Advanced search
Start date
Betweenand
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Interaction of Bothrops jararaca venom metalloproteinases with protein inhibitors

Full text
Author(s):
Asega, Amanda F. [1] ; Oliveira, Ana K. [1] ; Menezes, Milene C. [1] ; Neves-Ferreira, Ana Gisele C. [2] ; Serrano, Solange M. T. [1]
Total Authors: 5
Affiliation:
[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
Total Affiliations: 2
Document type: Journal article
Source: Toxicon; v. 80, p. 1-8, MAR 15 2014.
Web of Science Citations: 8
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 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)

FAPESP's process: 98/14307-9 - Center for Applied Toxinology
Grantee:Hugo Aguirre Armelin
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 10/00206-0 - Molecular characterization of the hemorrhage induced by the metalloproteinase HF3: analysis of its interaction with extracellular matrix components and of the hemorrhagic tissue regeneration.
Grantee:Amanda Francine Asega
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 10/17328-0 - Comparative proteomic characterization of platelet aggregation induced by thrombin and PA-BJ, a serine proteinase from the venom of Bothrops jararaca.
Grantee:Ana Karina de Oliveira
Support type: Scholarships in Brazil - Doctorate