Triflavin, an Arg-Gly-Asp-Containing Peptide, Inhibits Human Cervical Carcinoma (HeLa) Cell-Substratum Adhesion Through an RGD-Dependent Mechanism
Resource
PEPTIDES v.15 n.8 pp.1391-1398
Journal
PEPTIDES
Journal Volume
v.15
Journal Issue
n.8
Pages
1391-1398
Date Issued
1994
Date
1994
Author(s)
SHEU, JOEN-RONG
LIN, CHAO-HSINE
PENG, HUI-CHIN
HUANG, TUR-FU
Abstract
Triflavin, an Arg-Gly-Asp-cintaining peptide, inhibits human cervical carcinoma (HeLa) cell-substratum adhesion through an RGD-dependent mechanism. PEPTIDES 15(8) 1391-1398 , 1994.-Triflavin, 1 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 arginie-glycine- aspartic acid (RGD) sequence within each adhesive protein. In this study, we show that triflavin dose-dependently inhibited adhesion of human cerical 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 uptade of HeLa cells during 1 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.#0844#