Enhancing protein C interaction with thrombin results in a clot-activated anticoagulant
Article Abstract:
The circulating zymogen human protein C is activated at endothelial cell surfaces by thrombin in complex with an integral membrane protein. The activated form of protein C has several important properties including strong anticoagulant activity. However, protein C has only been therapeutically useful when administered in activated form and then it has a short biologic half-life. Genetic alteration results in a zymogen protein C with 60 times the half-life of the activated protein which can be activated by thrombin generated in clotting plasma alone, thus representing a site-activated agent.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
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The thrombin paradox
Article Abstract:
Research on the thrombin paradox has been undertaken by Gibbs and company who dissect the issue by showing that the change from glutamic acid to alanine resulting in Ala-229 thrombin drastically changes in vivo and in vitro characteristics. The paradox basically revolves around the fact that thrombin can both prevent or promote blood clotting and excessive amounts of it can be destructive while a little amount of it is better than none of it.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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Conversion of thrombin into an anticoagulant by protein engineering
Article Abstract:
The contrasting effects of thrombin on blood coagulation, both promoting and preventing blood clotting, are discussed with special emphasis on anticoagulation through the use of protein engineering methods. One such method involves substitution that resulted in an emphasis on protein C, which acts as a powerful anticoagulant. This method was also not vulnerable to bleeding complications.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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