Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Pinaire, J. et al.

Identification of a retinoid receptor response element in the human aldehyde dehydrogenase-2 promoter.

BACKGROUND: The human aldehyde dehydrogenase-2 promoter contains sites that bind members of the nuclear receptor family, and one (designated FP330-3') is predicted to bind retinoic acid receptors. METHODS: Binding of retinoid receptors to the FP330-3' oligonucleotide duplex and point mutations thereof was assayed using electrophoretic mobility shift assays. The function of the promoter element was determined in transfection assays. RESULTS: Heterodimers of retinoic acid receptor (RAR)alpha, beta, and gamma with retinoid X receptor (RXR)alpha bound the FP330-3' site. Mutagenesis of the FP330-3' site suggested that either the upstream DR-5 or downstream DR-1 could mediate binding of RAR/RXR. FP330-3' oligonucleotide duplexes were not bound by in vitro translated RXR homodimers but weakly competed with a synthetic DR-1 oligonucleotide duplex for binding by RXR. A reporter construct carrying four copies of the FP330-3' element was induced by cotransfection of rat hepatoma cells with a construct encoding RARalpha, when the RAR-specific ligand AM580 was present. Each of the three RXR isoforms alpha, beta, and gamma stimulated the expression of reporter constructs containing the FP330-3' sites in a 9-cis retinoic acid-dependent fashion in cells in culture. This was confirmed in the case of RXRalpha using the RXR-specific ligand methoprene. CONCLUSION: The human aldehyde dehydrogenase-2 promoter contains a retinoid response element, which may contribute to regulation of the gene.[1]

References

Identification of a retinoid receptor response element in the human aldehyde dehydrogenase-2 promoter. Pinaire, J., Chou, W.Y., Morton, M., You, M., Zeng, Y., Cho, W.K., Galli, A., Everett, L., Breen, H., Dumaual, N., Smith, J.R., Crabb, D. Alcohol. Clin. Exp. Res. (2003) [Pubmed]

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