Abstract
Aldehyde dehydrogenases (ALDHs; EC 1.2.1.3) oxidize various aliphatic and aromatic aldehyde substrates to the corresponding carboxylic acids (Lindahl, 1992; Yoshida, 1992). Substrates for ALDHs are diverse and include acetaldehyde (Harrington et al., 1987), biogenic amines (Mackerell et al., 1986) and other neurotransmitters (Tipton et al., 1987), retinoic acid (Lee et al., 1991), corticosteroids (Monder et al., 1982), and aldehyde products of lipid peroxidation (Lindahl and Petersen 1992). A superfamily for the mammalian ALDHs has been proposed on the basis of divergent evolution (Vasiliou et al., 1995c). Within this superfamily, at least three genes are inducible by foreign chemicals. The cytosolic ALDH1 and ALDH3 genes are inducible by phenobarbital and 2,3,7,8-tetrachlorodibenzo-p-dioxin (dioxin; TCDD), respectively (reviewed in Vasiliou et al., 1995c). The microsomal ALDH3 is inducible by TCDD and peroxisome proliferators like Clofibrate (Vasiliou et al., 1996). Among these three genes, the dioxin-inducible ALDH3 is the most thoroughly studied. The gene encoding ALDH3 has been cloned in rat (Asman et al., 1993), human (Hsu et al., 1992), and mouse (termed as Ahd4; Vasiliou et al., 1994). The mouse Ahd4 gene has been mapped to Chr 11 (Vasiliou et al., 1993b), and the human ALDH3 gene to chromosome 17 (Santisteban et al., 1985).
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Vasiliou, V., Reuter, S.F., Shiao, TY., Puga, A., Nebert, D.W. (1996). Mouse Dioxin-Inducible Ahd4 Gene. 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_6
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