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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

In vitro cleavage of bioactive peptides by peptidases from Bothrops jararaca venom and its neutralization by bothropic antivenom produced by Butantan Institute: Major contribution of serine peptidases

Texto completo
Autor(es):
Kuniyoshi, Alexandre Kazuo ; Kodama, Roberto Tadashi ; Ferreira Moraes, Luis Henrique ; Duzzi, Bruno ; Iwai, Leo Kei ; Lima, Ismael Feitosa ; Cajado-Carvalho, Daniela ; Portaro, Fernanda Vieira
Número total de Autores: 8
Tipo de documento: Artigo Científico
Fonte: Toxicon; v. 137, p. 114-119, OCT 2017.
Citações Web of Science: 1
Resumo

In Brazil, envenomation by Bothrops pitvipers is responsible for over 73% of snakebites, and their venom is a rich source of proteolytic enzymes. Most studies have demonstrated that Bothrops jararaca venom acts on macromolecular substrates, causing an imbalance in the victim's hemostatic system. In contrast, fewer studies have examined the proteolytic activity on small molecules such as peptides. In this study, we used a set of bioactive peptides (insulin B chain, Met-enkephalin, Leu-enkephalin, neuropeptide Y, peptide YY, pancreatic polypeptide, substance P and somatostatin) to identify new peptide substrates for the metallopeptidases and serine peptidases from the B. jararaca venom. The majority of these peptides were substrates for the venom, but neuropeptide Y and pancreatic polypeptide presented higher hydrolyses rates. Although most of the peptides were simultaneously substrates for both classes of pro teases, serine peptidases were the most active. Substance P was an exclusive substrate for metallopeptidases, while somatostatin was a selective substrate for serine peptidases. The neutralizing efficacy of the bothropic antivenom produced by the Butantan Institute was also assessed and found to totally prevent substance P hydrolysis, whereas somatostatin cleavage was not inhibited. Thus, the antivenom effectively inhibited metallopeptidase activity, but did not neutralize some of the serine peptidases. These results indicate that, in addition to cleaving proteins, the proteolytic enzymes from this venom also hydrolyze bioactive peptides, and this peptidase activity could effectively contribute to some of the many dire manifestations of envenomation. (C) 2017 Elsevier Ltd. All rights reserved. (AU)

Processo FAPESP: 15/13124-5 - Purificação e caracterização de peptídeos presentes nos venenos de serpentes africanas: à procura de inibidores de peptidases de importância médica
Beneficiário:Roberto Tadashi Kodama
Linha de fomento: Bolsas no Brasil - Doutorado
Processo FAPESP: 13/07467-1 - CeTICS - Centro de Toxinas, Imuno-Resposta e Sinalização Celular
Beneficiário:Hugo Aguirre Armelin
Linha de fomento: Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs
Processo FAPESP: 13/15344-7 - Eficácia do soro antibotrópico produzido no Instituto Butantan: obtenção, caracterização e neutralização de serinopeptidases de interesse do veneno de Bothrops Jararaca
Beneficiário:Alexandre Kazuo Kuniyoshi
Linha de fomento: Bolsas no Brasil - Doutorado
Processo FAPESP: 12/06677-0 - Estudo da atividade peptidásica dos venenos botrópicos e do potencial neutralizante do soro produzido no Instituto Butantan sobre esta atividade: novos aspectos sobre o envenenamento botrópico
Beneficiário:Fernanda Calheta Vieira Portaro
Linha de fomento: Auxílio à Pesquisa - Regular
Processo FAPESP: 15/15364-3 - Análise do potencial tóxico de proteases e peptídeos presentes no veneno do escorpião Tityus serrulatus e do poder neutralizante dos antivenenos comerciais: aprimorando o conhecimento do veneno e seu mecanismo de ação
Beneficiário:Fernanda Calheta Vieira Portaro
Linha de fomento: Auxílio à Pesquisa - Regular