H.-S. Han , H.-L. Wu , B.-T. Lin , C.-S. Shi , G.-Y. Shi
{"title":"Effect of thrombomodulin on plasminogen activation","authors":"H.-S. Han , H.-L. Wu , B.-T. Lin , C.-S. Shi , G.-Y. Shi","doi":"10.1054/fipr.2000.0059","DOIUrl":null,"url":null,"abstract":"<div><p>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.</p></div>","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"14 4","pages":"Pages 221-228"},"PeriodicalIF":0.0000,"publicationDate":"2000-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1054/fipr.2000.0059","citationCount":"11","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Fibrinolysis and Proteolysis","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0268949900900596","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 11
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.
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