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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2002-9-16
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pubmed:abstractText |
It has previously been demonstrated that the STAT-1 transcription factor plays a key role in apoptosis induced by the cellular regulatory factors interferon gamma and TNF-alpha. Here we demonstrate that cells lacking STAT-1 show reduced cell death/apoptosis in response to stressful stimuli such as heat or ischaemia. Expression of STAT-1 in these cells does not enhance basal cell death but restores sensitivity to stress-induced death whereas this effect is not observed upon over-expression of STAT-3. Enhanced sensitivity to stress-induced cell death requires the C-terminal activation domain of STAT-1 and the phosphorylation sites at tyrosine 701 and serine 727. Moreover, we show for the first time in any system that the isolated C-terminal domain of STAT-1 is able to enhance stress-induced cell death in the absence of the DNA binding domain or any other region of STAT-1. Hence, STAT-1 plays a key role in stress-induced cell death, potentially acting via a novel co-activator-type mechanism and represents a possible therapeutic target for strategies aimed at minimising cell death, for example, following ischaemic injury.
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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/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/STAT1 Transcription Factor,
http://linkedlifedata.com/resource/pubmed/chemical/STAT1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/STAT3 Transcription Factor,
http://linkedlifedata.com/resource/pubmed/chemical/STAT3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1350-9047
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1140-6
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12232802-Apoptosis,
pubmed-meshheading:12232802-Binding Sites,
pubmed-meshheading:12232802-DNA-Binding Proteins,
pubmed-meshheading:12232802-Eukaryotic Cells,
pubmed-meshheading:12232802-Heat-Shock Response,
pubmed-meshheading:12232802-Hot Temperature,
pubmed-meshheading:12232802-Humans,
pubmed-meshheading:12232802-Ischemia,
pubmed-meshheading:12232802-Mutation,
pubmed-meshheading:12232802-Phosphorylation,
pubmed-meshheading:12232802-Protein Structure, Tertiary,
pubmed-meshheading:12232802-STAT1 Transcription Factor,
pubmed-meshheading:12232802-STAT3 Transcription Factor,
pubmed-meshheading:12232802-Serine,
pubmed-meshheading:12232802-Signal Transduction,
pubmed-meshheading:12232802-Stress, Physiological,
pubmed-meshheading:12232802-Trans-Activators,
pubmed-meshheading:12232802-Transcription Factors,
pubmed-meshheading:12232802-Transcriptional Activation,
pubmed-meshheading:12232802-Tumor Cells, Cultured,
pubmed-meshheading:12232802-Tyrosine
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pubmed:year |
2002
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pubmed:articleTitle |
The C-terminal activation domain of the STAT-1 transcription factor is necessary and sufficient for stress-induced apoptosis.
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pubmed:affiliation |
Institute of Child Health, University College London, 30 Guilford Street, London WC1N 1EH, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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