Amino-acid-sequence determination and biological activity of tessulin, a naturally occurring trypsin-chymotrypsin inhibitor isolated from the leech Theromyzon tessulatum
Biochemistry study published in European Journal of Biochemistry (1998)
Abstract
We purified a new trypsin-chymotrypsin inhibitor, designated tessulin, from the rhynchobdellid leech Theromyzon tessulatum. This 9-kDa peptide was purified to apparent homogeneity by gel-permeation and anion-exchange chromatographies followed by reverse-phase HPLC. The structure of tessulin was determined by reduction, S-beta-pyridylethylation, trypsin digestion, automated Edman degradation and matrix-assisted laser desorption mass spectrometry (m/z 8985 Da). The 81-amino-acid peptide possesses 16 cysteines and exhibits a 16% sequence similarity with antistasin-type inhibitors. Tessulin inhibits trypsin (Ki 1 pM) and chymotrypsin (Ki 150 pM) and exhibits no activity with thrombin, factor Xa, cathepsin G and elastase. This is the first trypsin-chymotrypsin inhibitor isolated from leeches that does not inhibit elastase or cathepsin G, except for cytin and therin. Furthermore, tessulin, in conjunction with other serine-protease inhibitors isolated from Theromyzon (therin, theromin), significantly diminishes the level of human granulocyte and monocyte activation induced by lipopolysaccharides (10 microg). The combined level of inhibition is higher than that of aprotinin, another serine-protease inhibitor used biomedically. Thus, tessulin may be clinically significant in reducing inflammatory events.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Resumen
Purifies and sequences tessulin from rhynchobdellid leech Theromyzon tessulatum — first trypsin-chymotrypsin inhibitor in leeches that does not inhibit elastase. Anti-inflammatory in vitro.
Por qué esto importa para la hirudoterapia
Este estudio purificó y caracterizó la tesulina, un inhibidor de tripsina-quimotripsina de 9 kDa (m/z 8985 Da) procedente de la sanguijuela rincobdélida Theromyzon tessulatum, determinando su secuencia de 81 aminoácidos (16 cisteínas, 16% de similitud con los inhibidores tipo antistasina). La tesulina inhibe la tripsina (Ki 1 pM) y la quimotripsina (Ki 150 pM), pero no muestra actividad frente a la trombina, el factor Xa, la catepsina G o la elastasa, lo cual es único entre los inhibidores de sanguijuela, convirtiéndola en el primer inhibidor de tripsina-quimotripsina de sanguijuela que no inhibe la elastasa ni la catepsina G (exceptuando la citina y la terina). Combinada con la terina y la teromina, la tesulina redujo significativamente la activación de granulocitos y monocitos humanos inducida por LPS, superando a la aprotinina. Esto es relevante para el dominio de la ASH, ya que amplía el catálogo de péptidos bioactivos del secretoma de la sanguijuela con potencial significado antiinflamatorio. Advertencia: el estudio es trabajo bioquímico puramente in vitro, sin datos in vivo ni clínicos, y la tesulina no posee actividad anticoagulante.
Citación
Amino-acid-sequence determination and biological activity of tessulin, a naturally occurring trypsin-chymotrypsin inhibitor isolated from the leech Theromyzon tessulatum.
Chopin V et al. · European journal of biochemistry, 1998
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Añadido a la biblioteca ASH: May 27, 2026 · Última actualización del sitio: 18 de junio de 2026