Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/10692
Title: Interaction of Bothrops jararaca venom metalloproteinases with protein inhibitors
Authors: Asega, Amanda F.
Oliveira, Ana K.
Menezes, Milene C.
Ferreira, Ana Gisele C. Neves
Serrano, Solange M. T.
Affilliation: Instituto Butantan. Laboratório Especial de Toxinologia Aplicada-CeTICS. São Paulo, SP, Brasil.
Instituto Butantan. Laboratório Especial de Toxinologia Aplicada-CeTICS. São Paulo, SP, Brasil.
Instituto Butantan. Laboratório Especial de Toxinologia Aplicada-CeTICS. São Paulo, SP, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxonologia. Rio de Janeiro, RJ, Brasil.
Instituto Butantan. Laboratório Especial de Toxinologia Aplicada-CeTICS. São Paulo, SP, Brasil.
Abstract: 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 a2- 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, a2-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 a2-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.
Keywords: Hemorrhage
Inhibition
Metalloproteinase
Proteolysis
Snake venom
keywords: Inibição
DeCS: Hemorragia
Proteolysis
Metalloproteinase
Venenos de Serpentes
Issue Date: 2014
Publisher: Elsevier
Citation: ASEGA, Amanda F. et al. Interaction of Bothrops jararaca venom metalloproteinases with protein inhibitors. Toxicon, v. 80, p.1-8, Mar. 2014.
DOI: 10.1016/j.toxicon.2014.01.001
ISSN: 0041-0101
Copyright: open access
Appears in Collections:IOC - Artigos de Periódicos

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