Carcinoembryonic antigen binding to Kupffer cells is via a peptide located at the junction of the N-terminal and first loop domains.
A 11kD glycopeptide has been isolated by pepsin digestion of carcinoembryonic antigen (CEA) that is rapidly endocytosed by isolated rat Kupffer cells and lung alveolar macrophages. Uptake of this glycopeptide by the isolated cells can be inhibited by excess unmodified CEA. Removal of the N-linked oligosaccharide chains by N-glycanase did not alter cellular uptake but reduced the MW to approximately 5500. A seventeen amino acid N-terminal sequence locates this peptide at the junction of the N-terminal and first loop domain of CEA. It is suggested that the recognition of a peptide sequence in this area of CEA is responsible for its clearance from the circulation.
Thomas
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P
Department of Surgery, New England Deaconess Hospital, Harvard Medical School, Boston, MA 02115.
Toth
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CA
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002272:Carcinoembryonic Antigen / Q000032:analysis / Q000378:metabolism*; D006801:Humans; D007728:Kupffer Cells / Q000378:metabolism*; D008168:Lung / Q000166:cytology; D008264:Macrophages / Q000378:metabolism; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats
D002272:Carcinoembryonic Antigen; D010446:Peptide Fragments