rdf:type |
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lifeskim:mentions |
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pubmed:issue |
43
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pubmed:dateCreated |
1999-11-23
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pubmed:abstractText |
Engagement of the tumor necrosis factor-alpha (TNF-alpha) receptors by the TNF-alpha ligand results in the rapid induction of TNF-alpha gene expression. The study presented here shows that autoregulation of TNF-alpha gene transcription by selective signaling through tumor necrosis factor receptor 1 (TNFR1) requires p38 mitogen-activated protein (MAP) kinase activity and the binding of the transcription factors ATF-2 and Jun to the TNF-alpha cAMP-response element (CRE) promoter element. Consistent with these findings, TNFR1 engagement results in increased p38 MAP kinase activity and p38-dependent phosphorylation of ATF-2. Furthermore, overexpression of MADD (MAP kinase-activating death domain protein), an adapter protein that binds to the death domain of TNFR1 and activates MAP kinase cascades, results in CRE-dependent induction of TNF-alpha gene expression. Thus, the TNF-alpha CRE site is the target of TNFR1 stimulation and mediates the autoregulation of TNF-alpha gene transcription.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATF2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Activating Transcription Factor 2,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Atf2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP Response...,
http://linkedlifedata.com/resource/pubmed/chemical/Death Domain Receptor Signaling...,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/MADD protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Tumor Necrosis Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Tumor Necrosis Factor...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/p38 Mitogen-Activated Protein...
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
30882-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10521481-Activating Transcription Factor 2,
pubmed-meshheading:10521481-Animals,
pubmed-meshheading:10521481-Antigens, CD,
pubmed-meshheading:10521481-Base Sequence,
pubmed-meshheading:10521481-Binding Sites,
pubmed-meshheading:10521481-Carrier Proteins,
pubmed-meshheading:10521481-Cyclic AMP Response Element-Binding Protein,
pubmed-meshheading:10521481-Death Domain Receptor Signaling Adaptor Proteins,
pubmed-meshheading:10521481-Gene Expression Regulation,
pubmed-meshheading:10521481-Genes, Reporter,
pubmed-meshheading:10521481-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:10521481-Humans,
pubmed-meshheading:10521481-L Cells (Cell Line),
pubmed-meshheading:10521481-Leucine Zippers,
pubmed-meshheading:10521481-Mice,
pubmed-meshheading:10521481-Mitogen-Activated Protein Kinases,
pubmed-meshheading:10521481-Promoter Regions, Genetic,
pubmed-meshheading:10521481-Receptors, Tumor Necrosis Factor,
pubmed-meshheading:10521481-Receptors, Tumor Necrosis Factor, Type I,
pubmed-meshheading:10521481-Recombinant Fusion Proteins,
pubmed-meshheading:10521481-Signal Transduction,
pubmed-meshheading:10521481-Transcription Factors,
pubmed-meshheading:10521481-Transfection,
pubmed-meshheading:10521481-Tumor Necrosis Factor-alpha,
pubmed-meshheading:10521481-p38 Mitogen-Activated Protein Kinases
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pubmed:year |
1999
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pubmed:articleTitle |
Engagement of tumor necrosis factor (TNF) receptor 1 leads to ATF-2- and p38 mitogen-activated protein kinase-dependent TNF-alpha gene expression.
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pubmed:affiliation |
Center for Blood Research, Harvard Medical School, Boston, Massachusetts 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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