Triflavin, an Arg-Gly-Asp-containing peptide, inhibits human cervical carcinoma (HeLa) cell-substratum adhesion through an RGD-dependent mechanism

Joen Rong Sheu, Chao Hsin Lin, Hui Chin Peng, Tur Fu Huang

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Triflavin, a 7.5-kDa cysteine-rich polypeptide purified from Trimeresurus flavoviridis snake venom, belongs to a family of RGD-containing peptides, termed disintegrins, that have been isolated from the venoms of various vipers and shown to be potent inhibitors of platelet aggregation. The interaction of tumor cells with extracellular matrices such as fibronectin, vitronectin, and collagen has been shown to be mediated through a family of cell surface receptors that specifically recognize an arginine-glycine-aspartic acid (RGD) sequence within each adhesive protein. In this study, we show that triflavin dose-dependently inhibited adhesion of human cervical carcinoma (HeLa) cells to extracellular matrices (ECMs; i.e., fibronectin, fibrinogen, and vitronectin). On the other hand, triflavin exerted a limited inhibitory effect on cell adhesion to laminin and collagen (type I and IV). On a molar basis, triflavin is approximately 800 times more potent than Gly-Arg-Gly-Asp-Ser (GRGDS) at inhibiting cell adhesion. When immobilized on plate, triflavin significantly promoted HeLa cell adhesion, and this attachment was inhibited by GRGDS. Furthermore, FITC-conjugated triflavin bound to cells in a saturable manner and its binding was inhibited by GRGDS. In addition, triflavin did not affect [3H]thymidine uptake of HeLa cells during a 3-day incubation. These results suggest that triflavin probably binds to integrin receptors expressed on HeLa cell surface via its RGD sequence within its molecule, thereby inhibiting the adhesion of extracellular matrices to HeLa cells.

Original languageEnglish
Pages (from-to)1391-1398
Number of pages8
JournalPeptides
Volume15
Issue number8
DOIs
Publication statusPublished - 1994
Externally publishedYes

Fingerprint

Cell adhesion
HeLa Cells
Cell Adhesion
glycyl-arginyl-glycyl-aspartyl-serine
Carcinoma
Peptides
Extracellular Matrix
Vitronectin
Fibronectins
Adhesion
Trimeresurus
Viper Venoms
Disintegrins
Military electronic countermeasures
Snake Venoms
Collagen Type IV
triflavin
Fluorescein-5-isothiocyanate
Platelet Aggregation Inhibitors
Cell Surface Receptors

Keywords

  • Cell adhesion
  • RGD-containing peptide
  • Triflavin

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Physiology
  • Cellular and Molecular Neuroscience

Cite this

Triflavin, an Arg-Gly-Asp-containing peptide, inhibits human cervical carcinoma (HeLa) cell-substratum adhesion through an RGD-dependent mechanism. / Sheu, Joen Rong; Lin, Chao Hsin; Peng, Hui Chin; Huang, Tur Fu.

In: Peptides, Vol. 15, No. 8, 1994, p. 1391-1398.

Research output: Contribution to journalArticle

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