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rdf:type |
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lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0018183,
umls-concept:C0020792,
umls-concept:C0026473,
umls-concept:C0086418,
umls-concept:C0205314,
umls-concept:C0679622,
umls-concept:C1171362,
umls-concept:C1515670,
umls-concept:C1539106,
umls-concept:C1880022
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pubmed:issue |
15
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pubmed:dateCreated |
2004-4-6
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pubmed:databankReference |
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pubmed:abstractText |
Inhibitory and activatory C-type lectin-like receptors play an important role in immunity through the regulation of leukocytes. Here, we report the identification and characterization of a novel myeloid inhibitory C-type lectin-like receptor (MICL) whose expression is primarily restricted to granulocytes and monocytes. This receptor, which contains a single C-type lectin-like domain and a cytoplasmic immunoreceptor tyrosine-based inhibitory motif, is related to LOX-1 (lectin-like receptor for oxidized low density lipoprotein-1) and the beta-glucan receptor (Dectin-1) and is variably spliced and highly N-glycosylated. We demonstrate that it preferentially associates with the signaling phosphatases SHP-1 and SHP-2, but not with SHIP. Novel chimeric analyses with a construct combining MICL and the beta-glucan receptor show that MICL can inhibit cellular activation through its cytoplasmic immunoreceptor tyrosine-based inhibitory motif. These data suggest that MICL is a negative regulator of granulocyte and monocyte function.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14792-802
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14739280-Alternative Splicing,
pubmed-meshheading:14739280-Amino Acid Motifs,
pubmed-meshheading:14739280-Amino Acid Sequence,
pubmed-meshheading:14739280-Animals,
pubmed-meshheading:14739280-Base Sequence,
pubmed-meshheading:14739280-Blotting, Northern,
pubmed-meshheading:14739280-CHO Cells,
pubmed-meshheading:14739280-Cell Line,
pubmed-meshheading:14739280-Cloning, Molecular,
pubmed-meshheading:14739280-Cricetinae,
pubmed-meshheading:14739280-Cytoplasm,
pubmed-meshheading:14739280-Glycosylation,
pubmed-meshheading:14739280-Granulocytes,
pubmed-meshheading:14739280-Humans,
pubmed-meshheading:14739280-Lectins, C-Type,
pubmed-meshheading:14739280-Mice,
pubmed-meshheading:14739280-Models, Biological,
pubmed-meshheading:14739280-Molecular Sequence Data,
pubmed-meshheading:14739280-Monocytes,
pubmed-meshheading:14739280-NIH 3T3 Cells,
pubmed-meshheading:14739280-Phylogeny,
pubmed-meshheading:14739280-Precipitin Tests,
pubmed-meshheading:14739280-Protein Binding,
pubmed-meshheading:14739280-Protein Structure, Tertiary,
pubmed-meshheading:14739280-RNA,
pubmed-meshheading:14739280-RNA, Messenger,
pubmed-meshheading:14739280-Rats,
pubmed-meshheading:14739280-Receptors, LDL,
pubmed-meshheading:14739280-Receptors, Mitogen,
pubmed-meshheading:14739280-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:14739280-Sequence Homology, Amino Acid,
pubmed-meshheading:14739280-Signal Transduction,
pubmed-meshheading:14739280-Spectrometry, Fluorescence,
pubmed-meshheading:14739280-Tissue Distribution,
pubmed-meshheading:14739280-Transfection,
pubmed-meshheading:14739280-Tumor Necrosis Factor-alpha
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pubmed:year |
2004
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pubmed:articleTitle |
Identification and characterization of a novel human myeloid inhibitory C-type lectin-like receptor (MICL) that is predominantly expressed on granulocytes and monocytes.
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pubmed:affiliation |
Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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