Decorsin. A potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor from the leech Macrobdella decora
Research article published in The Journal of biological chemistry (1990)
Abstract
The discovery, purification, and characterization of decorsin, a protein isolated from the North American leech Macrobdella decora, are described. Decorsin acts as an antagonist of platelet glycoprotein IIb-IIIa (GPIIb-IIIa), and is a potent inhibitor of platelet aggregation. The protein was purified to apparent homogeneity from crude whole leech extracts by treatment with trifluoroacetic acid followed by GPIIb-IIIa affinity chromatography and C18 reverse-phase high performance liquid chromatography. Decorsin was also isolated from a solution of leech ingestate by treatment with trifluoroacetic acid followed by C18 reverse-phase high performance liquid chromatography. The primary sequence of decorsin indicates that the protein is 39 amino acids long and contains 6 cysteine and 6 proline residues, as well as the sequence Arg-Gly-Asp, (RGD), a proposed recognition site of many adhesion proteins. A molecular mass of 4379 was obtained by fast atom bombardment mass spectrometry and is consistent with the mass calculated from the observed sequence. Evidence for an N-3 isoform, lacking the first 3 amino-terminal residues is also presented. Both decorsin and the N-3 isoform inhibit GP IIb-IIIa binding to immobilized fibrinogen with an IC50 of approximately 1.5 nM. Human platelet aggregation induced by ADP is inhibited by decorsin with an IC50 of approximately 500 nM; complete inhibition was observed at less than or equal to 1 microM. Based on overall sequence homology, decorsin does not belong to the family of GPIIb-IIIa protein antagonists that is found in snake venoms (Dennis, M. S., Henzel, W. J., Pitti, R. M., Lipari, M. T., Napier, M. A., Deisher, T. A., Bunting, S., and Lazarus, R. A. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 2471-2475); however the carboxyl-terminal RGD-containing region from residues 27 to 38 of decorsin is approximately 60% homologous with the corresponding region of the snake venom proteins, suggesting that high affinity binding of these proteins to GPIIb-IIIa is defined by this epitope.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Resumen
The discovery, purification, and characterization of decorsin, a protein isolated from the North American leech Macrobdella decora, are described.
Por qué esto importa para la hirudoterapia
Este estudio describe el descubrimiento, la purificación y la caracterización de la decorsina, una proteína de 39 aminoácidos de la sanguijuela norteamericana Macrobdella decora que actúa como un potente antagonista de la glicoproteína IIb-IIIa plaquetaria y como inhibidor de la agregación plaquetaria. La decorsina contiene un motivo de secuencia RGD e inhibe la unión del fibrinógeno a GPIIb-IIIa con una IC50 de aproximadamente 1,5 nM, con inhibición completa de la agregación inducida por ADP a ≤1 µM. Para el ámbito de la ASH, esta es una caracterización directamente relevante de un agente antiplaquetario del secretoma de la sanguijuela, que complementa las proteínas anticoagulantes de la sanguijuela más conocidas. La limitación es que el trabajo es de naturaleza bioquímica/in vitro, Involucra purificación y caracterización mediante ensayos en lugar de datos clínicos o in vivo, y no aporta información sobre eficacia o seguridad terapéutica.
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Añadido a la biblioteca ASH: May 27, 2026 · Última actualización del sitio: 18 de junio de 2026