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We have previously shown that a human colon carcinoma cell line (SW1222) expresses a collagen receptor recognizing the Arg-Gly-Asp tripeptide sequence found in collagen. This receptor mediates the cellular attachment to collagen and, subsequently, the glandular differentiation seen in a three-dimensional collagen gel culture. In a search to identify cell surface molecules mediating the adhesion and differentiation of SW1222 cells, we have screened a panel of monoclonal antibodies recognizing epithelial cell surface determinants for their ability to inhibit the collagen binding of SW1222 cells. We have found that four monoclonal antibodies recognizing the 180-kDa carcinoembryonic antigen (CEA) glycoprotein and other members of the CEA family inhibited (up to 87%) the binding of SW1222 cells to type I collagen matrix. Using a cell attachment assay, we have not detected any direct collagen binding of either purified CEA or another CEA-expressing human colon carcinoma cell line (LS174T). These data suggest that CEA is not a collagen-binding protein itself but is likely to be associated with the functional Arg-Gly-Asp collagen receptor expressed by SW1222 cells. We suggest that CEA may function as an accessory molecule, controlling the functional activity of the SW1222 collagen receptor.

Original publication




Journal article


Proc Natl Acad Sci U S A

Publication Date





1541 - 1545


Amino Acid Sequence, Antibodies, Monoclonal, Antigens, Surface, Carcinoembryonic Antigen, Cell Adhesion, Cell Line, Collagen, Colonic Neoplasms, Humans, Kinetics, Molecular Sequence Data, Oligopeptides, Protein Binding, Tumor Cells, Cultured