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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
50
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pubmed:dateCreated |
2004-12-6
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pubmed:abstractText |
Heme oxygenase-1 is an antioxidant defense enzyme that converts heme to biliverdin, iron, and carbon monoxide. Bach-1 is a bZip protein that forms heterodimers with small Maf proteins and was reported recently to down-regulate the HO-1 gene in mice. Using small interfering RNAs targeted to human Bach-1 mRNA, we investigated whether modulation of human hepatic Bach-1 expression by small interfering (si)RNA technology influences heme oxygenase-1 gene expression. We found that Bach-1 siRNAs transfected into Huh-7 cells significantly reduced Bach-1 mRNA and protein levels approximately 80%, compared with non siRNA-treated cells. In contrast, transfection with the same amounts of nonspecific control duplexes or LaminB2-duplex did not reduce Bach-1 mRNA or protein levels, confirming the specificity of Bach-1 siRNA. Expression of the heme oxygenase-1 gene in Bach-1 siRNA-transfected cells was up-regulated 7-fold, compared with cells without Bach-1 siRNA. The effect of increasing concentrations of heme to up-regulate levels of heme oxygenase-1 was more pronounced when Bach-1 siRNA was present. Taken together, these results indicated that Bach-1 has a specific and selective ability to repress expression of human hepatic heme oxygenase-1. Silencing of Bach-1 by siRNAs is a useful method for up-regulating HO-1 gene expression. Exogenous heme produces additional up-regulation, beyond that produced by Bach-1 siRNAs, suggesting that heme does not act solely through its effects on Bach-1.
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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/BACH1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Basic-Leucine Zipper Transcription...,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Fanconi Anemia Complementation...,
http://linkedlifedata.com/resource/pubmed/chemical/HMOX1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Heme,
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase (Decyclizing),
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase-1,
http://linkedlifedata.com/resource/pubmed/chemical/Hmox1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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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 |
10
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
51769-74
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15465821-Animals,
pubmed-meshheading:15465821-Base Sequence,
pubmed-meshheading:15465821-Basic-Leucine Zipper Transcription Factors,
pubmed-meshheading:15465821-Cell Line,
pubmed-meshheading:15465821-DNA,
pubmed-meshheading:15465821-Fanconi Anemia Complementation Group Proteins,
pubmed-meshheading:15465821-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:15465821-Gene Silencing,
pubmed-meshheading:15465821-Heme,
pubmed-meshheading:15465821-Heme Oxygenase (Decyclizing),
pubmed-meshheading:15465821-Heme Oxygenase-1,
pubmed-meshheading:15465821-Hepatocytes,
pubmed-meshheading:15465821-Humans,
pubmed-meshheading:15465821-Leucine Zippers,
pubmed-meshheading:15465821-Membrane Proteins,
pubmed-meshheading:15465821-Mice,
pubmed-meshheading:15465821-RNA, Messenger,
pubmed-meshheading:15465821-RNA, Small Interfering,
pubmed-meshheading:15465821-Transcription Factors,
pubmed-meshheading:15465821-Transfection
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pubmed:year |
2004
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pubmed:articleTitle |
Role of Bach-1 in regulation of heme oxygenase-1 in human liver cells: insights from studies with small interfering RNAS.
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pubmed:affiliation |
Department of Medicine and Pharmacology, the General Clinical Research Center of the University of Connecticut Health Center, Farmington, Connecticut 06030, USA. Shan@uchc.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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