In vivo characterization of Lopap, a prothrombin activator serine protease from the Lonomia obliqua caterpillar venom

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dc.contributor.authorReis, C. V.
dc.contributor.authorFarsky, SHP
dc.contributor.authorFernandes, B. L.
dc.contributor.authorSantoro, M. L.
dc.contributor.authorOliva, MLV
dc.contributor.authorMariano, M.
dc.contributor.authorChudzinski-Tavassi, A. M.
dc.contributor.institutionFAPESP
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionButantan Inst
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T12:31:24Z
dc.date.available2016-01-24T12:31:24Z
dc.date.issued2001-06-01
dc.description.abstractIncreasing occurrence of hemorrhagic syndrome in man, caused by contact with Lonomia obliqua caterpillars, has been reported in Southern Brazil in the past 10 years. the L. obliqua venom causes a severe consumptive coagulopathy, which can lead to hemorrhagic syndrome. L. obliqua prothrombin activator protease (Lopap) is a 69-kDa prothrombin activator serine protease isolated from L. obliqua caterpillar bristle extract, which is able to evoke thrombus formation, unclottable blood, and fibrinogen depletion when injected into the blood stream of rats. the purified protein generated thrombin from prothrombin, able to clot purified human fibrinogen and plasma. A decrease in platelet count and inhibition of collagen-induced platelet aggregation were observed, as well as leukocyte infiltration in the lungs. Ln addition, we observed congestion and hemorrhage in renal glomeruli and necrosis in renal distal tubules. These data support the hypothesis that Lopap contributes to the clinical syndrome caused by human contact with L. obliqua, most probably through prothrombin activation, resulting in a consumption coagulopathy. (C) 2001 Elsevier B.V. All rights reserved.en
dc.description.affiliationFAPESP, Biochem & Biophys Lab, Butantan Inst, Ctr Appl Toxinol,CEPID, BR-05503900 São Paulo, Brazil
dc.description.affiliationFAPESP, Lab Immunochem, Butantan Inst, Ctr Appl Toxinol,CEPID, BR-05503900 São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Dept Microbiol, Inst Biomed Sci, São Paulo, Brazil
dc.description.affiliationButantan Inst, Lab Pathophysiol, São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biochem & Mol Biol, São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Discipline Immunol, São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biochem & Mol Biol, São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Discipline Immunol, São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent437-443
dc.identifierhttp://dx.doi.org/10.1016/S0049-3848(01)00268-7
dc.identifier.citationThrombosis Research. Oxford: Pergamon-Elsevier B.V., v. 102, n. 5, p. 437-443, 2001.
dc.identifier.doi10.1016/S0049-3848(01)00268-7
dc.identifier.issn0049-3848
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/26570
dc.identifier.wosWOS:000169278900007
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofThrombosis Research
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectLonomia obliquaen
dc.subjectcaterpillaren
dc.subjectprothrombin activatoren
dc.subjectcoagulopathyen
dc.titleIn vivo characterization of Lopap, a prothrombin activator serine protease from the Lonomia obliqua caterpillar venomen
dc.typeinfo:eu-repo/semantics/article
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