Triflavin, an Arg-Gly-Asp-Containing peptide, inhibits B16-F10 mouse melanoma cell adhesion to matrix proteins via direct binding to tumor cells

J. R. Sheu, T. F. Huang

Research output: Contribution to journalArticle

6 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)359-364
Number of pages6
JournalJournal of Biomedical Science
Volume3
Issue number5
DOIs
Publication statusPublished - 1996

Fingerprint

Cell-Matrix Junctions
Cell adhesion
Tumors
Melanoma
Cells
glycyl-arginyl-glycyl-aspartyl-serine
Peptides
Cell Adhesion
Fluorescein-5-isothiocyanate
Neoplasms
Proteins
Extracellular Matrix
Vitronectin
Snake Venoms
Collagen Type I
Fibronectins
Fibrinogen
Fluorescence
triflavin
Staining and Labeling

Keywords

  • Extracellulr matrix
  • Melanoma cells
  • RGD-containing peptide
  • Triflavin

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

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title = "Triflavin, an Arg-Gly-Asp-Containing peptide, inhibits B16-F10 mouse melanoma cell adhesion to matrix proteins via direct binding to tumor cells",
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.",
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T1 - Triflavin, an Arg-Gly-Asp-Containing peptide, inhibits B16-F10 mouse melanoma cell adhesion to matrix proteins via direct binding to tumor cells

AU - Sheu, J. R.

AU - Huang, T. F.

PY - 1996

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N2 - 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.

AB - 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.

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