Tumor cell adhesion to the triple-helical domain of basement membrane (type IV) collagen occurs at several different regions. Cellular recognition of the sequence spanning 1(IV)531-543 has been proposed to be independent of triple-helical conformation (Miles, A. J., Skubitz, A. P. N., Furcht, L. T., and Fields, G. B.(1994) J. Biol. Chem. 269, 30939-30945). In the present study, integrin interactions with a peptide analog of the 1(IV)531-543 sequence have been analyzed. Tumor cell adhesion (melanoma, ovarian carcinoma) to the 1(IV)531-543 chemically synthesized peptide was inhibited by a monoclonal antibody against the integrin subunit, and to a lesser extent by monoclonal antibodies against the and integrin subunits. An anti- monoclonal antibody and normal mouse IgG were ineffective as inhibitors of tumor cell adhesion to the peptide. Two cell surface proteins of 120 and 150 kDa bound to an 1(IV)531-543 peptide affinity column and were eluted with 20 mM EDTA. When the eluted proteins were incubated with monoclonal antibodies against either the or integrin subunit, proteins corresponding in molecular weight to and integrin subunits were precipitated. No proteins were immunoprecipated with monoclonal antibodies against the or integrin subunits. Thus, the integrin from two tumor cell types has been shown to bind directly to the 1(IV)531-543 peptide. The 1(IV)531-543 peptide is the first collagen-like sequence that has been shown to bind the integrin.

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