Metabolism of all-trans-retinoic acid in hamster liver microsomes: Oxidation of 4-hydroxy- to 4-keto-retinoic acid☆
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Biochemical and physiological importance of the CYP26 retinoic acid hydroxylases
2019, Pharmacology and TherapeuticsCitation Excerpt :However, the formation of 4-oxo-atRA likely requires an alcohol dehydrogenase enzyme in tissue and cell systems for the second oxidization step after initial 4-hydroxylation. Studies in HepG2 cells and microsomes have shown that 4-oxo-atRA formation from 4-OH-atRA, is mainly mediated by NAD+-dependent enzymes and not by CYP26A1 (Topletz et al., 2015), and early studies in hamster liver microsomes showed that 4-oxo-RA formation was mediated by an ADH enzyme (Roberts, Lamb, & Sporn, 1980). However, the identity of the enzyme(s) forming 4-oxo-RA remains to be determined.
Comparison of the function and expression of CYP26A1 and CYP26B1, the two retinoic acid hydroxylases
2012, Biochemical PharmacologyCitation Excerpt :These differences suggest that formation of oxo-compounds is more abundant in whole cells than in recombinant microsomes. It has previously been shown that a non-NADPH dependent enzyme is mainly responsible for 4-oxo-RA formation [39]. Thus the clearance of atRA and its active metabolites appears to involve other enzymes as well as CYP26 isoforms.
Expression profiles of phases 1 and 2 metabolizing enzymes in human skin and the reconstructed skin models Episkin™ and full thickness model from Episkin™
2009, Journal of Steroid Biochemistry and Molecular BiologyCytochrome P450: A target for drug development for skin diseases
2004, Journal of Investigative DermatologyCitation Excerpt :RA metabolizes via the hydroxylation of its cyclohexenyl moiety resulting in the formation of inactive 4-hydroxy-RA that further oxidized to keto-RA and other polar metabolites. It has been widely shown that these reactions are CYP dependent (Roberts et al, 1980;Williams and Napoli, 1985, 1987). Studies have shown that the in vitro hydroxylation of RA is catalyzed by the CYP (Roberts et al, 1991;Martini and Murray, 1993).
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An abstract of this work appeared in Fed. Proc.38, 761 (1978).