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BIBTEX RIS

“Insularin, a disintegrin from Bothrops insularis venom: Inhibition of platelet aggregation and endothelial cell adhesion by the native and recombinant GST-insularin proteins”

2010; Elsevier BV; Volume: 57; Issue: 1 Linguagem: Inglês

10.1016/j.toxicon.2010.10.013

1879-3150

Maisa S. Della-Casa, Inácio L.M. Junqueira-de-Azevedo, Diego Butera, Patrı́cia Bianca Clissa, Daiana Silva Lopes, Solange M.T. Serrano, Daniel C. Pimenta, Geraldo Santana Magalhães, Paulo Lee Ho, Ana Maria Moura‐da‐Silva,

Cell Adhesion Molecules Research

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, including 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 with glutathione S-transferase (GST-INS). Both native and recombinant insularin inhibited ADP-induced 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.