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Fig. 8. Adhesion to tenascin-W is {alpha}8ß1-integrin dependent. (A) Adhesion assay of T98G glioblastoma cells on tenascin-W coated at 20 µg ml-1. Function-blocking antibodies against specific integrin subunits were included at 10 µg ml-1 as indicated. None of the {alpha}-specific antibodies tested inhibited adhesion, but the anti-ß1 antibody reduced the adhesion to the level of the BSA coating. (B) Adhesion assay of SW480 colon carcinoma cells transfected with {alpha}9 integrin (SW480-{alpha}9) or with the empty plasmid (SW480-mock) on tenascin-W (TN-W), fibronectin (FN) or collagen (COLL). (C) Adhesion assays with {alpha}8-integrin- or mock-transfected K562 leukaemia cells on increasing concentrations of tenascin-W reveals that {alpha}8-transfected cells acquire adhesiveness to tenascin-W. (D) Adhesion of T98G cells to tenascin-W (TN-W, coated at 20 µg ml-1) and fibronectin (FN; coated at 20 µg ml-1) in the presence or absence of PBS, 100 µg ml-1 and 500 µg ml-1 of GRGDS or 500 µg ml-1 SDGRG peptides as indicated.





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