Echistatin inhibits the adhesion of murine melanoma cells to extracellular matrix components.

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.
AuthorsN Staiano, G R Villani, E Di Martino, C Squillacioti, P Vuotto, P Di Natale
JournalBiochemistry and molecular biology international (Biochem Mol Biol Int) Vol. 35 Issue 1 Pg. 11-9 (Jan 1995) ISSN: 1039-9712 [Print] AUSTRALIA
PMID7735124 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Extracellular Matrix Proteins
  • Peptides
  • Platelet Aggregation Inhibitors
  • Receptors, Fibronectin
  • echistatin
  • Amino Acid Sequence
  • Animals
  • Cell Adhesion (drug effects)
  • Extracellular Matrix Proteins (physiology)
  • Melanoma (pathology)
  • Mice
  • Molecular Sequence Data
  • Peptides (metabolism, pharmacokinetics, pharmacology)
  • Platelet Aggregation Inhibitors
  • Receptors, Fibronectin (metabolism)
  • Time Factors
  • Tumor Cells, Cultured (drug effects)

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