Add time:07/31/2019         Source:sciencedirect.com

Peptides containing the integrin recognition sequence, RGD, can inhibit experimental metastasis of mouse melanoma cells, but the integrin(s) affected in these experiments is unknown. Besides “classical” RGD-binding integrins such as α5β1 and αvβ3, RGD has been reported to bind α4β1, and mAbs to α4β1 can inhibit melanoma metastasis. We investigated the mode of action of the disintegrin eristostatin (cas 132051-67-3), an RGD-containing peptide isolated from snake venom, in a human melanoma experimental metastasis model. Lung colonization following i.v. injection of MV3 cells in nude mice was strongly inhibited by eristostatin. MV3 cells bound FITC-eristostatin and adhered to eristostatin-coated wells. This adhesion was partially inhibited by a GRGDSP peptide and by α4 mAb. Binding of FITC-eristostatin to Jurkat cells and adhesion of Jurkat (but not K562) cells to eristostatin-coated wells further suggested that eristostatin binds α4β1, even though, again, α4 mAb only partially inhibited adhesion. Expression of α4β1 was enhanced in metastatic melanoma cells compared to normal melanocytes and nonmetastatic melanoma cells. Finally, eristostatin inhibited adhesion of both MV3 and CHOα4 cells to the α4β1-ligand VCAM-1, while adhesion to other ligands via other integrins was not affected. These findings demonstrate that inhibition of melanoma cell metastasis by RGD-containing peptides such as eristostatin, may be due to interference with α4β1-VCAM binding, in addition to inhibition of the classical RGD-binding integrins.

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