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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1998-10-6
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pubmed:abstractText |
In this study, we elucidate the Fc epsilon RI-mediated Ag uptake and presentation mechanisms of dendritic cells (DC). We found that Fc epsilon RI-bound IgE, after polyvalent but not after monovalent ligation, is efficiently internalized into acidic, proteolytic compartments, degraded, and delivered into organelles containing MHC class II, HLA-DM, and lysosomal proteins. To follow the fate of the fragmented ligand, we sought to interfere with invariant chain (Ii) degradation, a process critical for peptide loading of nascent MHC class II molecules. We found DC to express cathepsin (Cat) S, a cysteine protease involved in Ii processing by B cells. Exposure of DC to a specific, active-site inhibitor of Cat S resulted in the loss of anti-Cat S immunoreactivity, led to the appearance of an N-terminal Ii remnant, and decreased the export of newly synthesized MHC class II to the DC surface. Furthermore, inactivation of Cat S as well as blockade of protein neosynthesis by cycloheximide strongly reduced IgE/Fc epsilon RI-mediated Ag presentation by DC. Thus, multimeric ligands of Fc epsilon RI, instead of being delivered into a recycling MHC class H pathway, are channeled efficiently into MIIC (MHC class II compartment)-like organelles of DC, in which Cat S-dependent Ii processing and peptide loading of newly synthesized MHC class II molecules occur. This IgE/Fc epsilon RI-dependent signaling pathway in DC may be a particularly effective route for immunization and a promising target for interfering with the early steps of allergen presentation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation...,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsins,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class II,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin E,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Isotypes,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, IgE,
http://linkedlifedata.com/resource/pubmed/chemical/cathepsin S,
http://linkedlifedata.com/resource/pubmed/chemical/invariant chain
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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 | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
161
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2731-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9743330-Animals,
pubmed-meshheading:9743330-Antigen Presentation,
pubmed-meshheading:9743330-Antigens, Differentiation, B-Lymphocyte,
pubmed-meshheading:9743330-Cathepsins,
pubmed-meshheading:9743330-Cell Compartmentation,
pubmed-meshheading:9743330-Cell Line,
pubmed-meshheading:9743330-Dendritic Cells,
pubmed-meshheading:9743330-Histocompatibility Antigens Class II,
pubmed-meshheading:9743330-Humans,
pubmed-meshheading:9743330-Immunoglobulin E,
pubmed-meshheading:9743330-Immunoglobulin Isotypes,
pubmed-meshheading:9743330-Ligands,
pubmed-meshheading:9743330-Lysosomes,
pubmed-meshheading:9743330-Mice,
pubmed-meshheading:9743330-Receptors, IgE
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pubmed:year |
1998
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pubmed:articleTitle |
Fc epsilon receptor I on dendritic cells delivers IgE-bound multivalent antigens into a cathepsin S-dependent pathway of MHC class II presentation.
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pubmed:affiliation |
Division of Immunology, Allergy and Infectious Diseases, University of Vienna Medical School, Austria. Dieter.Maurer@akh-wien.ac.at
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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