Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/200138
Type: Artigo de periódico
Title: Bj-pi2, A Non-hemorrhagic Metalloproteinase From Bothrops Jararaca Snake Venom.
Author: da Silva, Igor Rapp Ferreira
Lorenzetti, Raquel
Rennó, André Lisboa
Baldissera, Lineu
Zelanis, André
Serrano, Solange Maria de Toledo
Hyslop, Stephen
Abstract: 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. 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. BJ-PI2 was a 23.08kDa 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 α- and β-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. 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. BJ-PI2 contributes to enhanced vascular permeability and inflammatory cell migration after envenoming, but not to venom-induced hemorrhage and necrosis.
Subject: Amino Acid Sequence
Animals
Bothrops
Capillary Permeability
Cell Movement
Crotalid Venoms
Hemorrhage
Mass Spectrometry
Metalloproteases
Mice
Molecular Sequence Data
Rats
Rights: fechado
Identifier DOI: 10.1016/j.bbagen.2012.07.011
Address: http://www.ncbi.nlm.nih.gov/pubmed/22867987
Date Issue: 2012
Appears in Collections:Unicamp - Artigos e Outros Documentos

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