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.
Резюме
The discovery, purification, and characterization of decorsin, a protein isolated from the North American leech Macrobdella decora, are described.
Почему это важно для гирудотерапии
This study describes the discovery, purification, and characterization of decorsin, a 39-amino-acid protein from the North American leech Macrobdella decora that acts as a potent antagonist of platelet glycoprotein IIb-IIIa and inhibitor of platelet aggregation. Decorsin contains an RGD sequence motif and inhibits fibrinogen binding to GPIIb-IIIa with an IC50 of approximately 1.5 nM, with complete ADP-induced aggregation inhibition at ≤1 µM. For ASH's domain, this is a directly relevant characterization of an antiplatelet agent from the leech secretome, complementing better-known anticoagulant leech proteins. The limitation is that the work is biochemical/in-vitro in nature, involving purification and assay characterization rather than clinical or in-vivo data, and it provides no therapeutic efficacy or safety information.
Цитирование
Связанный клинический контекст
Узнайте, как это исследование связано с клинической практикой
Добавлено в библиотеку ASH: May 27, 2026 · Последнее обновление сайта: June 18, 2026