Effect of thrombomodulin on plasminogen activation

H. S. Han, H. L. Wu, B. T. Lin, C. S. Shi, G. Y. Shi

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)

Abstract

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- 6B 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 ε-aminocaproic acid. In conclusion, our results suggest that TMD23 could specifically bind to plasminogen and effectively enhance plasminogen activation. (C) 2000 Harcourt Publishers Ltd.

Original languageEnglish
Pages (from-to)221-228
Number of pages8
JournalFibrinolysis and Proteolysis
Volume14
Issue number4
DOIs
Publication statusPublished - 2000 Jan 1

All Science Journal Classification (ASJC) codes

  • Hematology

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