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dc.creatorRucavado Romero, Alexandra
dc.creatorSoto Morera, Mónica
dc.creatorKamiguti, Aura S.
dc.creatorTheakston, R. David G.
dc.creatorFox, Jay W.
dc.creatorEscalante Muñoz, Teresa
dc.creatorGutiérrez, José María
dc.date.accessioned2017-01-31T16:10:34Z
dc.date.available2017-01-31T16:10:34Z
dc.date.issued2001-04
dc.identifier.citationhttps://th.schattauer.de/en/contents/archive/issue/869/manuscript/2737.htmles_ES
dc.identifier.issn0340-6245
dc.identifier.urihttp://hdl.handle.net/10669/29475
dc.description.abstractThrombocytopenia occurs in a number of patients bitten by Bothrops asper, a species responsible for the majority of snakebites in Central America and southern Mexico. In this work we describe the isolation of a new platelet-aggregating protein, named aspercetin, from the venom of B. asper, which induces thrombocytopenia in mice. Isolation was carried out by a combination of ion-exchange chromatography on DEAE-Sepharose and affinity chromatography on Affi-Gel Blue. Aspercetin is a disulfide-linked heterodimer, with a pI of 4.5 and a molecular mass of 29,759 Da, detemined by MALDI-ESI mass spectrometry. N-terminal sequence shows homology with a number of venom proteins which belong to the C-type lectin family. Aspercetin has functional similarities with botrocetin, from B. jararaca venom, since it induces platelet aggregation only in the presence of plasma or purified von Willebrand factor. Aspercetin-mediated platelet aggregation results from the interaction of von Willebrand factor with platelet receptor GPIb. Aspercetin lacks anticoagulant effect and does not agglutinate erythrocytes, in contrast with other representatives of the C-type lectin family isolated from snake venoms. Moreover, aspercetin is not lethal, nor does it induce myonecrosis, hemorrhage and edema. When injected intravenously or intramuscularly in mice it induces a rapid, dose-dependent drop in platelet counts and prolongs the bleeding time, suggesting that it may play a role in the thrombocytopenia that develops in a number of B. asper envenomations. Moreover, mice injected intravenously with aspercetin and then receiving an intradermal injection of B. asper hemorrhagic metalloproteinase BaP1 develop a larger hemorrhagic lesion than mice receiving only BaP1. This suggests that aspercetin, by reducing platelet numbers, may contribute to the hemorrhagic effect characteristic of B. asper envenomations.es_ES
dc.description.sponsorshipInternational Foundation for Science/[F2707-2]/IFS/Sueciaes_ES
dc.description.sponsorshipUniversidad de Costa Rica /[741-98-505]/UCR/Costa Ricaes_ES
dc.language.isoen_USes_ES
dc.sourceThrombosis and Haemostasis; Volumen 85, Número 4. 2001es_ES
dc.subjectPlatelet aggregationes_ES
dc.subjectBothrops asper venomes_ES
dc.subjectAspercetines_ES
dc.subjectC-type lectines_ES
dc.subjectHemorrhagees_ES
dc.subjectThrombocytopeniaes_ES
dc.subjectSnake venomes_ES
dc.titleCharacterization of aspercetin, a platelet aggregating component from the venom of the snake Bothrops asper which induces thrombocytopenia and potentiates metalloproteinase-induced hemorrhagees_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.description.procedenceUCR::Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.codproyecto741-98-505
dc.identifier.pmid11341509


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