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KMID : 0360319930250060855
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Journal of Korean Cancer Research Association
1993 Volume.25 No. 6 p.855 ~ p.864
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Functional Role of Carcinoembryonic Antigen in the Intercellular Adhesion of Human Colorectal Carcinoma Cell Lines
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김진천
이시 세이찌/토마스 피터/스틸글렌/제섭존
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Abstract
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Human Carcinoembryonic antigen(CEA) has been known to have an important role in intercellular adhesion of human colorecatal carcinoma cells. The purpose of this study was to verify the functional role of CEA as an adhesion molecule in respect to
the
sequential stream of colorectal tumor cell biology using our consecutive studies reported and ongoing. Two CEA-expressing carcinoma cell lines(KM-12c and CCL-188) and the CEA cDNA transfectants(CEA-1, 17A) bound to CEA, while the CEA-nonproducing
carcinoma cell line(Clone A) and the parental CHO cell lines did not. Monoclonal antibodies to epitopes on CEA that crossreact with nonspecific crossreacting antigen(NCA) (MN3, T84.1, Cl10, MN15), but not the CEA specific antigen(IMMU4, IMMU14).
Inhibited adhesion of CEA-expressing cells to CEA. When the inhibitory anti-CEA antibodies were tested in a competitive radioimmunoassay, two drstinct epitopes(one in the N-terminal domain, the other in the first repeating loop domain) were
identified.
Soluble NCA improved adhesion of KM-12c cells and radiolabelled CEA to CEA on a solid phase. Monoclonal antibodies to an epitope specific to NCA(228.2) or to epitopes on CD44 (j173) inhibited adhesion of KM-12c cells to solid phase CEA. These
suggest
the role of NCA and CD44 as an accessory binding protein in the intercellular adhesion of CEA. The two epitopes of CEA involved in intercellular adhesion were also tested against synthetic peptide including YPELPK residue of CEA molocule that was
known
as the site of Kupffer cell binding by enzyme immunoassay. Both epitopes did not seem to have correspondence to epitope bound to Kupffer cell.
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