Portal de Periódicos da CAPES

Artigo Produção Nacional Revisado por pares

BIBTEX RIS

Characterization of a monomeric disintegrin, ocellatusin, present in the venom of the Nigerian carpet viper, Echis ocellatus 1

2002; Wiley; Volume: 512; Issue: 1-3 Linguagem: Inglês

10.1016/s0014-5793(02)02233-0

1873-3468

J. Bryan Smith, R.D.G. Theakston, Ana Coelho, Christina Barja‐Fidalgo, Juan J. Calvete, Cezary Marcinkiewicz,

Cell Adhesion Molecules Research

Ocellatusin is a new RGD‐containing short monomeric disintegrin. It is a better inhibitor of α 5 β 1 integrin and a more potent inducer of the expression of a ligand‐induced binding site epitope on β 1 integrin subunit than echistatin. In further contrast to echistatin, ocellatusin has a direct chemotactic stimulus on human neutrophils in vitro. The distinct effects of these two close evolutionarily related disintegrins might be explained by the presence of methionine‐22 and histidine‐29 in the RGD loop of ocellatusin, which are arginine and aspartic acid, respectively, in echistatin. These mutations may modulate the conformation and/or recognition properties of the integrin‐binding loop of ocellatusin.