American Society of Hirudotherapy

Strategies for development of novel antithrombotics: modulating thrombin's procoagulant and anticoagulant properties.

Review published in Cellular and molecular life sciences : CMLS (1997)

Last Updated: June 18, 2026Reviewed by: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Narrative reviewDrug DevelopmentSalivary PharmacologyHall et al. · 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.

Publication typeJournal ArticleReview
Indexed MeSH termsAllosteric RegulationAnimalsAnticoagulantsAntithrombin IIIAntithrombinsFibrinolytic AgentsHumansProtein ConformationProtein EngineeringStructure-Activity RelationshipThrombinThrombomodulin

Summary

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.

Why This Matters for Hirudotherapy

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.

Citation

Strategies for development of novel antithrombotics: modulating thrombin's procoagulant and anticoagulant properties.

Hall et al. · Cellular and molecular life sciences : CMLS, 1997

DOI

Added to ASH library: May 28, 2026 · Site last updated: June 18, 2026

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