DECREASED THROMBIN AFFINITY OF CELL-SURFACE THROMBOMODULIN FOLLOWING TREATMENT OF CULTURED ENDOTHELIAL-CELLS WITH BETA-D-XYLOSIDE

被引：22

作者：

PARKINSON, JF ^{[1
]}

GARCIA, JGN ^{[1
]}

BANG, NU ^{[1
]}

机构：

[1] INDIANA UNIV,WISHARD MEM HOSP,DEPT MED,INDIANAPOLIS,IN 46202

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 169卷 / 01期

关键词：

D O I：

10.1016/0006-291X(90)91451-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：

Thrombomodulin, an endothelial cell-surface anticoagulant, has been postulated to contain a glycosaminoglycan. Thrombomodulin function was therefore studied in endothelial cells treated with β-D-xyloside, an inhibitor of glycosaminoglycan attachment to proteoglycan core proteins. β-D-xyloside caused a reproducible 3 to 5-fold increase in the Km of thrombomodulin for thrombin and a 20-30% decrease in the rate of protein C activation by the thrombin-thrombomodulin complex. These results support a role for glycosaminoglycans in thrombomodulin function and suggest that β-D-xylosides can be used to investigate both the anticoagulant mechanisms and the biosynthesis of cell-surface thrombomodulin. © 1990.

引用

页码：177 / 183

页数：7

共 27 条

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