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Fig. 1. Proteins at concentrations that promote similar levels of cell adhesion [human platelet osteonectin (10 µg ml^–1), osteopontin (4 µg ml^–1), fibronectin (1.25 µg ml^–1) and laminin (2 µg ml^–1)] were coated on 96-well plates and cell adhesion assays were performed as described. Results [mean% binding compared with control, no treatment, (white bars) ± s.d.] are shown for MDA-231 breast carcinoma cells; similar results were obtained with PC-3 prostate carcinoma cells. (A) Anti-integrin blocking antibodies (black bars) ₅, _v, ₅ + _v, ß₁ and _vß₃ inhibited MDA-231 cell binding to human platelet osteonectin and fibronectin while a non-blocking ₅ antibody (striped bar) did not. MDA-231 cell attachment is inhibited to laminin by ₆ and ß₁ anti-integrin antibodies and to osteopontin by ₃, ₆, _v, ß₁, _vß₃ and _vß₅ anti-integrin antibodies. (B) RGD peptide inhibits tumor cell adhesion to human platelet osteonectin at lower concentrations than to fibronectin or osteopontin. RGE was used as the control peptide. *P<0.05, **P<0.01, significant differences were determined in Dunnett's multiple comparison post-test, comparing no treatment (0, white bars) with treatment (peptide or integrin, black bars).

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