VCAM-1 ON ACTIVATED ENDOTHELIUM INTERACTS WITH THE LEUKOCYTE INTEGRIN VLA-4 AT A SITE DISTINCT FROM THE VLA-4 FIBRONECTIN BINDING-SITE

被引：1778

作者：

ELICES, MJ ^{[1
]}

OSBORN, L ^{[1
]}

TAKADA, Y ^{[1
]}

CROUSE, C ^{[1
]}

LUHOWSKYJ, S ^{[1
]}

HEMLER, ME ^{[1
]}

LOBB, RR ^{[1
]}

机构：

[1] BIOGEN INC, CAMBRIDGE, MA 02142 USA

来源：

CELL | 1990年 / 60卷 / 04期

关键词：

D O I：

10.1016/0092-8674(90)90661-W

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Cytokine-activated human endothelial cells express vascular cell adhesion molecule-1 (VCAM-1), which binds lymphocytes. We now identify the integrin VLA-4 as a receptor for VCAM-1 because VLA-4 surface expression on K-562 cells (following transfection of the VLA α4 subunit cDNA) resulted in specific cell adhesion to VCAM-1, and anti VLM4 antibodies completely inhibited VCAM-1-dependent cell-cell attachment. In addition, VLA-4 expression allowed K562 cells to attach to the heparin 11 binding region (FN-40) of fibronectin. However, VLA-41VCAM-1 and VLA-4/FN-40 interactions are readily distinguishable: only the former was inhibited by the anti VLA-4 monoclonal antibody HP1/3, and only the latter was inhibited by soluble FN40. The VCAM-1/VLA-4 ligand-receptor pair may play a major role in the recruitment of mononuclear leukocytes to inflammatory sites in vivo. © 1990.

引用

页码：577 / 584

页数：8

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