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

BJ-PI2, A non-hemorrhagic metalloproteinase from Bothrops jararaca snake venom

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Author(s):
Ferreira da Silva, Igor Rapp [1] ; Lorenzetti, Raquel [1] ; Renno, Andre Lisboa [1] ; Baldissera, Jr., Lineu [1] ; Zelanis, Andre [2] ; de Toledo Serrano, Solange Maria [2] ; Hyslop, Stephen [1]
Total Authors: 7
Affiliation:
[1] Univ Estadual Campinas UNICAMP, Dept Farmacol, Fac Ciencias Med, BR-13083887 Campinas, SP - Brazil
[2] Inst Butantan, Lab Especial Toxinol Aplicada CAT CEPID, BR-05503900 Sao Paulo - Brazil
Total Affiliations: 2
Document type: Journal article
Source: BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS; v. 1820, n. 11, p. 1809-1821, NOV 2012.
Web of Science Citations: 14
Abstract

Background: Envenoming by Bothrops jararaca can result in local pain, edema, hemorrhage and necrosis, partially mediated by snake venom metalloproteinases (SVMPs). Here, we describe the characterization of BJ-PI2, a P-I class SVMP from B. jararaca venom, and its local tissue actions. Methods: BJ-PI2 was purified by a combination of gel filtration, anion-exchange chromatography and reverse phase HPLC, and identified by mass spectrometry. Clotting and fibrin(ogen)olytic activities were assayed using conventional methods. Hemorrhagic activity and changes in vascular permeability were examined in rat dorsal skin. Myonecrosis and inflammatory activity were examined in mouse gastrocnemius muscle. Results: BJ-PI2 was a 23.08 kDa single-chain polypeptide. Tryptic fragments showed highest homology with SVMP insularinase A from Bothrops insularis, but also with B. jararaca SVMP bothrojaractivase; less similarity was observed with B. jararaca SVMPs BJ-PI and jararafibrases II and IV. BJ-PI2 did not clot fibrinogen or rat citrated plasma but had alpha- and beta-fibrinogenolytic activity (inhibited by EDTA and 1,10-phenanthroline but not by PMSF) and attenuated coagulation after plasma recalcification. BJ-PI2 had fibrinolytic activity. BJ-PI2 increased the vascular permeability of rat dorsal skin (inhibited by 1,10-phenanthroline). BJ-PI2 was not hemorrhagic or myonecrotic but caused migration of inflammatory cells. In contrast, venom was strongly hemorrhagic and myonecrotic but caused less infiltration of inflammatory cells. Conclusions: BJ-PI2 is a non-hemorrhagic, non-myonecrotic, non-coagulant P-I class SVMP that may enhance vascular permeability and inflammatory cell migration in vivo. General significance: BJ-PI2 contributes to enhanced vascular permeability and inflammatory cell migration after envenoming, but not to venom-induced hemorrhage and necrosis. 2012 Elsevier B.V. All rights reserved. (AU)

FAPESP's process: 98/14307-9 - Center for Applied Toxinology
Grantee:Hugo Aguirre Armelin
Support Opportunities: Research Grants - Research, Innovation and Dissemination Centers - RIDC