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*
Laboratory for Immunological Research, Schering-Plough, Dardilly, France; and
DNAX, Research Institute, Palo Alto, CA 94304
We have identified a novel member of the calcium-dependent (C-type)
lectin family. This molecule, designated DCIR (for dendritic cell (DC)
immunoreceptor), is a type II membrane glycoprotein of 237 aa with a
single carbohydrate recognition domain (CRD), closest in homology to
those of the macrophage lectin and hepatic asialoglycoprotein
receptors. The intracellular domain of DCIR contains a consensus
immunoreceptor tyrosine-based inhibitory motif. A mouse cDNA, encoding
a homologous protein has been identified. Northern blot analysis showed
DCIR mRNA to be predominantly transcribed in hematopoietic tissues. The
gene encoding human DCIR was localized to chromosome 12p13, in a region
close to the NK gene complex. Unlike members of this complex, DCIR
displays a typical lectin CRD rather than an NK cell type extracellular
domain, and was expressed on DC, monocytes, macrophages, B lymphocytes,
and granulocytes, but not detected on NK and T cells. DCIR was strongly
expressed by DC derived from blood monocytes cultured with GM-CSF and
IL-4. DCIR was mostly expressed by monocyte-related rather than
Langerhans cell related DC obtained from CD34+ progenitor
cells. Finally, DCIR expression was down-regulated by signals inducing
DC maturation such as CD40 ligand, LPS, or TNF-
. Thus, DCIR is
differentially expressed on DC depending on their origin and stage of
maturation/activation. DCIR represents a novel surface molecule
expressed by Ag presenting cells, and of potential importance in
regulation of DC function.
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