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rdf:type |
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lifeskim:mentions |
umls-concept:C0021081,
umls-concept:C0425152,
umls-concept:C0591833,
umls-concept:C0597357,
umls-concept:C0871261,
umls-concept:C1156673,
umls-concept:C1540289,
umls-concept:C1548602,
umls-concept:C1704259,
umls-concept:C1704632,
umls-concept:C1705987,
umls-concept:C1706817,
umls-concept:C1956385,
umls-concept:C2911692
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pubmed:issue |
6
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pubmed:dateCreated |
2004-9-9
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pubmed:abstractText |
In this study, using a soluble CD200-Ig fusion protein, we provide evidence that murine dendritic cells (DCs) possess a functional CD200R, whose engagement results in the reinforcement or appearance of immunosuppressive properties in these cells. In particular, the plasmacytoid subset (CD11c+B220+120G8+) of splenic DCs (pDCs) is induced by CD200-Ig to express the enzyme IDO, which initiates the tolerogenic pathway of tryptophan catabolism. As a result, pDCs are capable of suppressing Ag-specific responses in vivo when transferred into recipient hosts after treatment with CD200-Ig. IDO induction in pDCs through CD200R engagement requires type I IFNR signaling. Although the release of IFN-alpha may contribute to the full expression of CD200-Ig activity, autocrine IFN-alpha is unlikely to mediate alone the effects of CD200R engagement. These data prospect novel functions for both pDCs and the CD200-CD200R pair in the mouse. At the same time, these data underscore the possible unifying role of the IDO mechanism in immune tolerance.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/CD200 receptor, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cd200r1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Dioxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Indoleamine-Pyrrole 2,3,-Dioxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Interferon alpha-beta,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interferon,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/antigens, CD200
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0022-1767
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2004 The American Association of Immunologists, Inc.
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
173
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3748-54
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:15356121-Animals,
pubmed-meshheading:15356121-Antigens, CD,
pubmed-meshheading:15356121-Antigens, Surface,
pubmed-meshheading:15356121-Binding Sites, Antibody,
pubmed-meshheading:15356121-Cell Adhesion,
pubmed-meshheading:15356121-Cell Line, Tumor,
pubmed-meshheading:15356121-Dendritic Cells,
pubmed-meshheading:15356121-Dioxygenases,
pubmed-meshheading:15356121-Enzyme Induction,
pubmed-meshheading:15356121-Female,
pubmed-meshheading:15356121-Immune Tolerance,
pubmed-meshheading:15356121-Indoleamine-Pyrrole 2,3,-Dioxygenase,
pubmed-meshheading:15356121-Interferon-alpha,
pubmed-meshheading:15356121-Membrane Glycoproteins,
pubmed-meshheading:15356121-Membrane Proteins,
pubmed-meshheading:15356121-Mice,
pubmed-meshheading:15356121-Mice, Inbred DBA,
pubmed-meshheading:15356121-Mice, Knockout,
pubmed-meshheading:15356121-Oxygenases,
pubmed-meshheading:15356121-Receptor, Interferon alpha-beta,
pubmed-meshheading:15356121-Receptors, Cell Surface,
pubmed-meshheading:15356121-Receptors, Interferon,
pubmed-meshheading:15356121-Recombinant Fusion Proteins,
pubmed-meshheading:15356121-Signal Transduction,
pubmed-meshheading:15356121-Transfection,
pubmed-meshheading:15356121-Tryptophan
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pubmed:year |
2004
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pubmed:articleTitle |
Murine plasmacytoid dendritic cells initiate the immunosuppressive pathway of tryptophan catabolism in response to CD200 receptor engagement.
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pubmed:affiliation |
Department of Experimental Medicine, University of Perugia, Perugia, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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