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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1995-3-31
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pubmed:abstractText |
Tumor necrosis factor (TNF)-stimulated gene 6 (TSG-6) encodes a protein expressed during inflammation. We have previously shown that transcription factors of the NF-IL6 and AP-1 families cooperatively modulate activation of the TSG-6 gene by TNF or interleukin 1 (IL-1) through a promoter region that contains an NF-IL6 site (-106 to -114) and an AP-1 element (-126 to -119). In this study we report the identification of an additional NF-IL6 site (NF-IL6*) located at positions -92 to -83. Footprinting and electrophoretic mobility shift assay suggested that NF-IL6 binds with higher affinity to the newly identified NF-IL6* site than to the earlier identified promoter-distal NF-IL6 site and that the two sites cooperate in binding NF-IL6. TNF and IL-1 stimulate specific binding of nuclear proteins to the NF-IL6* site more efficiently than to the promoter-distal NF-IL6 site. Moreover, a mutation in the NF-IL6* site abolished transactivation of the TSG-6 promoter by NF-IL6 despite the presence of the intact promoter-distal NF-IL6 site. A mutation in the promoter-distal NF-IL6 site also greatly decreased activation of the TSG-6 promoter by NF-IL6. We conclude that the two NF-IL6 sites are functionally interdependent in the activation of the TSG-6 gene.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CCAAT-Enhancer-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/TNFAIP6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
270
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pubmed:geneSymbol |
TSG-6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3677-82
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:7876106-Base Sequence,
pubmed-meshheading:7876106-Binding Sites,
pubmed-meshheading:7876106-CCAAT-Enhancer-Binding Proteins,
pubmed-meshheading:7876106-Cell Adhesion Molecules,
pubmed-meshheading:7876106-Cells, Cultured,
pubmed-meshheading:7876106-DNA-Binding Proteins,
pubmed-meshheading:7876106-HeLa Cells,
pubmed-meshheading:7876106-Humans,
pubmed-meshheading:7876106-Molecular Sequence Data,
pubmed-meshheading:7876106-Mutation,
pubmed-meshheading:7876106-Nuclear Proteins,
pubmed-meshheading:7876106-Oligodeoxyribonucleotides,
pubmed-meshheading:7876106-Promoter Regions, Genetic,
pubmed-meshheading:7876106-Protein Binding,
pubmed-meshheading:7876106-Transcription Factors
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pubmed:year |
1995
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pubmed:articleTitle |
Activation of the TSG-6 gene by NF-IL6 requires two adjacent NF-IL6 binding sites.
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pubmed:affiliation |
Department of Microbiology, New York University Medical Center, New York 10016.
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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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