Snake venom metalloproteinases: structure/function relationships studies using monoclonal antibodies
| العنوان: | Snake venom metalloproteinases: structure/function relationships studies using monoclonal antibodies |
|---|---|
| المؤلفون: | Luciana Bento, H.A. Takehara, I. Tanjoni, Ana Maria Moura-da-Silva, Maisa S. Della-Casa, Diego Butera, Rafael Marques-Porto, José María Gutiérrez, I. Fernandes |
| المصدر: | Toxicon; Volumen 42, Número 7, 2003 Kérwá Universidad de Costa Rica instacron:UCR |
| بيانات النشر: | Elsevier BV, 2003. |
| سنة النشر: | 2003 |
| مصطلحات موضوعية: | Snake venom, Jararhagin, Hemorrhagic Activity, Hemorrhage, Venom, Biology, Matrix metalloproteinase, Toxicology, Epitope, Mice, Structure-Activity Relationship, Antibody Specificity, Crotalid Venoms, Disintegrin, Animals, Bothrops, Metalloproteinase, Integrin binding, Mice, Inbred BALB C, Antibodies, Monoclonal, Metalloendopeptidases, Monoclonal Antibodies, Biochemistry, Immunology, Metalloproteases, biology.protein, Collagen |
| الوصف: | 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. Fundação de Amparo à Pesquisa do Estado de São Paulo/[99/12432-3]/FAPESP/Brasil Fundação de Amparo à Pesquisa do Estado de São Paulo/[00/13651-0]/FAPESP/Brasil Conselho Nacional de Desenvolvimento Científico e Tecnológico/[52.0636/1996.1]/CNPq/Brasil Wellcome Trust/[062043]//Inglaterra UCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP) |
| تدمد: | 0041-0101 |
| DOI: | 10.1016/j.toxicon.2003.10.010 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0524152bbb21105ed6e5c7025e7436d8 https://doi.org/10.1016/j.toxicon.2003.10.010 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....0524152bbb21105ed6e5c7025e7436d8 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 00410101 |
|---|---|
| DOI: | 10.1016/j.toxicon.2003.10.010 |