The present study focuses on the question to what extent adhesion and migration of human melanoma cells (MV3) are mediated by integrins or components of the glycocalix. Earlier experiments showed that melanoma cells still adhered to a collagen matrix even when the a2b1 integrin mediated part of cell adhesion was blocked by the snake-venom rhodocetin. To identify the contribution of the glycocalix to cell adhesion and migration, human melanoma cells were seeded on collagen matrices and treated with tunicamycin for different time periods. Tunicamycin prevents the formation of n-acetyl-glucosamine lipid intermediates and glycosylation of newly synthesized proteins by inhibiting N-acetylglucosamin transferases. Tunicamycin led to a decrease of the migratory speed by 25% and a reduction of the number of cells adhesive to the collagen matrix by 20%. We quantified the tunicamycin-dependent loss of the glycocalix by staining the cells with fluorescently labeled wheat germ agglutinine (WGA). Tunicamycin treated cells showed a reduction of fluorescence intensity by 20%. Results imply a basic importance of the glycocalix for cell migration of human melanoma cells.