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Glycobiology Advance Access published online on August 18, 2004
Glycobiology, doi:10.1093/glycob/cwh139
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Received June 30, 2004
Revised August 13, 2004
Accepted August 13, 2004

ORIGINAL ARTICLES

Identification of Lewisx structures of the cell adhesion molecule CEACAM1 from human granulocytes

Lothar Lucka 1, Malkanthi Fernando 2, Detlef Grunow 1, Christoph Kannicht 3, Andrea K. Horst 2, Peter Nollau 2, Christoph Wagener 2*

1 Charité-Universitätsmedizin Berlin, Campus Benjamin Franklin, Institut für Biochemie und Molekularbiologie, Arnimallee 22, D-14195 Berlin-Dahlem, Germany
2 Universitätsklinkum Hamburg-Eppendorf, Institut für Klinische Chemie, Martinistraße 52, D-20251 Hamburg, Germany
3 Octapharma, Molecular Biochemistry Berlin, Arnimallee 22, D-14195 Berlin, Germany

* To whom correspondence should be addressed. E-mail: wagener{at}uke.uni-hamburg.de.


  Abstract

CEA-related cell adhesion molecule 1 (CEACAM1) is expressed on epithelia, blood vessel endothelia and leukocytes. A variety of physiological functions have been assigned to CEACAM1. It is involved in the formation of glands and blood vessels, in immune reactions and in the regulation of tumor growth. As a homophilic and heterophilic adhesion receptor, it signals through different cellular pathways. The existence of special oligosaccharide structures such as Lewisx or sialyl-Lewisx glycans within this highly glycosylated protein has been postulated, but a chemical proof is missing so far. Since such structures are known to be essential for different cell-cell recognition and adhesion processes, characterizing the CEACAM1 glycan structure is of pivotal importance in revealing the biological function of CEACAM1.

Here, we examined the terminal glycosylation pattern of CEACAM1 from human granulocytes, focusing on Lewisx epitopes. Lewisx-specific antibodies react with immunoaffinity-purified native CEACAM1. Antibody binding was completely abolished by treatment with fucosidase III, confirming a terminal {beta}(1-3,4) fucose linkage to the N-acetylglucosamine of lactosamine residues, a key feature of Lewis epitopes. To verify these data, MALDI-TOF-MS analysis after stepwise exoglycosidase digestion of the CEACAM1 N-glycan mixture was performed. A complex mixture of CEACAM1-bound oligosaccharides could be characterized with an unusually high amount of fucose. The sequential digestions clearly identified several different Lewisx glycan epitopes, which may modulate the cell adhesive functions of CEACAM1.

Keywords: Carcinoembryonic antigen; N-glycan analysis; Lewisx glycan epitope; mass spectrometry; cell adhesion.
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