Strategies for development of novel antithrombotics: modulating thrombin's procoagulant and anticoagulant properties.
Review published in Cellular and molecular life sciences : CMLS (1997)
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.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Резюме
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.
Почему это важно для гирудотерапии
This review discusses strategies for developing novel antithrombotic agents by exploiting thrombin's allosteric regulation, noting that thrombin's procoagulant and anticoagulant functions are physiologically regulated by thrombomodulin and can be modulated by sodium binding, site-directed mutagenesis, and a small synthetic molecule. It frames modulation of thrombin's intrinsic properties as a novel antithrombotic approach. The abstract does not mention hirudin, leeches, leech-derived compounds, or hirudotherapy, so it offers no direct evidence for ASH's domain. Any connection to leech-based therapeutics would be speculative and outside the abstract's stated content.
Цитирование
Strategies for development of novel antithrombotics: modulating thrombin's procoagulant and anticoagulant properties.
Hall et al. · Cellular and molecular life sciences : CMLS, 1997
Связанный клинический контекст
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