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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
39
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pubmed:dateCreated |
2004-9-20
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pubmed:abstractText |
Nucling is a novel protein isolated from murine embryonal carcinoma cells with an up-regulated expression during cardiac muscle differentiation. We show here that Nucling was up-regulated by proapoptotic stimuli and important for the induction of apoptosis after cytotoxic stress. We further demonstrated that overexpressed Nucling was able to induce apoptosis. In Nucling-deficient cells, the expression levels of Apaf-1 and cytochrome c, which are the major components of an apoptosis-promoting complex named apoptosome, were both down-regulated under cellular stress. A deficiency of Nucling also conferred resistance to apoptotic stress on the cell. After UV irradiation, Nucling was shown to reside in an Apaf-1/pro-caspase-9 complex, suggesting that Nucling might be a key molecule for the formation and maintenance of this complex. Nucling induced translocation of Apaf-1 to the nucleus, thereby distributing the Nucling/Apaf-1/pro-caspase-9 complex to the nuclear fraction. These findings suggest that Nucling recruits and transports the apoptosome complex during stress-induced apoptosis.
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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/APAF1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Chloromethyl Ketones,
http://linkedlifedata.com/resource/pubmed/chemical/Apaf1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Apoptotic Protease-Activating...,
http://linkedlifedata.com/resource/pubmed/chemical/CASP9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Casp9 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 9,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Proteinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochromes c,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/Uaca protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/benzyloxycarbonylvalyl-alanyl-aspart...
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:FukuiKiyoshiK,
pubmed-author:IshimuraKazunoriK,
pubmed-author:JosKK,
pubmed-author:KajiRyujiR,
pubmed-author:MakTak WTW,
pubmed-author:MatsumotoMitsuruM,
pubmed-author:MitaniTasukuT,
pubmed-author:Mukai-SakaiRikaR,
pubmed-author:SakaiTakashiT,
pubmed-author:ShimadaHidenoriH,
pubmed-author:ShishidoYujiY,
pubmed-author:TengXichuanX,
pubmed-author:ToidaKazunoriK
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pubmed:copyrightInfo |
Copyright 2004 American Society for Biochemistry and Molecular Biology, Inc.
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
41131-40
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15271982-Alleles,
pubmed-meshheading:15271982-Amino Acid Chloromethyl Ketones,
pubmed-meshheading:15271982-Animals,
pubmed-meshheading:15271982-Apoptosis,
pubmed-meshheading:15271982-Apoptotic Protease-Activating Factor 1,
pubmed-meshheading:15271982-Blotting, Northern,
pubmed-meshheading:15271982-Blotting, Western,
pubmed-meshheading:15271982-COS Cells,
pubmed-meshheading:15271982-Caspase 9,
pubmed-meshheading:15271982-Caspases,
pubmed-meshheading:15271982-Cell Death,
pubmed-meshheading:15271982-Cell Line,
pubmed-meshheading:15271982-Cysteine Proteinase Inhibitors,
pubmed-meshheading:15271982-Cytochromes c,
pubmed-meshheading:15271982-Dose-Response Relationship, Drug,
pubmed-meshheading:15271982-Down-Regulation,
pubmed-meshheading:15271982-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:15271982-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:15271982-Genetic Vectors,
pubmed-meshheading:15271982-HeLa Cells,
pubmed-meshheading:15271982-Humans,
pubmed-meshheading:15271982-Hydrogen Peroxide,
pubmed-meshheading:15271982-In Situ Nick-End Labeling,
pubmed-meshheading:15271982-Membrane Proteins,
pubmed-meshheading:15271982-Mice,
pubmed-meshheading:15271982-Mice, Transgenic,
pubmed-meshheading:15271982-Microscopy, Confocal,
pubmed-meshheading:15271982-Mitochondria,
pubmed-meshheading:15271982-Models, Genetic,
pubmed-meshheading:15271982-Plasmids,
pubmed-meshheading:15271982-Proteins,
pubmed-meshheading:15271982-RNA,
pubmed-meshheading:15271982-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:15271982-Transfection,
pubmed-meshheading:15271982-Transgenes,
pubmed-meshheading:15271982-Ultraviolet Rays,
pubmed-meshheading:15271982-Up-Regulation
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pubmed:year |
2004
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pubmed:articleTitle |
Nucling recruits Apaf-1/pro-caspase-9 complex for the induction of stress-induced apoptosis.
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pubmed:affiliation |
The Institute for Enzyme Research, The University of Tokushima, Tokushima 770-8503, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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