Bj-pi2, A Non-hemorrhagic Metalloproteinase From Bothrops Jararaca Snake Venom

dc.creatorDa Silva I.R.F.
dc.creatorLorenzetti R.
dc.creatorRenno A.L.
dc.creatorBaldissera Jr. L.
dc.creatorZelanis A.
dc.creatorSerrano S.M.D.T.
dc.creatorHyslop S.
dc.date2012
dc.date2015-06-26T20:29:40Z
dc.date2015-11-26T14:26:14Z
dc.date2015-06-26T20:29:40Z
dc.date2015-11-26T14:26:14Z
dc.date.accessioned2018-03-28T21:29:13Z
dc.date.available2018-03-28T21:29:13Z
dc.identifier
dc.identifierBiochimica Et Biophysica Acta - General Subjects. , v. 1820, n. 11, p. 1809 - 1821, 2012.
dc.identifier3044165
dc.identifier10.1016/j.bbagen.2012.07.011
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-84865076647&partnerID=40&md5=7755afe2f23520c390a3c1a447fa0d74
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/97115
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/97115
dc.identifier2-s2.0-84865076647
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1246023
dc.descriptionBackground: 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 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. 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.
dc.description1820
dc.description11
dc.description1809
dc.description1821
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dc.languageen
dc.publisher
dc.relationBiochimica et Biophysica Acta - General Subjects
dc.rightsfechado
dc.sourceScopus
dc.titleBj-pi2, A Non-hemorrhagic Metalloproteinase From Bothrops Jararaca Snake Venom
dc.typeArtículos de revistas


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