Abstract
The signaling effects of the vitamin A derivative retinoic acid are mediated by the retinoic acid receptor family (Kastner et al., 1994; Mangelsdorf et al., 1994). Recent studies on mice carrying retinoic acid receptor mutations have demonstrated that retinoic acid is essential for development of several embryonic tissues including the craniofacial region, eye, heart, and other organs (Lohnes et al., 1994; Mendelsohn et al., 1994). However, little is known about the enzymatic mechanism involved in the correct spatial and temporal regulation of retinoic acid synthesis from retinol (vitamin A) during embryonic development.
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Ang, H.L., Deltour, L., Hayamizu, T.F., Zgombic-Knight, M., and Duester, G., 1996a, Retinoic acid synthesis in mouse embryos during gastrulation and craniofacial development linked to class IV alcohol dehydrogenase gene expression, J. Biol. Chem. 271: 9526–9534.
Ang, H.L., Deltour, L., Zgombic-Knight, M., Wagner, M.A., and Duester, G., 1996b, Expression patterns of class I and class IV alcohol dehydrogenase genes in developing epithelia suggest a role for ADH in local retinoic acid synthesis, Alcohol. Clin. Exp. Res. 20: in press.
Bhat, P.V., Labrecque, J., Boutin, J.M., Lacroix, A., and Yoshida, A., 1995, Cloning of a cDNA encoding rat aldehyde dehydrogenase with high activity for retinal oxidation, Gene 166: 303–306.
Boleda, M.D., Saubi, N., Farrés, J., and Parés, X., 1993, Physiological substrates for rat alcohol dehydrogenase classes: Aldehydes of lipid peroxidation, omega-hydroxyfatty acids, and retinoids, Arch. Biochem. Biophys. 307: 85–90.
Chai, X., Boerman, M.H.E.M., Zhai, Y., and Napoli, J.L., 1995, Cloning of a cDNA for liver microsomal retinol dehydrogenase. A tissue-specific, short-chain alcohol dehydrogenase, J. Biol Chem. 270: 3900–3904.
Connor, M.J. and Smit, M.H., 1987, Terminal-group oxidation of retinol by mouse epidermis: Inhibition in vitro and in vivo, Biochem. J. 244: 489–492.
Deltour, L., Ang, H.L., and Duester, G., 1996, Ethanol inhibition of retinoic acid synthesis as a potential mechanism for fetal alcohol syndrome, FASEB J. 10: in press.
Dockham, P.A., Lee, M.-O., and Sladek, N.E., 1992, Identification of human liver aldehyde dehydrogenases that catalyze the oxidation of aldophosphamide and retinaldehyde, Biochem. Pharmacol. 43: 2453–2469.
Duester, G., Ang, H.L., Deltour, L., Foglio, M.H., Hayamizu, T.F., and Zgombic-Knight, M., 1995, Class I and class IV alcohol dehydrogenase (retinol dehydrogenase) gene expression in mouse embryos, Adv. Exp. Med. Biol. 372:301–313.
Holmquist, B. and Vallee, B.L., 1991, Human liver class III alcohol and glutathione dependent formaldehyde dehydrogenase are the same enzyme, Biochem. Biophys. Res. Commun. 178: 1371–1377.
Jörnvall, H., Danielsson, O., Hjelmqvist, L., Persson, B., and Shafqat, J., 1995, The alcohol dehydrogenase system, Adv. Exp. Med. Biol. 372: 281–294.
Julià, P., Farrés, J., and Parés, X., 1986, Ocular alcohol dehydrogenase in the rat: Regional distribution and kinetics of the ADH-1 isoenzyme with retinol and retinal, Exp. Eye Res. 42: 305–314.
Kastner, P., Chambon, P., and Leid, M., 1994, Role of nuclear retinoic acid receptors in the regulation of gene expression, in “Vitamin A in Health and Disease,” R. Blomhoff, ed.,Marcel Dekker, Inc., New York, p. 189.
Kedishvili, N.Y., Bosron, W.F., Stone, C.L., Hurley, T.D., Peggs, C.F., Thomasson, H.R., Popov, K.M., Carr, L.G., Edenberg, H.J., and Li, T.-K., 1995, Expression and kinetic characterization of recombinant human stomach alcohol dehydrogenase. Active-site amino acid sequence explains substrate specificity compared with liver isozymes, J. Biol. Chem. 270: 3625–3630.
Koivusalo, M., Baumann, M., and Uotila, L., 1989, Evidence for the identity of glutathione-dependent formaldehyde dehydrogenase and class III alcohol dehydrogenase, FEBS Lett. 257: 105–109.
Lee, M.-O., Manthey, C.L., and Sladek, N.E., 1991, Identification of mouse liver aldehyde dehydrogenases that catalyze the oxidation of retinaldehyde to retinoic acid, Biochem. Pharmacol. 42: 1279–1285.
Lohnes, D., Mark, M., Mendelsohn, C., Dollé, P., Dierich, A., Gorry, P., Gansmuller, A., and Chambon, P., 1994, Function of the retinoic acid receptors (RARs) during development. (I) Craniofacial and skeletal abnormalities in RAR double mutants, Development 120: 2723–2748.
Mangelsdorf, D.J., Umesono, K., and Evans, R.M., 1994, The retinoid receptors, in “The Retinoids: Biology, Chemistry, and Medicine, 2nd Edition,” M.B. Sporn, A.B. Roberts, and D.S. Goodman, eds., Raven Press, Ltd., New York, p. 319.
Mendelsohn, C., Lohnes, D., Décimo, D., Lufkin, T., LeMeur, M., Chambon, P., and Mark, M., 1994, Function of the retinoic acid receptors (RARs) during development. (II) Multiple abnormalities at various stages of organogenesis in RAR double mutants, Development 120: 2749–2771.
Mezey, E. and Holt, P.R., 1971, The inhibitory effect of ethanol on retinol oxidation by human liver and cattle retina, Exp. Mol. Pathol. 15: 148–156.
Raner, G.M., Vaz, A.D.N., and Coon, M.J., 1996, Metabolism of all-trans, 9-cis, and 13-cis isomers of retinal by purified isozymes of microsomal cytochrome P450 and mechanism-based inhibition of retinoid oxidation by citral, Mol. Pharmacol. 49: 515–522.
Van Thiel, D.H., Gavaler, J., and Lester, R., 1974, Ethanol inhibition of vitamin A metabolism in the testes: Possible mechanism for sterility in alcoholics, Science 186: 941–942.
Wagner, M., Han, B., and Jessell, T.M., 1992, Regional differences in retinoid release from embryonic neural tissue detected by an in vitro reporter assay, Development 116: 55–66.
Yang, Z.-N., Davis, G.J., Hurley, T.D., Stone, C.L., Li, T.-K., and Bosron, W.F., 1994, Catalytic efficiency of human alcohol dehydrogenases for retinol oxidation and retinal reduction, Alcohol. Clin. Exp. Res. 18: 587–591.
Zgombic-Knight, M., Ang, H.L., Foglio, M.H., and Duester, G., 1995, Cloning of the mouse class IV alcohol dehydrogenase (retinol dehydrogenase) cDNA and tissue-specific expression patterns of the murine ADH gene family, J. Biol. Chem. 270: 10868–10877.
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Duester, G., Deltour, L., Ang, H.L. (1996). Evidence that Class IV Alcohol Dehydrogenase May Function in Embryonic Retinoic Acid Synthesis. 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_41
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DOI: https://doi.org/10.1007/978-1-4615-5871-2_41
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