Abstract
The oxidation of retinaldehyde to retinoic acid (RA) provides the retinoid form of highest potency for a variety of cellular systems. RA has been implicated in many processes, such as growth and differentiation of epithelia in the adult organism (De Luca 1991), and determination of the antero-posterior axis for the limb bud (Eichele and Thaller 1987; Tickle et al. 1982) and the entire body of the vertebrate embryo (Durston et al. 1989; Hogan, Thaller, and Eichele 1992). In addition, RA is thought to promote neuronal survival, differentiation and neurite outgrowth (Haskell et al. 1987; Quinn and De Boni 1991; Wuarin, Sidell, and De Vellis 1990). RA exerts its effects by binding to specific nuclear receptors that regulate transcription. The diversity in RA actions is commonly attributed to differences in local expression patterns of different receptors and cytoplasmic binding proteins that modify the availability of intracellular RA (Giguére 1994). In addition, however, retinoid metabolism may contribute significantly to local diversity in RA actions. Retinoid metabolism includes the processes of precursor circulation and cellular uptake mediated by binding proteins, the reversible oxidation of retinol to retinaldehyde, the irreversible oxidation of retinaldehyde to RA, and RA degradation. Here we focus on the enzymes that mediate the oxidation of retinaldehyde to RA.
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McCaffery, P., Dräger, U.C. (1995). Retinoic Acid Synthesizing Enzymes in the Embryonic and Adult Vertebrate. In: Weiner, H., Holmes, R.S., Wermuth, B. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 5. Advances in Experimental Medicine and Biology, vol 372. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1965-2_23
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DOI: https://doi.org/10.1007/978-1-4615-1965-2_23
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