American Society of Hirudotherapy

Inhibition of induced and spontaneous platelet aggregation by destabilase from medicinal leech

Basic science published in Platelets (2000)

Last Updated: June 18, 2026Reviewed by: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Research reportSalivary PharmacologyDrug DevelopmentBaskova I et al. · Platelets, 2000

Abstract

Destabilase, endo-epsilon-(gamma-Glu)-Lys isopeptidase from the medicinal leech, inhibits arterial thrombus formation in rats. Inhibition of platelet aggregation was supposed to be one of the main mechanisms of this phenomenon. To elucidate this question highly purified destabilase preparations were used. Aggregation was monitored both by a turbidometric method and by a method based on real-time estimation of mean aggregate size. Spontaneous aggregation of human platelets was completely blocked by destabilase. At 5 microM ADP maximal inhibition was 63%. Aggregation induced by PAF (100 nM) and collagen (0.1 mg/ml) was inhibited in the presence of destabilase by 50 and 65%, respectively. This enzyme does not activate adenylate cyclase but inhibits it. We suggest that destabilase interacts with high-affinity binding sites on the platelet plasma membrane, thus providing an anti-aggregating effect. This idea coincides with the data that destabilase primary structure has high homology with some adhesive proteins.

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

Publication typeJournal Article
Indexed MeSH termsAdenosine DiphosphateAdenylyl CyclasesAlprostadilAnimalsBlood PlateletsCardiovascular DiseasesCollagenDose-Response Relationship, DrugEndopeptidasesFibrinolytic AgentsHumansLeeches

Summary

Destabilase completely blocks spontaneous human platelet aggregation and reduces ADP-, PAF-, and collagen-induced aggregation by 50-65%, likely via plasma membrane high-affinity binding sites.

Why This Matters for Hirudotherapy

This study investigated destabilase, an isopeptidase from the medicinal leech that inhibits arterial thrombus formation in rats, focusing on its antiplatelet mechanisms using highly purified preparations monitored by turbidometric and real-time aggregation methods. The findings are relevant to understanding the leech secretome, as destabilase completely blocked spontaneous human platelet aggregation and inhibited ADP-induced aggregation by up to 63%, PAF-induced by 50%, and collagen-induced by 65%. The authors propose that destabilase interacts with high-affinity binding sites on platelet plasma membranes and note its structural homology with adhesive proteins. The study encompasses both in vivo rat thrombosis findings and in vitro human platelet experiments, though no clinical

Citation

Inhibition of induced and spontaneous platelet aggregation by destabilase from medicinal leech.

Baskova I et al. · Platelets, 2000

DOI

Added to ASH library: May 27, 2026 · Site last updated: June 18, 2026

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.