Identification of mouse liver aldehyde dehydrogenases that catalyze the oxidation of retinaldehyde to retinoic acid☆
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Cited by (128)
Pharmacological inhibition of ALDH1A in mice decreases all-trans retinoic acid concentrations in a tissue specific manner
2015, Biochemical PharmacologyCitation Excerpt :Previous work has demonstrated that AOX forms atRA from at-retinal [53] and contributes to approximately 50% of the atRA formation from at-retinal in the rabbit liver cytosol [54]. In agreement with this, the AOX inhibitor hydralazine inhibited approximately 50% of the mouse liver atRA formation suggesting a much greater importance of AOX in atRA formation in mice than previously suggested [30]. For example, previously DBA/2 mice were used to determine the contribution of ALDH1A1 to liver atRA formation suggesting minimal AOX contribution [30].
Ethanol modulates the synthesis and catabolism of retinoic acid in the rat prostate
2015, Reproductive ToxicologyRetinoic acid signaling in spinal cord development
2013, International Journal of Biochemistry and Cell BiologyPhysiological insights into all-trans-retinoic acid biosynthesis
2012, Biochimica et Biophysica Acta - Molecular and Cell Biology of LipidsPerspectives on zebrafish as a model in environmental toxicology
2010, Fish PhysiologyCitation Excerpt :The zebrafish AKR1s have been cloned and sequenced in our labs (Karchner et al., unpublished data). Aldehyde dehydrogenases (ALDHs) are also termed retinaldehyde dehydrogenases, as one of the most important ALDH reactions in vertebrate development is the irreversible oxidation of retinal to retinoic acid (Lee et al. 1991). Retinoids play very important roles in vertebrate patterning, and zebrafish ALDH genes have been investigated primarily in the context of development (Dobbs-McAuliffe et al. 2004; Pittlik et al. 2008).
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Supported by USPHS Grant CA 21737. A description of parts of this investigation has appeared in abstract form (Lee et al., FASEB J4: A659, 1990).