Abstract
Triflavin, an Arg-Gly-Asp (RGD)-containing snake venom peptide, inhibits B16-F10 mouse melanoma cell adhesion to extracellular matrices, e.g., fibronectin, vitronectin, fibrinogen, and collagen type I. In this study, GRGDS inhibits B16-F10 mouse melanoma cell adhesion to immobilized triflavin in a dose-dependent manner. In addition, flow-cytometric analysis and the fluorescence staining method in which FITC-triflavin is utilized as a binding ligand were used. GRGDS inhibits the binding of FITC-triflavin to B16-F10 cells. Additionally, the above results suggest that triflavin directly binds to its receptors expressed on B16-F10 cell surface primarily via its RGD sequence, there-by inhibiting B16-F10 cell adhesion to extracellular matrices.
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Sheu, J.R., Huang, T.F. Triflavin, an Arg-Gly-Asp-containing peptide, inhibits B16-F10 mouse melanoma cell adhesion to matrix proteins via direct binding to tumor cells. J Biomed Sci 3, 359–364 (1996). https://doi.org/10.1007/BF02257966
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DOI: https://doi.org/10.1007/BF02257966