Source:http://linkedlifedata.com/resource/pubmed/id/20723761
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2010-8-20
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pubmed:databankReference | |
pubmed:abstractText |
Interferon (IFN)-induced immunoproteasomes (i-proteasomes) have been associated with improved processing of major histocompatibility complex (MHC) class I antigens. Here, we show that i-proteasomes function to protect cell viability under conditions of IFN-induced oxidative stress. IFNs trigger the production of reactive oxygen species, which induce protein oxidation and the formation of nascent, oxidant-damaged proteins. We find that the ubiquitylation machinery is concomitantly upregulated in response to IFNs, functioning to target defective ribosomal products (DRiPs) for degradation by i-proteasomes. i-proteasome-deficiency in cells and in murine inflammation models results in the formation of aggresome-like induced structures and increased sensitivity to apoptosis. Efficient clearance of these aggregates by the enhanced proteolytic activity of the i-proteasome is important for the preservation of cell viability upon IFN-induced oxidative stress. Our findings suggest that rather than having a specific role in the production of class I antigens, i-proteasomes increase the peptide supply for antigen presentation as part of a more general role in the maintenance of protein homeostasis.
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1097-4172
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pubmed:author |
pubmed-author:AktasOrhanO,
pubmed-author:Bech-OtschirDawadschargalD,
pubmed-author:BialyLukasz PLP,
pubmed-author:EbsteinFrédéricF,
pubmed-author:KloetzelPeter-MPM,
pubmed-author:KrügerElkeE,
pubmed-author:KuckelkornUlrikeU,
pubmed-author:LangeNicoleN,
pubmed-author:ProzorovskiTimourT,
pubmed-author:RiegerMelanieM,
pubmed-author:SchröterFriederikeF,
pubmed-author:SeifertUlrikeU,
pubmed-author:SteffenJanosJ,
pubmed-author:VoigtAntjeA
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pubmed:copyrightInfo |
Copyright 2010 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
20
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pubmed:volume |
142
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
613-24
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pubmed:dateRevised |
2010-9-29
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pubmed:meshHeading |
pubmed-meshheading:20723761-Animals,
pubmed-meshheading:20723761-Antigen Presentation,
pubmed-meshheading:20723761-Encephalomyelitis, Autoimmune, Experimental,
pubmed-meshheading:20723761-Histocompatibility Antigens Class I,
pubmed-meshheading:20723761-Homeostasis,
pubmed-meshheading:20723761-Humans,
pubmed-meshheading:20723761-Inflammation,
pubmed-meshheading:20723761-Interferons,
pubmed-meshheading:20723761-Mice,
pubmed-meshheading:20723761-Mice, Inbred C57BL,
pubmed-meshheading:20723761-Proteasome Endopeptidase Complex,
pubmed-meshheading:20723761-Proteins,
pubmed-meshheading:20723761-Ubiquitination
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pubmed:year |
2010
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pubmed:articleTitle |
Immunoproteasomes preserve protein homeostasis upon interferon-induced oxidative stress.
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pubmed:affiliation |
Institut für Biochemie CC2, Charité - Universitätsmedizin Berlin, Oudenarder Strasse 16, D-13347 Berlin, Germany.
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pubmed:publicationType |
Journal Article
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