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*
Institute for Medical Microbiology and Immunology, University of Ulm, Ulm, Germany; and
Department of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden
Dendritic cells (DC) are important APCs that play a key role in the
induction of an immune response. The signaling molecules that govern
early events in DC activation are not well understood. We therefore
investigated whether DC express carcinoembryonic Ag-related cell
adhesion molecule 1 (CEACAM1, also known as BGP or CD66a), a
well-characterized signal-regulating cell-cell adhesion molecule that
is expressed on granulocytes, monocytes, and activated T cells and B
cells. We found that murine DC express in vitro as well as in vivo both
major isoforms of CEACAM1, CEACAM1-L (having a long cytoplasmic domain
with immunoreceptor tyrosine-based inhibitory motifs) and CEACAM1-S
(having a short cytoplasmic domain lacking phosphorylatable tyrosine
residues). Ligation of surface-expressed CEACAM1 on DC with the
specific mAb AgB10 triggered release of the chemokines macrophage
inflammatory protein 1
, macrophage inflammatory protein 2, and
monocyte chemoattractant protein 1 and induced migration of
granulocytes, monocytes, T cells, and immature DC. Furthermore, the
surface expression of the costimulatory molecules CD40, CD54, CD80, and
CD86 was increased, indicating that CEACAM1-induced signaling regulates
early maturation and activation of dendritic cells. In addition,
signaling via CEACAM1 induced release of the cytokines IL-6, IL-12 p40,
and IL-12 p70 and facilitated priming of naive MHC II-restricted
CD4+ T cells with a Th1-like effector phenotype. Hence, our
results show that CEACAM1 is a signal-transducing receptor that can
regulate early maturation and activation of DC, thereby facilitating
priming and polarization of T cell responses.
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