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dc.creatorRocha, Surza Lucia Gonçalves
dc.creatorLomonte, Bruno
dc.creatorNeves Ferreira, Ana Gisele da Costa
dc.creatorTrugilho, Monique Ramos de Oliveira
dc.creatorJunqueira de Azevedo, Inácio de Loiola Meirelles
dc.creatorHo, Paulo Lee
dc.creatorDomont, Gilberto B.
dc.creatorGutiérrez, José María
dc.creatorPerales, Jonas
dc.date.accessioned2017-02-03T16:47:11Z
dc.date.available2017-02-03T16:47:11Z
dc.date.issued2002-12-11
dc.identifier.citationhttp://onlinelibrary.wiley.com/doi/10.1046/j.1432-1033.2002.03308.x/abstract;jsessionid=9FC017CA1490CBC61E3841B9D8D353C8.f04t04
dc.identifier.issn1742-4658
dc.identifier.urihttps://hdl.handle.net/10669/29488
dc.description.abstractBothrops snake venoms are known to induce local tissue damage such as hemorrhage and myonecrosis. The opossum Didelphis marsupialis is resistant to these snake venoms and has natural venom inhibitors in its plasma. The aim of this work was to clone and study the chemical, physicochemical and biological properties of DM64, an antimyotoxic protein from opossum serum. DM64 is an acidic protein showing 15% glycosylation and with a molecular mass of 63 659 Da when analysed by MALDI-TOF MS. It was cloned and the amino acid sequence was found to be homologous to DM43, a metalloproteinase inhibitor from D. marsupialis serum, and to human α1B-glycoprotein, indicating the presence of five immunoglobulin-like domains. DM64 neutralized both the in vivo myotoxicity and the in vitro cytotoxicity of myotoxins I (mt-I/Asp49) and II (mt-II/Lys49) from Bothrops asper venom. The inhibitor formed noncovalent complexes with both toxins, but did not inhibit the PLA2 activity of mt-I. Accordingly, DM64 did not neutralize the anticoagulant effect of mt-I nor its intracerebroventricular lethality, effects that depend on its enzymatic activity, and which demonstrate the dissociation between the catalytic and toxic activities of this Asp49 myotoxic PLA2. Furthermore, despite its similarity with metalloproteinase inhibitors, DM64 presented no antihemorrhagic activity against Bothrops jararaca or Bothrops asper crude venoms, and did not inhibit the fibrinogenolytic activity of jararhagin or bothrolysin. This is the first report of a myotoxin inhibitor with an immunoglobulin-like structure isolated and characterized from animal blood.es_ES
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico//CNPq/Brasiles_ES
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado do Rio de Janeiro//FAPERJ/Brasiles_ES
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo//FAPESP/Brasiles_ES
dc.description.sponsorshipFundação Oswaldo Cruz//Fiocruz/Brasiles_ES
dc.language.isoen_USes_ES
dc.sourceEuropean Journal of Biochemistry; Volumen 269, Número 24. 2002es_ES
dc.subjectDidelphis marsupialises_ES
dc.subjectInhibitores_ES
dc.subjectMyotoxines_ES
dc.subjectPhospholipasees_ES
dc.subjectSnake venomes_ES
dc.titleFunctional analysis of DM64, an antimyotoxic protein with immunoglobulin-like structure from Didelphis marsupialis serumes_ES
dc.typeartículo científico
dc.identifier.doi10.1046/j.1432-1033.2002.03308.x
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.pmid12473101


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