Increased hepatic retinal dehydrogenase activity after phenobarbital and ethanol administration.

@article{Leo1989IncreasedHR,
  title={Increased hepatic retinal dehydrogenase activity after phenobarbital and ethanol administration.},
  author={Maria Anna Leo and C. I. Kim and N Lowe and Charles S. Lieber},
  journal={Biochemical pharmacology},
  year={1989},
  volume={38 1},
  pages={
          97-103
        }
}
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35 Citations
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35 Citations

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Identification of mouse liver aldehyde dehydrogenases that catalyze the oxidation of retinaldehyde to retinoic acid.
Characteristic properties of retinal oxidase (retinoic acid synthase) from rabbit hepatocytes.
Retinol forms retinoic acid via retinal.
Purification and partial characterization of a rat kidney aldehyde dehydrogenase that oxidizes retinal to retinoic acid.
TLDR
It is suggested that aldehyde dehydrogenase found in the kidney may be a specific retinal dehydrogen enzyme, involved in vitamin A metabolism.
Identification of human liver aldehyde dehydrogenases that catalyze the oxidation of aldophosphamide and retinaldehyde.
Kinetic evidence for the involvement of a common enzyme in the microsomal reduction of retinal and androstenedione in rat liver
  • R. Martini, M. Murray
  • Biology, Medicine
    The Journal of Steroid Biochemistry and Molecular Biology
  • 1993
Purification and characterization of a novel cytosolic NADP(H)-dependent retinol oxidoreductase from rabbit liver.
Class IV alcohol/retinol dehydrogenase localization in epidermal basal layer: Potential site of retinoic acid synthesis during skin development
TLDR
Examining mouse skin for the expression of genes encoding class I ADH and class IV ADH, the only ADH isozymes in this species able to function as retinol dehydrogenases in vitro provides evidence that the basal layer of the epidermis may be the primary site of local retinoic acid synthesis needed for retinoid signaling in the skin.
Involvement of Alcohol-Metabolizing Enzymes in Retinoic Acid Synthesis and Inhibition by Ethanol
TLDR
The presently available evidence concerning the role of alcohol dehydrogenase in retinoic acid synthesis, the roles of retinooic acid in neural tube development, and therole of ethanol as an agent that can disrupt both retinoi acid synthesis and Neural tube development is described.
A hypothetical mechanism for fetal alcohol syndrome involving ethanol inhibition of retinoic acid synthesis at the alcohol dehydrogenase step.
  • G. Duester
  • Medicine
    Alcoholism, clinical and experimental research
  • 1991
TLDR
An hypothesis is presented in which many of the abnormalities observed in fetal alcohol syndrome may be caused by high levels of ethanol acting as a competitive inhibitor of ADH-catalyzed retinol oxidation in the embryo or fetus.
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References

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TLDR
The existence of a microsomal ethanol-oxidizing system, especially its capacity to increase in activity adaptively after ethanol feeding, may explain various effects of ethanol, including proliferation of hepatic smooth endoplasmic reticulum, induction of other hepaticmicrosomal drug-detoxifying enzymes, and the metabolic tolerance to ethanol which develops in alcoholics.
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The ability to inhibit the oxidation ofretinol to retinoic acid in mouse epidermis provides a potential method to resolve the roles of retinol and retinoIC acid in epithelial function.
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Genetic Aspects of Increase in Rat Liver Aldehyde Dehydrogenase Induced by Phenobarbital
In the supernatant fraction of homogenized rat liver, the activity of aldehyde dehydrogenase that is dependent on nicotinamide adenine dinucleotide (E.C. 1.2.1.3) is increased up to tenfold after…
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TLDR
An acute dose of ethanol increases serum vitamin A and decreases hepatic vitamin A, most likely because of increased release from the liver or decreased uptake by the liver of retinyl esters as part of the lipoproteins.
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