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Strategies for development of novel antithrombotics: modulating thrombin's procoagulant and anticoagulant properties CELLULAR AND MOLECULAR LIFE SCIENCES HALL, S. W., Gibbs, C. S., Leung, L. L. 1997; 53 (9): 731-736

Abstract

Thrombin is a serine proteinase that can interact with a large number of diverse macromolecular substrates, which results in either a procoagulant or anticoagulant effect. These divergent properties are physiologically regulated by the endogenous protein thrombomodulin. This review summarizes recent work on a variety of methods used to exploit the allosteric nature of the enzyme. The procoagulant and anticoagulant functions of thrombin can be modulated by sodium binding, site-directed mutagenesis, and a small synthetic molecule. Modulation of thrombin's intrinsic properties represents a novel approach to the development of unique antithrombotic agents.

View details for Web of Science ID A1997YB75600002

View details for PubMedID 9368669