Triflavin, an Arg-Gly-Asp-Containing peptide, inhibits B16-F10 mouse melanoma cell adhesion to matrix proteins via direct binding to tumor cells
Journal
Journal of Biomedical Science
Journal Volume
3
Journal Issue
5
Pages
359-364
Date Issued
1996
Author(s)
Sheu J.R.
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, thereby inhibiting B16-F10 cell adhesion to extracellular matrices. Copyright 1996 S. Karger AG, Basel
Type
journal article