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Snake venom metalloproteinases: structure/function relationships studies using monoclonal antibodies

dc.creatorTanjoni, Isabelle
dc.creatorButera, Diego
dc.creatorBento, Luciana
dc.creatorDella Casa, Maisa S.
dc.creatorMarques Porto, Rafael
dc.creatorTakehara, Harumi Ando
dc.creatorGutiérrez, José María
dc.creatorFernandes, Irene
dc.creatorMoura Da Silva, Ana M.
dc.date.accessioned2017-02-07T16:48:19Z
dc.date.available2017-02-07T16:48:19Z
dc.date.issued2003-12
dc.description.abstractSnake Venom Metalloproteinases (SVMPs) are synthesized as zymogens and undergo proteolytic processing resulting in a variety of multifunctional proteins. Jararhagin is a P-III SVMP, isolated from the venom of Bothrops jararaca, comprising metalloproteinase, disintegrin-like and cysteine-rich domains. The catalytic domain is responsible for the hemorrhagic activity. The disintegrin-like/cysteine-rich domains block α2β1 integrin binding to collagen and apparently enhance the hemorrhagic activity of SVMPs. The relevance of disintegrin-like domain is described in this paper using a series of mouse anti-jararhagin monoclonal antibodies (MAJar 1–7). MAJar 3 was the only antibody able to completely neutralize jararhagin hemorrhagic activity. Neutralization of catalytic activity was partial by incubation with MAJar 1. MAJars 1 and 3 efficiently neutralized jararhagin binding to collagen with IC50 of 330 and 8.4 nM, respectively. MAJars 1 and 3 recognized the C-terminal portion of the disintegrin domain, which is apparently in conformational proximity with the catalytic domain according to additivity tests. These data suggest that disintegrin-like domain epitopes are in close contact with catalytic site or functionally modulate the expression of hemorrhagic activity in SVMPs.es_ES
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo/[99/12432-3]/FAPESP/Brasiles_ES
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo/[00/13651-0]/FAPESP/Brasiles_ES
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico/[52.0636/1996.1]/CNPq/Brasiles_ES
dc.description.sponsorshipWellcome Trust/[062043]//Inglaterraes_ES
dc.identifier.citationhttp://www.sciencedirect.com/science/article/pii/S0041010103002964
dc.identifier.doi10.1016/j.toxicon.2003.10.010
dc.identifier.issn0041-0101
dc.identifier.pmid14757212
dc.identifier.urihttps://hdl.handle.net/10669/29507
dc.language.isoen_USes_ES
dc.rightsacceso embargado
dc.sourceToxicon; Volumen 42, Número 7, 2003es_ES
dc.subjectMetalloproteinasees_ES
dc.subjectDisintegrines_ES
dc.subjectJararhagines_ES
dc.subjectCollagenes_ES
dc.subjectMonoclonal Antibodieses_ES
dc.subjectHemorrhagic Activityes_ES
dc.subjectSnake venomes_ES
dc.titleSnake venom metalloproteinases: structure/function relationships studies using monoclonal antibodieses_ES
dc.typeartículo original

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