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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
1999-8-31
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pubmed:databankReference |
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pubmed:abstractText |
Ligand activation of the nuclear receptor PPARgamma induces adipogenesis and increases insulin sensitivity, while activation of other PPAR isoforms (-alpha and -delta) induces little or no fat cell differentiation. Expression and activation of chimeras formed between PPARgamma and PPARdelta in fibroblasts has allowed us to localize a major domain of PPARgamma responsible for adipogenesis to the N-terminal 138 amino acids, a region with AF-1 transcriptional activity. Using this region of PPARgamma as bait, we have used a yeast two-hybrid screen to clone a novel protein, termed PGC-2, containing a partial SCAN domain. PGC-2 binds to and increases the transcriptional activity of PPARgamma but does not interact with other PPARs or most other nuclear receptors. Ectopic expression of PGC-2 in preadipocytes containing endogenous PPARgamma causes a dramatic increase in fat cell differentiation at both the morphological and molecular levels. These results suggest that interactions between PGC-2, a receptor isoform-selective cofactor and PPARgamma contribute to the adipogenic action of this receptor.
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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/Azo Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Estrogen,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/oil red O
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3676-87
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pubmed:dateRevised |
2008-11-20
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pubmed:meshHeading |
pubmed-meshheading:10393183-Adipocytes,
pubmed-meshheading:10393183-Amino Acid Sequence,
pubmed-meshheading:10393183-Animals,
pubmed-meshheading:10393183-Azo Compounds,
pubmed-meshheading:10393183-Base Sequence,
pubmed-meshheading:10393183-Cell Differentiation,
pubmed-meshheading:10393183-Cell Line,
pubmed-meshheading:10393183-Cloning, Molecular,
pubmed-meshheading:10393183-Gene Expression Regulation,
pubmed-meshheading:10393183-Mice,
pubmed-meshheading:10393183-Molecular Sequence Data,
pubmed-meshheading:10393183-Protein Binding,
pubmed-meshheading:10393183-Protein Isoforms,
pubmed-meshheading:10393183-RNA, Messenger,
pubmed-meshheading:10393183-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:10393183-Receptors, Estrogen,
pubmed-meshheading:10393183-Recombinant Fusion Proteins,
pubmed-meshheading:10393183-Stem Cells,
pubmed-meshheading:10393183-Substrate Specificity,
pubmed-meshheading:10393183-Transcription, Genetic,
pubmed-meshheading:10393183-Transcription Factors,
pubmed-meshheading:10393183-Transfection,
pubmed-meshheading:10393183-Yeasts
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pubmed:year |
1999
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pubmed:articleTitle |
An adipogenic cofactor bound by the differentiation domain of PPARgamma.
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pubmed:affiliation |
Dana-Farber Cancer Institute, 44 Binney Street Boston, MA 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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