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,
Departments of
* Microbiology and
Immunology, and
Regional Primate Research Center, University of Washington, Seattle, WA 98195; and
Department of Immunology, University of Manitoba, Winnipeg, Manitoba, Canada
We have characterized dendritic cell (DC)-associated lectin-1
(DCAL-1), a novel, type II, transmembrane, C-type lectin-like protein.
DCAL-1 has restricted expression in hemopoietic cells, in particular,
DCs and B cells, but T cells and monocytes do not express it. The
DCAL-1 locus is within a cluster of C-type lectin-like
loci on human chromosome 12p12–13 just 3' to the CD69
locus. The consensus sequence of the DCAL-1 gene was confirmed by
RACE-PCR; however, based on sequence alignment with genomic DNA and
with various human expressed sequence tags, we predict that DCAL-1 has
two splice variants. C-type lectins share a common sequence motif of 14
invariable and 18 highly conserved aa residues known as the
carbohydrate recognition domain. DCAL-1, however, is missing three of
the cysteine residues required to form the standard carbohydrate
recognition domain. DCAL-1 mRNA and protein expression are increased
upon the differentiation of monocytes to CD1a+ DCs. B cells
also express high levels of DCAL-1 on their cell surface. Using a
DCAL-1 fusion protein we identified a population of CD4+
CD45RA+ T cells that express DCAL-1 ligand. Coincubation
with soluble DCAL-1 enhanced the proliferation of CD4+ T
cells in response to CD3 ligation and significantly increased IL-4
secretion. In contrast, coincubation with soluble DC-specific
ICAM-3-grabbing nonintegrin (CD209) fusion protein as a control
had no effect on CD4+ T cell proliferation or IL-4 and
IFN-
secretion. Therefore, the function of DCAL-1 on DCs and B cells
may act as a T cell costimulatory molecule, which skews
CD4+ T cells toward a Th2 response by enhancing their
secretion of IL-4.
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