ROLE OF 3RD N-TERMINAL DOMAIN OF VCAM-1

被引：6

作者：

WEBB, DL ^{[1
]}

MARLOR, CW ^{[1
]}

CONRAD, PJ ^{[1
]}

BARKOWSKICLARK, S ^{[1
]}

BLUE, ML ^{[1
]}

机构：

[1] MILES INC,RES CTR,INST MOLEC BIOL,W HAVEN,CT 06516

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1993年 / 197卷 / 02期

关键词：

D O I：

10.1006/bbrc.1993.2532

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：

The interaction between VLA-4 and VCAM-1 has been implicated in the recruitment, adhesion, and activation of mononuclear leukocytes in chronic inflammatory conditions and autoimmune disease. The seven domain extracellular portion of VCAM-1, sVCAM1-7, and the first three and two N- terminal domains of VCAM-1, sVCAM1-3 and sVCAM1-2, respectively, were expressed in baculovirus and purified. Using these purified soluble forms of VCAM-1 and cellular transfectants expressing various cell bound forms of VCAM-1, we show that the major binding site for VLA-4 is located within the first two domains of VCAM-1 and that the third domain of VCAM-1 appears to be required for functional integrity of the VLA-4 binding site. © 1993 Academic Press, Inc.

引用

页码：674 / 681

页数：8

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