Effect of thrombomodulin on plasminogen activation

被引：13

作者：

Han, HS

Wu, HL

Lin, BT

Shi, CS

Shi, GY ^{[1
]}

机构：

[1] Natl Cheng Kung Univ, Coll Med, Dept Biochem, Tainan 701, Taiwan

[2] Chung Hwa Inst Technol, Dept Med Technol, Tainan, Taiwan

来源：

FIBRINOLYSIS & PROTEOLYSIS | 2000年 / 14卷 / 04期

关键词：

D O I：

10.1054/fipr.2000.0059

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 (TM), a thrombin receptor on the endothelial cell surface, plays an important role in the regulation of blood coagulation. In this study, recombinant TM containing six epidermal growth factor-like structures (D2), and serine and threonine (Ser/Thr)-rich domain (D3), TMD23 (corresponding to Ala224-Ser497), was prepared by a recombinant baculovirus expression system and purified to apparent homogeneity by DEAE-Sepharose CL-GB and affinity nickel-chelating column chromatographies. TMD23 in combination with thrombin could effectively activate protein C. TMD23 alone could enhance Glu-plasminogen activation by single-chain urokinase-type plasminogen activator in a dose-dependent manner. The specific binding of plasminogen to TMD23 was also demonstrated and the binding was inhibited by E-aminocaproic acid. In conclusion, our results suggest that TMD23 could specifically bind to plasminogen and effectively enhance plasminogen activation. (C) 2000 Harcourt Publishers Ltd.

引用

页码：221 / 228

页数：8