A peptide sequence on carcinoembryonic antigen binds to a 80kD protein on Kupffer cells.
Clearance of carcinoembryonic antigen (CEA) from the circulation is by binding to Kupffer cells in the liver. We have shown that CEA binding to Kupffer cells occurs via a peptide sequence YPELPK representing amino acids 107-112 of the CEA sequence. This peptide sequence is located in the region between the N-terminal and the first immunoglobulin like loop domain. Using native CEA and peptides containing this sequence complexed with a heterobifunctional crosslinking agent and ligand blotting with biotinylated CEA and NCA we have shown binding to an 80kD protein on the Kupffer cell surface. This binding protein may be important in the development of hepatic metastases.
Thomas
P
P
Department of Surgery, New England Deaconess Hospital, Harvard Medical School, Boston, MA 02115.
Petrick
A T
AT
Toth
C A
CA
Fox
E S
ES
Elting
J J
JJ
Steele
G
G
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002272:Carcinoembryonic Antigen / Q000378:metabolism*; D002478:Cells, Cultured; D002846:Chromatography, Affinity; D007700:Kinetics; D007728:Kupffer Cells / Q000378:metabolism*; D008297:Male; D008565:Membrane Proteins / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010455:Peptides / Q000138:chemical synthesis / Q000378:metabolism*; D051381:Rats; D017207:Rats, Sprague-Dawley; D013329:Structure-Activity Relationship
D002272:Carcinoembryonic Antigen; D008565:Membrane Proteins; D010455:Peptides