Triflavin, an Arg-Gly-Asp-Containing Peptide, Inhibits B16-F10 Mouse Melanoma Cell Adhesion to Matrix Proteins via Direct Binding to Tumor Cells.
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
Sheu
J.R.
JR
Graduate Institute of Medical Sciences, Taipei Medical College, National Taiwan University, Taipei, Taiwan.
Huang
T.F.
TF