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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
40
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pubmed:dateCreated |
2000-10-23
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pubmed:abstractText |
Results show that smooth muscle-specific promoters represent novel downstream targets of the winged helix factor hepatocyte nuclear factor-3 homologue 1 (HFH-1). HFH-1 strongly represses telokin promoter activity when overexpressed in A10 vascular smooth muscle cells. HFH-1 was also found to repress transcription of several other smooth muscle-specific promoters, including the SM22alpha promoter. HFH-1 inhibits telokin promoter activity, by binding to a forkhead consensus site located within an AT-rich region of the telokin promoter. The DNA-binding domain alone was sufficient to mediate inhibition, suggesting that binding of HFH-1 blocks the binding of other positive-acting factors. HFH-1 does not disrupt serum response factor binding to an adjacent CArG box within the telokin promoter, implying that HFH-1 must compete with other unidentified trans-activators to mediate repression. The localization of HFH-1 mRNA to the epithelial cell layer of mouse bladder and stomach implicates HFH-1 in repressing telokin expression in epithelial cells. This suggests that cell-specific expression of telokin is likely mediated by both positive-acting factors in smooth muscle cells and negative-acting factors in nonmuscle cell types. We propose a model in which the smooth muscle specificity of the telokin promoter is regulated by interactions between positive- and negative-acting members of the hepatocyte nuclear factor-3/forkhead family of transcription factors.
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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/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Forkhead Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Foxq1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin-Light-Chain Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Response Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Tagln protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/telokin,
http://linkedlifedata.com/resource/pubmed/chemical/transgelin
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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 |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
31162-70
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pubmed:dateRevised |
2011-11-10
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pubmed:meshHeading |
pubmed-meshheading:10896677-Animals,
pubmed-meshheading:10896677-Blotting, Northern,
pubmed-meshheading:10896677-Cells, Cultured,
pubmed-meshheading:10896677-DNA,
pubmed-meshheading:10896677-DNA, Complementary,
pubmed-meshheading:10896677-DNA-Binding Proteins,
pubmed-meshheading:10896677-Epithelial Cells,
pubmed-meshheading:10896677-Forkhead Transcription Factors,
pubmed-meshheading:10896677-Gene Library,
pubmed-meshheading:10896677-In Situ Hybridization,
pubmed-meshheading:10896677-Mice,
pubmed-meshheading:10896677-Microfilament Proteins,
pubmed-meshheading:10896677-Models, Biological,
pubmed-meshheading:10896677-Models, Genetic,
pubmed-meshheading:10896677-Muscle, Smooth, Vascular,
pubmed-meshheading:10896677-Muscle Proteins,
pubmed-meshheading:10896677-Myosin-Light-Chain Kinase,
pubmed-meshheading:10896677-Nuclear Proteins,
pubmed-meshheading:10896677-Peptide Fragments,
pubmed-meshheading:10896677-Peptides,
pubmed-meshheading:10896677-Plasmids,
pubmed-meshheading:10896677-Promoter Regions, Genetic,
pubmed-meshheading:10896677-Protein Binding,
pubmed-meshheading:10896677-RNA, Messenger,
pubmed-meshheading:10896677-Ribonucleases,
pubmed-meshheading:10896677-Serum Response Factor,
pubmed-meshheading:10896677-Stomach,
pubmed-meshheading:10896677-Tissue Distribution,
pubmed-meshheading:10896677-Trans-Activators,
pubmed-meshheading:10896677-Transcription, Genetic,
pubmed-meshheading:10896677-Transcription Factors,
pubmed-meshheading:10896677-Transcriptional Activation,
pubmed-meshheading:10896677-Two-Hybrid System Techniques,
pubmed-meshheading:10896677-Urinary Bladder
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pubmed:year |
2000
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pubmed:articleTitle |
Hepatocyte nuclear factor-3 homologue 1 (HFH-1) represses transcription of smooth muscle-specific genes.
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pubmed:affiliation |
Department of Physiology and Biophysics, Indiana University School of Medicine, Indianapolis, Indiana 46202-5120, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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