Snake venom metalloproteinases: structure/function relationships studies using monoclonal antibodies
dc.creator | Tanjoni, Isabelle | |
dc.creator | Butera, Diego | |
dc.creator | Bento, Luciana | |
dc.creator | Della Casa, Maisa S. | |
dc.creator | Marques Porto, Rafael | |
dc.creator | Takehara, Harumi Ando | |
dc.creator | Gutiérrez, José María | |
dc.creator | Fernandes, Irene | |
dc.creator | Moura Da Silva, Ana M. | |
dc.date.accessioned | 2017-02-07T16:48:19Z | |
dc.date.available | 2017-02-07T16:48:19Z | |
dc.date.issued | 2003-12 | |
dc.description.abstract | Snake 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.procedence | UCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP) | es_ES |
dc.description.sponsorship | Fundação de Amparo à Pesquisa do Estado de São Paulo/[99/12432-3]/FAPESP/Brasil | es_ES |
dc.description.sponsorship | Fundação de Amparo à Pesquisa do Estado de São Paulo/[00/13651-0]/FAPESP/Brasil | es_ES |
dc.description.sponsorship | Conselho Nacional de Desenvolvimento Científico e Tecnológico/[52.0636/1996.1]/CNPq/Brasil | es_ES |
dc.description.sponsorship | Wellcome Trust/[062043]//Inglaterra | es_ES |
dc.identifier.citation | http://www.sciencedirect.com/science/article/pii/S0041010103002964 | |
dc.identifier.doi | 10.1016/j.toxicon.2003.10.010 | |
dc.identifier.issn | 0041-0101 | |
dc.identifier.pmid | 14757212 | |
dc.identifier.uri | https://hdl.handle.net/10669/29507 | |
dc.language.iso | en_US | es_ES |
dc.rights | acceso embargado | |
dc.source | Toxicon; Volumen 42, Número 7, 2003 | es_ES |
dc.subject | Metalloproteinase | es_ES |
dc.subject | Disintegrin | es_ES |
dc.subject | Jararhagin | es_ES |
dc.subject | Collagen | es_ES |
dc.subject | Monoclonal Antibodies | es_ES |
dc.subject | Hemorrhagic Activity | es_ES |
dc.subject | Snake venom | es_ES |
dc.title | Snake venom metalloproteinases: structure/function relationships studies using monoclonal antibodies | es_ES |
dc.type | artículo original |