Trigramin, an RGD-containing peptide from snake venom, inhibits cell-substratum adhesion of human melanoma cells.

Abstract

Trigramin, a cysteine-rich, RGD-containing peptide isolated from the venom of the Trimeresurus gramineus snake, inhibited the adhesion of human melanoma cells to fibronectin and fibrinogen. Compared on a molar basis to GRGDSP, trigramin was approximately 500 times more potent than the hexapeptide at inhibiting cell adhesion to fibronectin. The activity of trigramin was abolished by chemical reduction of the molecule, indicating that the secondary structure is important to the biological activity. Trigramin presents an example of an effective inhibitor of cell adhesion that has developed in nature and may prove to be a useful probe in studying the cell surface receptors involved in cell adhesion.

• Authors: K A Knudsen, G P Tuszynski, T F Huang, S Niewiarowski
• Journal: Experimental cell research (Exp Cell Res) Vol. 179 Issue 1 Pg. 42-9 (Nov 1988) ISSN: 0014-4827 [Print] United States
• PMID: 3049127 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Fibronectins
• Integrins
• Intercellular Signaling Peptides and Proteins
• Membrane Glycoproteins
• Oligopeptides
• Peptides
• Snake Venoms
• trigramin
• arginyl-glycyl-aspartic acid
• Fibrinogen

Topics

• Cell Adhesion (drug effects)
• Cells, Cultured
• Fibrinogen (antagonists & inhibitors)
• Fibronectins
• Humans
• Integrins
• Intercellular Signaling Peptides and Proteins
• Melanoma (metabolism, pathology)
• Membrane Glycoproteins (metabolism)
• Microscopy, Phase-Contrast
• Oligopeptides (metabolism)
• Peptides (pharmacology)
• Snake Venoms (analysis)