SELECTIN GMP-140 (CD62, PADGEM) BINDS TO SIALOSYL-LEA AND SIALOSYL-LEX, AND SULFATED GLYCANS MODULATE THIS BINDING

被引：151

作者：

HANDA, K ^{[1
]}

NUDELMAN, ED ^{[1
]}

STROUD, MR ^{[1
]}

SHIOZAWA, T ^{[1
]}

HAKOMORI, S ^{[1
]}

机构：

[1] UNIV WASHINGTON,DEPT PATHOBIOL,SEATTLE,WA 98195

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 181卷 / 03期

关键词：

D O I：

10.1016/0006-291X(91)92069-V

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：

GMP-140 (CD62; PADGEM) is a member of the selectin family expressed highly at the surface of platelets and endothelial cells by agonists such as thrombin or phorbol esters. Previous studies indicate that the lectin domain of GMP-140 recognizes sialosyl-Lex (SLex) and to a lesser extent Lex (Polley MJ, et al., Proc Natl Acad Sci USA 88:6224, 1991). We now report that GMP-140 binds to sialosyl Lea (SLea) and to SLex, and that degree of binding to SLea is greater than that to SLex under our experimental conditions. Binding of activated platelets to SLea or SLex was inhibited to various degrees in the presence of sulfated glycans, suggesting that sulfated glycans induce conformational change in the lectin domain of GMP-140 and modulates its binding affinity to SLea and SLex. © 1991.

引用

页码：1223 / 1230

页数：8

共 19 条

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