Sociedad Americana de Hirudoterapia

Amino acid sequence of piguamerin, an antistasin-type protease inhibitor from the blood sucking leech Hirudo nipponia

Research article published in Eur J Biochem (1998)

Última actualización: June 18, 2026Revisado por: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Preclinical (animal)Genómica y proteómicaFarmacología salivalKim DR et al. · Eur J Biochem, 1998

Abstract

A serine-protease inhibitor of plasma kallikrein was screened and purified from a native Korean leech species, Hirudo nipponia. The peptide, named piguamerin, potently inhibited plasma and tissue kallikreins, and trypsin. Sequence analyses by automated Edman degradation revealed 48 amino acid residues and a molecular mass for the peptide of 5090 Da. Piguamerin is similar to antistasin-type inhibitors with the same spacing of ten cysteine residues, but shows differences from hirustasin, antistasin and ghilanten at the residues surrounding Arg27, which is a common P1 reactive residue for these inhibitors. The purified inhibitor modulated plasma clotting in tests of activated partial thromboplastin time at nanomolar concentrations. The serine-protease inhibitor of this leech may be involved in leech hematophagia.

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

Publication typeJournal ArticleResearch Support, Non-U.S. Gov't
Indexed MeSH termsAmino Acid SequenceAnimalsAnticoagulantsChromatography, High Pressure LiquidInvertebrate HormonesLeechesMolecular Sequence DataMolecular WeightSequence Homology, Amino AcidSerine Proteinase InhibitorsSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Resumen

A serine-protease inhibitor of plasma kallikrein was screened and purified from a native Korean leech species, Hirudo nipponia.

Por qué esto importa para la hirudoterapia

This study isolated and characterized piguamerin, a 48-residue serine protease inhibitor from the Korean leech Hirudo nipponia that potently inhibited plasma and tissue kallikreins and trypsin. Piguamerin shares the antistasin-type ten-cysteine spacing but differs from related inhibitors around the P1 reactive residue Arg27, and the purified peptide modulated plasma clotting in activated partial thromboplastin time tests at nanomolar concentrations. For ASH's domain, this work contributes to characterizing bioactive peptides within the leech secretome, and the authors suggest such inhibitors may be involved in leech hematophagia. The findings are biochemical in nature and do not address therapeutic efficacy or in-vivo application in humans.

Citación

Amino acid sequence of piguamerin, an antistasin-type protease inhibitor from the blood sucking leech Hirudo nipponia.

Kim DR et al. · Eur J Biochem, 1998

DOI

Contexto clínico relacionado

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Añadido a la biblioteca ASH: May 27, 2026 · Última actualización del sitio: June 18, 2026

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