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Insularin, a disintegrin from Bothrops insularis venom: Inhibition ofplatelet aggregation and endothelial cell adhesion by the native andrecombinant GST-insularin proteins
Della Casa, Maisa Splendore; de Azevedo, Inácio Junqueira; Butera, Diego; Clissa, Patrícia Bianca; Lopes, Daiana S; Serrano, Solange M. T; Pimenta, Daniel C; Magalhães, Geraldo S; Ho, Paulo Lee.
Afiliação
  • Della Casa, Maisa Splendore; Instituto Butantan. São Paulo. BR
  • de Azevedo, Inácio Junqueira; Instituto Butantan. São Paulo. BR
  • Butera, Diego; s.af
  • Clissa, Patrícia Bianca; Instituto Butantan. São Paulo. BR
  • Lopes, Daiana S; Instituto Butantan. São Paulo. BR
  • Serrano, Solange M. T; Instituto Butantan. São Paulo. BR
  • Pimenta, Daniel C; Instituto Butantan. São Paulo. BR
  • Magalhães, Geraldo S; Instituto Butantan. São Paulo. BR
  • Ho, Paulo Lee; Instituto Butantan. São Paulo. BR
Toxicon ; Toxicon;57(1): 125-133, Jan. 2011.
Article em En | SES-SP, SESSP-IBPROD, SES-SP, SESSP-IBACERVO | ID: biblio-1068268
Biblioteca responsável: BR78.1
Localização: BR78.1
ABSTRACT
Insularin (INS) was obtained from Bothrops insularis venom by reversed-phase highperformance liquid chromatography using a C18 column and characterized as a disintegrin by peptide mass fingerprint and inhibition of ADP-induced platelet aggregation. A cDNA coding for P-II a metalloproteinase/disintegrin was cloned from a cDNA library from B. insularis venom glands. The deduced protein sequence possesses 73 amino acid residues, ncluding the N-terminal, internal peptides of native insularin, the ARGDNP-sequence and 12 cysteines in a conserved alignment. This cDNA fragment was subcloned in the pGEX-4T-1 vector and expressed in a prokaryotic expression system as a fusion protein withglutathione S-transferase (GST-INS). Both native and recombinant insularin inhibited ADPinduced platelet aggregation and endothelial cells (HUVEC) adhesion with similar activities indicating that GST-INS folded correctly and preserved the integrin-binding loop. Insularin may be a tool in studies that involve platelets and endothelial cell adhesion dependent on alphaIIbeta3 and alphavbeta3 integrins.
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Coleções: 06-national / BR Base de dados: SES-SP / SESSP-IBACERVO / SESSP-IBPROD Assunto principal: Venenos / Agregação Plaquetária / Desintegrinas Limite: Animals Idioma: En Revista: Toxicon Ano de publicação: 2011 Tipo de documento: Article
Buscar no Google
Adicionar na Minha BVS
Imprimir
XML

Coleções: 06-national / BR Base de dados: SES-SP / SESSP-IBACERVO / SESSP-IBPROD Assunto principal: Venenos / Agregação Plaquetária / Desintegrinas Limite: Animals Idioma: En Revista: Toxicon Ano de publicação: 2011 Tipo de documento: Article