Abstract
The aldehyde dehydrogenases (ALDH, aldehyde NAD(P)+ oxidoreductase E.C. 1.2.1.3) are a superfamily of NAD(P)+-dependent enzymes which are comprised of at least three classes or families based on sequence similarity. The Class 3 aldehyde dehydrogenase gene is expressed in a tissue-specific manner in microsomal and cytosolic fractions of rodents (Dunn et al., 1988; Boesch et al., 1996), with the highest level of constitutive expression occurring in corneal epithelium, stomach, and heart. This gene is also expressed at high levels in neoplastic tissue and some cell lines. The gene product also displays induced expression in liver, lung, bladder, colon, spleen and thymus after exposure of rodents to polycyclic aromatic hydrocarbons (PAH1). Takimoto et al. (1994) have characterized the 5′-flanking region of the ALDH-3 gene and demonstrated that it contains at least three major functional regulatory domains: a strong promoter proximal to the transcription start site, an inhibitory region just upstream of the promoter, and a PAH-responsive enhancer region approx. 3.5 kb upstream of the promoter. Expression of this gene appears to be controlled by interaction of at least these three functional domains.
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Prough, R.A., Falkner, K.C., Xiao, GH., Lindahl, R.G. (1996). Regulation of Rat ALDH-3 by Hepatic Protein Kinases and Glucocorticoids. In: Weiner, H., Lindahl, R., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 6. Advances in Experimental Medicine and Biology, vol 414. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5871-2_5
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DOI: https://doi.org/10.1007/978-1-4615-5871-2_5
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