Inhibition of induced and spontaneous platelet aggregation by destabilase from medicinal leech
Basic science published in 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.
Resumen
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.
Por qué esto importa para la hirudoterapia
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
Citación
Inhibition of induced and spontaneous platelet aggregation by destabilase from medicinal leech.
Baskova I et al. · Platelets, 2000
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Añadido a la biblioteca ASH: May 27, 2026 · Última actualización del sitio: June 18, 2026