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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

DOI

10.1073/pnas.87.4.1541

Type

Journal article

Journal

Proc Natl Acad Sci U S A

Publication Date

02/1990

Volume

87

Pages

1541 - 1545

Keywords

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