American Society of Hirudotherapy

Proteinase inhibitors from the medicinal leech Hirudo medicinalis

Review published in Biochemistry. Biokhimiia (2001)

Last Updated: November 1, 2026Reviewed by: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Narrative reviewSalivary PharmacologyDrug DevelopmentBaskova I, Zavalova L · Biochemistry. Biokhimiia, 2001

Abstract

The medicinal leech Hirudo medicinalis produces various types of proteinase inhibitors: bdellins (inhibitors of trypsin, plasmin, and acrosin), hirustasin (inhibitor of tissue kallikrein, trypsin, alpha-chymotrypsin, and granulocyte cathepsin G), tryptase inhibitor, eglins (inhibitors of alpha-chymotrypsin, subtilisin, and chymasin and the granulocyte proteinases elastase and cathepsin G), inhibitor of factor Xa, hirudin (thrombin inhibitor), inhibitor of carboxypeptidase, and inhibitor of complement component C1s. This review summarizes data on their primary and tertiary structures, action mechanisms, and biological activities.

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

Publication typeJournal ArticleReview
Indexed MeSH termsAnimalsAntithrombin IIICarboxypeptidasesCarboxypeptidases AComplement Inactivator ProteinsHirudinsHumansInvertebrate HormonesLeechesOrganic ChemicalsProtease InhibitorsProteinsSerine EndopeptidasesSerpinsTryptases

Summary

This review catalogs proteinase inhibitors from the medicinal leech Hirudo medicinalis — including bdellins, hirustasin, eglins, hirudin and inhibitors of factor Xa, carboxypeptidase and complement C1s — summarizing their primary and tertiary structures, mechanisms and biological activities.

Why This Matters for Hirudotherapy

This review summarizes published data on proteinase inhibitors produced by Hirudo medicinalis—including bdellins, hirustasin, eglins, hirudin, and inhibitors of factor Xa, carboxypeptidase, tryptase, and complement component C1s—covering their primary and tertiary structures, action mechanisms, and biological activities. These inhibitors target a range of proteases such as thrombin, plasmin, trypsin, elastase, cathepsin G, tissue kallikrein, and C1s, documenting the molecular diversity of bioactive proteins characterized from a medicinal leech species. The article is directly relevant to the biochemical characterization of leech-derived protease inhibitors, consolidating structural and mechanistic information across multiple inhibitor families. As a review, it presents no new experimental data or clinical findings; its value lies in organizing existing knowledge of these characterized molecules rather than providing original research outcomes.

Citation

Reference (Vancouver style)

Baskova IP, Zavalova LL. Proteinase inhibitors from the medicinal leech Hirudo medicinalis. Biochemistry (Mosc). 2001;66(7):703-714. doi:10.1023/a:1010223325313. PMID: 11563948

Bibliographic details (authors, volume, pages, DOI) are taken from the PubMed record.

DOIPubMed

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This website provides educational information and does not constitute medical advice, diagnosis, or treatment recommendations. Medicinal leech therapy carries clinically meaningful risks and should be performed only by qualified clinicians under institutionally approved protocols. FDA 510(k) clearance for medicinal leeches is limited to specific indications; investigational and off-label discussions are labeled accordingly. For patient-specific guidance, consult a qualified healthcare provider.