Abstract
A convulxin (Cvx)-like protein was isolated from Crotalus durissus collilineatus venom by a combination of molecular exclusion and reversed-phase HPLC chromatographies. The molecular mass of the Cvx-like protein in the absence and presence of DTT was 78 kDa and 12-13 kDa, respectively. The Cvx-like protein consisted of two nonidentical polypeptide chains (α and β). The N-terminal amino-acid sequences of the α and β subunits were GLHCPSDWYAYDGHCYKIFNEEMNWED and GFCCPSHWSSYSRYCYKFFSQEMNWEDAEK, respectively, with both subunits having a high content of Glu, Ser, Cys, and Asp. The Cvx-like protein showed high homology with other venom C-type lectins, but had low hemagglutinating activity on intact and trypsinized erythrocytes. The Cvx-like protein stimulated insulin receptor phosphorylation and potentiated insulin secretion from isolated islets in the presence of sub- (2.8 mM) or supra-physiological (16.7 mM) glucose concentrations. These results suggest that the increase in insulin secretion induced by Cvx-like protein may be mediated by a protein tyrosine kinase-dependent pathway and may involve other membrane receptors, such as GP VI or Scr family proteins.
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Toyama, M.H., Carneiro, E.M., Marangoni, S. et al. Isolation and Characterization of a Convulxin-Like Protein from Crotalus durissus collilineatus Venom. J Protein Chem 20, 585–591 (2001). https://doi.org/10.1023/A:1013377331569
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DOI: https://doi.org/10.1023/A:1013377331569