American Society of Hirudotherapy

[Polyfunctionality of destabilase, a lysozyme from a medicinal leech]

Research article published in Bioorganicheskaia khimiia (2008)

Last Updated: June 18, 2026Reviewed by: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Narrative reviewSalivary PharmacologyBaskova I, Zavalova L · Bioorganicheskaia khimiia, 2008

Abstract

Experimental data indicating the polyfunctionality of destabilase, a lysozyme from the salivary gland secretion of the medicinal leech, a unique representative of invertebrate lysozymes, were analyzed. The destabilase combines the properties of endo-s-lysyl-y-glutamyl isopeptidase (D-dimer monomerase), lysozyme, and chitinase and simultaneously is a nonenzymatic antimicrobial agent. The polypeptide sequence of lysozyme destabilase is encoded by a family of three genes (Ds1, Ds2, and Ds3). The ability of the enzyme to hydrolyze endoisopeptide bonds formed by transglutaminases, which are detected in many pathological conditions, including thrombosis, is considered from the viewpoint of its further application in practice.

Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.

Publication typeEnglish AbstractJournal ArticleResearch Support, Non-U.S. Gov'tReview
Indexed MeSH termsAmino Acid SequenceAnimalsEndopeptidasesHirudo medicinalisMolecular Sequence Data

Summary

Experimental data indicating the polyfunctionality of destabilase, a lysozyme from the salivary gland secretion of the medicinal leech, a unique representative of invertebrate lysozymes, were analyzed.

Why This Matters for Hirudotherapy

This review analyzed experimental data on the polyfunctionality of destabilase, a lysozyme from the salivary gland secretion of the medicinal leech (Hirudo medicinalis). Destabilase uniquely combines endoisopeptidase (D-dimer monomerase), lysozyme, and chitinase activities and also functions as a nonenzymatic antimicrobial agent. This work is directly relevant to the leech salivary secretome and ASH's domain, as the enzyme's ability to hydrolyze endoisopeptide bonds formed by transglutaminases—implicated in pathological conditions including thrombosis—suggests a mechanistic basis for potential therapeutic interest. However, as a review, it synthesizes prior findings rather than presenting new experimental data, and no clinical outcomes, dosing, or translational results are reported; the discussion of practical applications remains conceptual and untested in trial settings.

Citation

[Polyfunctionality of destabilase, a lysozyme from a medicinal leech].

Baskova I, Zavalova L · Bioorganicheskaia khimiia, 2008

DOI

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

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