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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Interaction of Bothrops jararaca venom metalloproteinases with protein inhibitors

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Autor(es):
Asega, Amanda F. [1] ; Oliveira, Ana K. [1] ; Menezes, Milene C. [1] ; Neves-Ferreira, Ana Gisele C. [2] ; Serrano, Solange M. T. [1]
Número total de Autores: 5
Afiliação do(s) autor(es):
[1] CeTICS, Inst Butantan, Lab Especial Toxinol Aplicada, BR-05503000 Sao Paulo - Brazil
[2] Fiocruz MS, Inst Oswald Cruz, Lab Toxinol, Rio De Janeiro - Brazil
Número total de Afiliações: 2
Tipo de documento: Artigo Científico
Fonte: Toxicon; v. 80, p. 1-8, MAR 15 2014.
Citações Web of Science: 9
Resumo

Snake venom metalloproteinases (SVMPs) play important roles in the local and systemic hemorrhage observed upon envenomation. In a previous study on the structural elements important for the activities of HF3 (highly hemorrhagic, P-III-SVMP), bothropasin (hemorrhagic, P-III-SVMP) and BJ-PI (non-hemorrhagic, P-I-SVMP), from Bothrops jararaca, it was demonstrated that they differ in their proteolysis profile of plasma and extracellular matrix proteins. In this study, we evaluated the ability of proteins DM43 and alpha 2-macroglobulin to interfere with the proteolytic activity of these SVMPs on fibrinogen and collagen VI and with their ability to induce hemorrhage. DM43 inhibited the proteolytic activity of bothropasin and BJ-PI but not that of HF3, and was not cleaved the three proteinases. On the other hand, alpha 2-macroglobulin did not inhibit any of the proteinases and was rather cleaved by them. In agreement with these findings, binding analysis showed interaction of bothropasin and BJ-PI but not HF3 to DM43 while none of the proteinases bound to alpha 2-macroglobulin. Moreover, DM43 promoted partial inhibition of the hemorrhagic activity of bothropasin but not that of HF3. Our results demonstrate that metalloproteinases of B. jararaca venom showing different domain composition, glycosylation level and hemorrhagic potency show variable susceptibilities to protein inhibitors. (C) 2014 Elsevier Ltd. All rights reserved. (AU)

Processo FAPESP: 98/14307-9 - Center for Applied Toxinology
Beneficiário:Hugo Aguirre Armelin
Linha de fomento: Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs
Processo FAPESP: 10/17328-0 - Caracterização proteômica comparativa da agregação plaquetária induzida pela trombina e pela PA-BJ, uma serinoproteinase do veneno da Bothrops Jararaca
Beneficiário:Ana Karina de Oliveira
Linha de fomento: Bolsas no Brasil - Doutorado
Processo FAPESP: 10/00206-0 - Caracterização molecular da hemorragia induzida pela metaloproteinase HF3: análise das interações com componentes da matriz extracelular, e da regeneração tecidual pós-hemorragia
Beneficiário:Amanda Francine Asega
Linha de fomento: Bolsas no Brasil - Pós-Doutorado