Carcinoembryonic antigen functions as an accessory adhesion molecule mediating colon epithelial cell-collagen interactions

Massimo Pignatelli, Helga Durbin, Walter F. Bodmer

Research output: Contribution to journalArticle

105 Citations (Scopus)

Abstract

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 CEAexpressing human colon carcinoma cell line (LS174T). These data suggest that CEA is not a collagen-binding protein itself hut 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 languageEnglish
Pages (from-to)1541-1545
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume87
Issue number4
Publication statusPublished - 1990
Externally publishedYes

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Carcinoembryonic Antigen
Cell Communication
Colon
Collagen
Epithelial Cells
Collagen Receptors
Monoclonal Antibodies
Carcinoma
Cell Line
Collagen Type I
Cell Differentiation
Glycoproteins
Carrier Proteins
Gels

Keywords

  • Arg-Gly-Asp
  • Extracellular matrix
  • Integrin
  • Receptor

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

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abstract = "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 CEAexpressing human colon carcinoma cell line (LS174T). These data suggest that CEA is not a collagen-binding protein itself hut 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.",
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N2 - 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 CEAexpressing human colon carcinoma cell line (LS174T). These data suggest that CEA is not a collagen-binding protein itself hut 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.

AB - 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 CEAexpressing human colon carcinoma cell line (LS174T). These data suggest that CEA is not a collagen-binding protein itself hut 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.

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