55. Intraspecific Variation of Biological Activities in Venoms from Wild and Captive Bothrops jararaca

Saad, Eduardo; Barros, Luciana Curtolo de; Biscola, Natália P.; Pimenta, Daniel Carvalho; Barraviera, Silvia Regina Sartori Barraviera; Barraviera, Benedito; Ferreira, Rui Seabra

doi:10.1016/j.toxicon.2012.04.056

Cited by 8 publications

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“…Accidents caused by snakes are a serious public health problem in tropical and subtropical countries, due to their incidence, severity and sequelae (Saad et al, 2012). In Brazil, the majority of the venomous snake accidents are caused by Bothrops species (Albuquerque et al, 2013) and the pathophysiology of these envenomations is characterized by three major actions of the venoms: (i) a proteolytic action that causes local lesions and tissue destruction; (ii) a coagulant action that induces blood incoagulability by the consumption of fibrinogen; and (iii) a hemorrhagic action promoted by lesions in the basal membrane of capillaries and the release of hypotensive substances (Cruz et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

BjSP, a novel serine protease from Bothrops jararaca snake venom that degrades fibrinogen without forming fibrin clots

Carone

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Sartim

et al. 2018

Toxicology and Applied Pharmacology

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Snake venom serine proteases (SVSPs) are commonly described as capable of affecting hemostasis by interacting with several coagulation system components. In this study, we describe the isolation and characterization of BjSP from Bothrops jararaca snake venom, a serine protease with distinctive properties. This enzyme was isolated by three consecutive chromatographic steps and showed acidic character (pI 4.4), molecular mass of 28 kDa and N-carbohydrate content around 10%. Its partial amino acid sequence presented 100% identity to a serine protease cDNA clone previously identified from B. jararaca venom gland, but not yet isolated or characterized. BjSP was significantly inhibited by specific serine protease inhibitors and showed high stability at different pH values and temperatures. The enzyme displayed no effects on washed platelets, but was able to degrade fibrin clots in vitro and also the Aα and Bβ chains of fibrinogen differently from thrombin, forming additional fibrinopeptides derived from the Bβ chain, which should be related to its inability to coagulate fibrinogen solutions or platelet-poor plasma. In the mapping of catalytic subsites, the protease showed high hydrolytic specificity for tyrosine, especially in subsite S1. Additionally, its amidolytic activity on different chromogenic substrates suggests possible effects on other factors of the coagulation cascade. In conclusion, BjSP is a serine protease that acts nonspecifically on fibrinogen, generating different Bβ fibrinopeptides and thus not forming fibrin clots. Its distinguished properties in comparison to most SVSPs stimulate further studies in an attempt to validate its potential as a defibrinogenating agent.

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Section: Introductionmentioning

confidence: 99%

BjSP, a novel serine protease from Bothrops jararaca snake venom that degrades fibrinogen without forming fibrin clots

Carone

Menaldo

Sartim

et al. 2018

Toxicology and Applied Pharmacology

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“…Adicionalmente, além desta complexa composição, as peçonhas apresentam grande variabilidade tanto interespécie quanto intraespécie na proporção dos seus componentes, o que se deve a fatores como: origem geográfica, alimentação, idade, gênero, clima, vegetação, crescimento ou não em cativeiro (Meier, 1986;Chippaux et al, 1991;Francischetti et al, 2000;Saldarriaga et al, 2003;Queiroz et al, 2008;Gutiérrez et al, 2009;Boldrini-Franca et al, 2010;Saad et al, 2012).…”

Section: Peçonhasunclassified

IIsolamento e caracterização bioquímica e funcional de um inibidor de metaloproteases presente no soro da serpente Bothrops alternatus

Palacio¹

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“…Além desta grande variedade de componentes, as serpentes apresentam em suas peçonhas, diferenças intra e interespécies quanto à proporção destes. Esta diferença é devido a fatores particulares como: idade, gênero, alimentação, clima, origem geográfica, vegetação, entre outros (BOLDRINI-FRANÇA, 2010;SAAD et al, 2012).…”

Section: Peçonhas De Serpentesunclassified

Caracterização bioquímica e funcional de um inibidor recombinante de miotoxinas, do tipo-?, da serpente Bothrops alternatus

Sousa¹

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, por ter aberto as portas do Laboratório de Toxinologia dando todo o suporte necessário para realização deste trabalho e pela valiosa orientação, contribuindo para minha formação acadêmica e profissional, muito obrigado. Aos meus pais, Lodovico e Rosa, pela compreensão, amor e por todos os esforços dedicados à minha formação, permitindo que eu atingisse este objetivo. Aos meus irmãos, Rafael e Natália, por me apoiarem e acreditarem no meu sucesso. Ao Norival e à Adélia, por todo suporte, por terem compartilhando comigo suas experiências e pela grande contribuição técnica a esta pesquisa.

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55. Intraspecific Variation of Biological Activities in Venoms from Wild and Captive Bothrops jararaca

Cited by 8 publications

References 0 publications

BjSP, a novel serine protease from Bothrops jararaca snake venom that degrades fibrinogen without forming fibrin clots

BjSP, a novel serine protease from Bothrops jararaca snake venom that degrades fibrinogen without forming fibrin clots

IIsolamento e caracterização bioquímica e funcional de um inibidor de metaloproteases presente no soro da serpente Bothrops alternatus

Caracterização bioquímica e funcional de um inibidor recombinante de miotoxinas, do tipo-?, da serpente Bothrops alternatus

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