Echistatin inhibits the adhesion of murine melanoma cells to extracellular matrix components.
Biochem Mol Biol Int
; 35(1): 11-9, 1995 Jan.
Article
em En
| MEDLINE
| ID: mdl-7735124
ABSTRACT
Echistatin, an RGD containing peptide isolated from Echis carinatus snake venom, inhibited the in vitro attachment of B16-BL6 mouse melanoma cells to fibronectin, vitronectin and laminin. Its inhibitory activity on cell adhesion was non-cytotoxic, dose-dependent and fully reversible. Kinetic analysis showed a competitive type of inhibition for all the three substrates examined here. Chemical reduction and alkylation of echistatin almost abolished its effect on cell adhesion to extracellular matrix components. Native echistatin was also able to inhibit B16-BL6 cell attachment to IgG antihuman fibronectin receptor-coated wells, thus suggesting that the molecule binds to adhesive receptors on melanoma cell surface. Our results indicate that echistatin is an useful disintegrin for research on cell adhesion.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Proteínas da Matriz Extracelular
/
Melanoma
Limite:
Animals
Idioma:
En
Revista:
Biochem Mol Biol Int
Ano de publicação:
1995
Tipo de documento:
Article