Triflavin, an antiplatelet peptide, inhibits tumor cell-extracellular matrix adhesion through an arginine-glycine-aspartic acid-dependent mechanism.

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

The interaction of tumor cells with extracellular matrix components such as laminin, fibronectin, and collagen has been shown to be mediated through a family of cell-surface receptors that specifically recognize an arginine-glycine-aspartic acid amino acid sequence within each protein. Triflavin, a 7.5 kDa cysteine-rich polypeptide purified from Trimeresurus flavoviridis snake venom, belongs to a family of arginine-glycine-aspartic acid-containing peptides termed disintegrins that have been isolated from the venoms of various vipers and shown to be potent inhibitors of platelet aggregation. In this study, we showed that triflavin inhibited adhesion of human hepatoma J-5 cells to extracellular matrices (fibronectin, vitronectin, fibrinogen, and collagen type I) in a dose-dependent manner. On the other hand, triflavin exerted a limited inhibitory effect on cell attachment to collagen type IV and laminin (<or = 40%). Triflavin is approximately 1000 times more potent than glycine-arginine-glycine-aspartic acid-serine at inhibiting cell adhesion. When immobilized on plate, triflavin promoted J-5 cell attachment; this attachment was inhibited by glycine-arginine-glycine-aspartic acid-serine. In addition, triflavin labeled with iodine 125 binds to J-5 cells in a saturable manner and its binding was also inhibited by glycine-arginine-glycine-aspartic acid-serine. Its Kd value was estimated to be 3.9 x 10(-7) mol/L and the number of binding sites was around 60,000 per cell. Furthermore, triflavin did not affect tritiated thymidine uptake during a 3-day incubation.(ABSTRACT TRUNCATED AT 250 WORDS)

Original languageEnglish
Pages (from-to)256-263
Number of pages8
JournalJournal of Laboratory and Clinical Medicine
Volume123
Issue number2
Publication statusPublished - Feb 1994
Externally publishedYes

Fingerprint

Cell-Matrix Junctions
Aspartic Acid
Glycine
Extracellular Matrix
Arginine
Tumors
Adhesion
Cells
Peptides
Neoplasms
Serine
Laminin
Fibronectins
Trimeresurus
Viper Venoms
Disintegrins
Vitronectin
Snake Venoms
Collagen Type IV
triflavin

ASJC Scopus subject areas

  • Medicine(all)
  • Pathology and Forensic Medicine

Cite this

@article{4eadadfbbb32420cb91518c4ccece7d5,
title = "Triflavin, an antiplatelet peptide, inhibits tumor cell-extracellular matrix adhesion through an arginine-glycine-aspartic acid-dependent mechanism.",
abstract = "The interaction of tumor cells with extracellular matrix components such as laminin, fibronectin, and collagen has been shown to be mediated through a family of cell-surface receptors that specifically recognize an arginine-glycine-aspartic acid amino acid sequence within each protein. Triflavin, a 7.5 kDa cysteine-rich polypeptide purified from Trimeresurus flavoviridis snake venom, belongs to a family of arginine-glycine-aspartic acid-containing peptides termed disintegrins that have been isolated from the venoms of various vipers and shown to be potent inhibitors of platelet aggregation. In this study, we showed that triflavin inhibited adhesion of human hepatoma J-5 cells to extracellular matrices (fibronectin, vitronectin, fibrinogen, and collagen type I) in a dose-dependent manner. On the other hand, triflavin exerted a limited inhibitory effect on cell attachment to collagen type IV and laminin (",
author = "Sheu, {J. R.} and Chien-Huang Lin and Huang, {T. F.}",
year = "1994",
month = "2",
language = "English",
volume = "123",
pages = "256--263",
journal = "Translational Research",
issn = "1931-5244",
publisher = "Mosby Inc.",
number = "2",

}

TY - JOUR

T1 - Triflavin, an antiplatelet peptide, inhibits tumor cell-extracellular matrix adhesion through an arginine-glycine-aspartic acid-dependent mechanism.

AU - Sheu, J. R.

AU - Lin, Chien-Huang

AU - Huang, T. F.

PY - 1994/2

Y1 - 1994/2

N2 - The interaction of tumor cells with extracellular matrix components such as laminin, fibronectin, and collagen has been shown to be mediated through a family of cell-surface receptors that specifically recognize an arginine-glycine-aspartic acid amino acid sequence within each protein. Triflavin, a 7.5 kDa cysteine-rich polypeptide purified from Trimeresurus flavoviridis snake venom, belongs to a family of arginine-glycine-aspartic acid-containing peptides termed disintegrins that have been isolated from the venoms of various vipers and shown to be potent inhibitors of platelet aggregation. In this study, we showed that triflavin inhibited adhesion of human hepatoma J-5 cells to extracellular matrices (fibronectin, vitronectin, fibrinogen, and collagen type I) in a dose-dependent manner. On the other hand, triflavin exerted a limited inhibitory effect on cell attachment to collagen type IV and laminin (

AB - The interaction of tumor cells with extracellular matrix components such as laminin, fibronectin, and collagen has been shown to be mediated through a family of cell-surface receptors that specifically recognize an arginine-glycine-aspartic acid amino acid sequence within each protein. Triflavin, a 7.5 kDa cysteine-rich polypeptide purified from Trimeresurus flavoviridis snake venom, belongs to a family of arginine-glycine-aspartic acid-containing peptides termed disintegrins that have been isolated from the venoms of various vipers and shown to be potent inhibitors of platelet aggregation. In this study, we showed that triflavin inhibited adhesion of human hepatoma J-5 cells to extracellular matrices (fibronectin, vitronectin, fibrinogen, and collagen type I) in a dose-dependent manner. On the other hand, triflavin exerted a limited inhibitory effect on cell attachment to collagen type IV and laminin (

UR - http://www.scopus.com/inward/record.url?scp=0028371958&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028371958&partnerID=8YFLogxK

M3 - Article

C2 - 8301202

AN - SCOPUS:0028371958

VL - 123

SP - 256

EP - 263

JO - Translational Research

JF - Translational Research

SN - 1931-5244

IS - 2

ER -