this study, we showed that co-expressing uPAR with alphaMbeta2 in 293 transfectants down-regulated the ligand-binding capacity of alphaMbeta2 to denatured protein, fibrinogen, and intercellular adhesion molecule 1 (ICAM-1). Migration of transfectants on fibrinogen mediated by alphaMbeta2 was reduced in the presence of uPAR. In addition, the constitutive ligand-binding property of an alphaMbeta2 mutant was attenuated by its association with uPAR. Co-immunoprecipitation analyses using a panel of alphaMbeta2-specific mAbs suggest shielding of the ligand-recognition site of alphaMbeta2 by uPAR.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Tang ML,Kong LS,Law SK,Tan SM

doi

10.1016/j.bbrc.2006.07.179

subject

Has Abstract

pub_date

2006-09-29 00:00:00

pages

1184-93

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)01761-X

journal_volume

348

pub_type

杂志文章

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