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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6029
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pubmed:dateCreated |
2011-4-29
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pubmed:abstractText |
Cytotoxic T lymphocyte antigen 4 (CTLA-4) is an essential negative regulator of T cell immune responses whose mechanism of action is the subject of debate. CTLA-4 shares two ligands (CD80 and CD86) with a stimulatory receptor, CD28. Here, we show that CTLA-4 can capture its ligands from opposing cells by a process of trans-endocytosis. After removal, these costimulatory ligands are degraded inside CTLA-4-expressing cells, resulting in impaired costimulation via CD28. Acquisition of CD86 from antigen-presenting cells is stimulated by T cell receptor engagement and observed in vitro and in vivo. These data reveal a mechanism of immune regulation in which CTLA-4 acts as an effector molecule to inhibit CD28 costimulation by the cell-extrinsic depletion of ligands, accounting for many of the known features of the CD28-CTLA-4 system.
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pubmed:grant |
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pubmed:commentsCorrections |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD28,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD80,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD86,
http://linkedlifedata.com/resource/pubmed/chemical/CTLA-4 Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/CTLA4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ctla4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Ovalbumin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1095-9203
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pubmed:author |
pubmed-author:AndersonGrahamG,
pubmed-author:AttridgeKesleyK,
pubmed-author:BakerJenniferJ,
pubmed-author:BriggsZoeZ,
pubmed-author:FutterClare ECE,
pubmed-author:HouTie ZTZ,
pubmed-author:JefferyLouisa ELE,
pubmed-author:KaurSatdipS,
pubmed-author:ManzottiClaireC,
pubmed-author:NakamuraKyokoK,
pubmed-author:QureshiOmar SOS,
pubmed-author:SansomDavid MDM,
pubmed-author:SchmidtEmily MEM,
pubmed-author:WalkerLucy S KLS,
pubmed-author:ZhengYongY
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pubmed:issnType |
Electronic
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pubmed:day |
29
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pubmed:volume |
332
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
600-3
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:21474713-Animals,
pubmed-meshheading:21474713-Antigens, CD,
pubmed-meshheading:21474713-Antigens, CD28,
pubmed-meshheading:21474713-Antigens, CD80,
pubmed-meshheading:21474713-Antigens, CD86,
pubmed-meshheading:21474713-CHO Cells,
pubmed-meshheading:21474713-CTLA-4 Antigen,
pubmed-meshheading:21474713-Cricetinae,
pubmed-meshheading:21474713-Cricetulus,
pubmed-meshheading:21474713-Dendritic Cells,
pubmed-meshheading:21474713-Endocytosis,
pubmed-meshheading:21474713-Humans,
pubmed-meshheading:21474713-Jurkat Cells,
pubmed-meshheading:21474713-Ligands,
pubmed-meshheading:21474713-Lymphocyte Activation,
pubmed-meshheading:21474713-Mice,
pubmed-meshheading:21474713-Mice, Transgenic,
pubmed-meshheading:21474713-Models, Biological,
pubmed-meshheading:21474713-Ovalbumin,
pubmed-meshheading:21474713-Receptors, Antigen, T-Cell,
pubmed-meshheading:21474713-Recombinant Fusion Proteins,
pubmed-meshheading:21474713-T-Lymphocyte Subsets,
pubmed-meshheading:21474713-T-Lymphocytes, Regulatory
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pubmed:year |
2011
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pubmed:articleTitle |
Trans-endocytosis of CD80 and CD86: a molecular basis for the cell-extrinsic function of CTLA-4.
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pubmed:affiliation |
Medical Research Council (MRC) Centre for Immune Regulation, School of Immunity and Infection, Institute of Biomedical Research, University of Birmingham Medical School, Birmingham B15 2TT, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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