Journal ArticleDOI
Induction of aldehyde dehydrogenases.
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TLDR
Rat liver contains two inducible aldehyde dehydrogenases in the cytosol, and phenobarbital, 1,1,1-trichloro-2,2-bis-(p-chlorophenylethane) (DDT), and dodecachlorooctahydro-1,3,4-metheno- 2H-cyclobuto[cd]pentalene (Mirex) induce only the φ enzyme significantlyAbout:
This article is published in Biochemical Pharmacology.The article was published on 1978-01-01. It has received 70 citations till now. The article focuses on the topics: Aldehyde dehydrogenase & Enzyme.read more
Citations
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Journal ArticleDOI
Aldehyde Dehydrogenases and Their Role in Carcinogenesis
TL;DR: This work suggests that modulation of ALDH activity may an important determinant of the effectiveness of certain chemotherapeutic agents and what is currently known about the general structural and functional properties of the enzymes and the interrelationships of the various forms.
Journal ArticleDOI
ALDH1A1 and ALDH3A1 expression in lung cancers: correlation with histologic type and potential precursors.
TL;DR: Elevated expression of both enzymes may be associated with malignant transformation to AdenoCA, and cigarette smoking seems to result in increased expression of these enzymes in normal pneumocytes.
Book ChapterDOI
Mechanism of action and structure-activity relationships for the chlorinated dibenzo- p- dioxins and related compounds
Joyce A. Goldstein,Stephen Safe +1 more
Journal ArticleDOI
Identification of mouse liver aldehyde dehydrogenases that catalyze the oxidation of retinaldehyde to retinoic acid
TL;DR: Seven aldehyde dehydrogenases found in the cytosol of mouse stomach epithelium and cornea catalyzed the oxidation of retinaldehyde to retinoic acid, a metabolite of vitamin A that promotes the differentiation of epithelial and other cells.
References
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Journal ArticleDOI
The subcellular distribution and properties of aldehyde dehydrogenases in rat liver.
TL;DR: Kinetic experiments suggested the possible existence of at least two different NAD(+)-dependent aldehyde dehydrogenases in rat liver and distribution studies showed that one enzyme, designated enzyme I, was exclusively localized in the mitochondria and that another enzyme, designate enzyme II, was localized in both the mitochondia and the microsomal fraction.
Journal ArticleDOI
Tissue and subcellular distribution of mammalian aldehyde-oxidizing capacity
TL;DR: The results may be of importance in studies with such compounds as epinephrine, 5-hydroxytryptamine, choline, histamine, and ethanol, among others, since all of these substances can be converted, in vivo , to aldehydes that may undergo further oxidation.
Journal ArticleDOI
Horse liver aldehyde dehydrogenase. II. Kinetics and mechanistic implications of the dehydrogenase and esterase activity.
Rhoda I. Feldman,Henry Weiner +1 more
TL;DR: It is suggested that either the formation or the breakdown of a covalent intermediate through nucleophilic attack on the carbonyl carbon of the substrate is most probably the rate-limiting step in the dehydrogenase reaction scheme.
Journal ArticleDOI
Localization and characteristics of rat liver mitochondrial aldehyde dehydrogenases.
TL;DR: Two NAD-dependent aldehyde dehydrogenase enzymes from rat liver mitochondria have been partially purified and characterized and by utilization of the different substrate properties of these two enzymes it was possible to demonstrate a time-dependent release from digitonin-treated Liver mitochondria.
Journal ArticleDOI
Genetic Aspects of Increase in Rat Liver Aldehyde Dehydrogenase Induced by Phenobarbital
TL;DR: In the supernatant fraction of homogenized rat liver, the activity of aldehyde dehydrogenase that is dependent on nicotinamide adenine dinucleotide is increased up to tenfold after administration of phenobarbital for 3 days.