APCs Express DCIR, a Novel C-Type Lectin Surface Receptor Containing an Immunoreceptor Tyrosine-Based Inhibitory Motif

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...

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Bibliographic Details
Published in:The Journal of immunology (1950) 1999-08, Vol.163 (4), p.1973-1983
Main Authors: Bates, Elizabeth E. M, Fournier, Nathalie, Garcia, Eric, Valladeau, Jenny, Durand, Isabelle, Pin, Jean-Jacques, Zurawski, Sandra M, Patel, Sejal, Abrams, John S, Lebecque, Serge, Garrone, Pierre, Saeland, Sem
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
B-Lymphocytes - metabolism
Base Sequence
Cell Differentiation - genetics
Cell Differentiation - immunology
Cells, Cultured
Chromosomes, Human, Pair 12
Cloning, Molecular
Dendritic Cells - cytology
Dendritic Cells - immunology
Dendritic Cells - metabolism
DNA, Complementary - isolation & purification
Gene Dosage
Hematopoietic Stem Cells - metabolism
Humans
Intracellular Fluid - metabolism
Lectins, C-Type
Liver - metabolism
Lymphoid Tissue - metabolism
Macrophages - immunology
Macrophages - metabolism
Membrane Glycoproteins - biosynthesis
Membrane Glycoproteins - chemistry
Membrane Glycoproteins - genetics
Mice
Molecular Sequence Data
Multigene Family - immunology
Organ Specificity - genetics
Peptide Fragments - biosynthesis
Peptide Fragments - chemistry
Peptide Fragments - genetics
Receptors, Immunologic
Receptors, Mitogen - biosynthesis
Receptors, Mitogen - chemistry
Receptors, Mitogen - genetics
Sequence Homology, Amino Acid
Tyrosine - metabolism
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Summary: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-alpha. 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.
ISSN:0022-1767
1550-6606
DOI:10.4049/jimmunol.163.4.1973