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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2004-3-30
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pubmed:abstractText |
Cellular levels of key regulatory proteins are controlled via ubiquitination and subsequent degradation. Deubiquitinating enzymes or isopeptidases can potentially prevent targeted destruction of protein substrates through deubiquitination prior to proteasomal degradation. However, only one deubiquitinating enzyme to date has been matched to a specific substrate in mammalian cells and shown to functionally modify it. Here we show that the isopeptidase USP2a (ubiquitin-specific protease-2a) interacts with and stabilizes fatty acid synthase (FAS), which is often overexpressed in biologically aggressive human tumors. Further, USP2a is androgen-regulated and overexpressed in prostate cancer, and its functional inactivation results in decreased FAS protein and enhanced apoptosis. Thus, the isopeptidase USP2a plays a critical role in prostate cancer cell survival through FAS stabilization and represents a therapeutic target in prostate cancer.
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pubmed:grant |
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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/Androgens,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acid Synthetase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/USP2 protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1535-6108
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pubmed:author |
pubmed-author:BaronAntonellaA,
pubmed-author:GranerEdgardE,
pubmed-author:HueskenDieterD,
pubmed-author:LechpammerMirnaM,
pubmed-author:LodaMassimoM,
pubmed-author:MigitaToshiroT,
pubmed-author:RossiSabrinaS,
pubmed-author:SignorettiSabinaS,
pubmed-author:TangDanD,
pubmed-author:WeinsteinLisa JLJ,
pubmed-author:ZimmermannJohannJ
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pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
253-61
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15050917-Androgens,
pubmed-meshheading:15050917-Animals,
pubmed-meshheading:15050917-Chromatography, Affinity,
pubmed-meshheading:15050917-Cysteine Endopeptidases,
pubmed-meshheading:15050917-Endopeptidases,
pubmed-meshheading:15050917-Fatty Acid Synthetase Complex,
pubmed-meshheading:15050917-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:15050917-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:15050917-Humans,
pubmed-meshheading:15050917-Isoenzymes,
pubmed-meshheading:15050917-Male,
pubmed-meshheading:15050917-Mass Spectrometry,
pubmed-meshheading:15050917-Multienzyme Complexes,
pubmed-meshheading:15050917-Prostatic Neoplasms,
pubmed-meshheading:15050917-Proteasome Endopeptidase Complex,
pubmed-meshheading:15050917-RNA, Small Interfering,
pubmed-meshheading:15050917-Rats
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pubmed:year |
2004
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pubmed:articleTitle |
The isopeptidase USP2a regulates the stability of fatty acid synthase in prostate cancer.
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pubmed:affiliation |
Department of Medical Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02155 USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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