Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.1.1.1 (alcohol dehydrogenase)
 9,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Locally applied retinol is metabolized to retinoic acid in mouse epidermis in vivo. To characterize the oxidation system we investigated the ability of soluble extracts of hairless-mouse epidermis to convert retinol and retinal into retinoic acid. The extracts oxidized retinol to retinoic acid in two steps catalysed by two NAD+-dependent enzymes that were resolved on h.p.l.c. The first enzyme catalyses the reversible oxidation of retinol to retinal and is an alcohol dehydrogenase isoenzyme. The second enzyme oxidizes retinal to retinoic acid. Retinol oxidation by epidermal extracts was inhibited by the alcohol dehydrogenase inhibitor 4-methylpyrazole and by the polyene citral. The toxicity and relatively low potency at inhibiting the epidermal alcohol dehydrogenase isoenzyme curtailed the use of 4-methylpyrazole in vivo. However, citral significantly inhibited retinoic acid formation from retinol in the epidermis in vivo. The ability to inhibit the oxidation of retinol to retinoic acid in mouse epidermis provides a potential method to resolve the roles of retinol and retinoic acid in epithelial function.
 ...
PMID:Terminal-group oxidation of retinol by mouse epidermis. Inhibition in vitro and in vivo. 366 36

Retinyl palmitate, a widely used ingredient in cosmetic products, is promoted for its beneficial effects on the appearance of skin. Previous studies suggest that enzymes are available in skin to metabolize this ingredient during skin absorption. Esterase activity hydrolyzes retinyl palmitate to retinol (vitamin A), which is oxidized in many tissues to retinoic acid primarily by alcohol dehydrogenase. The activities of esterase and alcohol dehydrogenase were characterized in hairless guinea pig skin by using flow-through diffusion cells and radiolabeled model compounds (methyl salicylate and benzyl alcohol) previously shown to be metabolized by these enzymes. Methyl salicylate was hydrolyzed by esterase to a greater extent in viable skin than in nonviable skin. Glycine conjugation of salicylic acid and benzoic acid occurred only in viable skin. The metabolism of methyl salicylate and benzyl alcohol occurred to a greater extent in male guinea pig skin than in female guinea pig skin. The percutaneous absorption of both radiolabeled compounds was similar in viable and nonviable skin. About 30 and 18% of topically applied retinyl palmitate were absorbed from an acetone vehicle by hairless guinea pig skin and human skin, respectively. Less than 1% of the applied dose of this lipophilic compound diffused from skin into the receptor fluid. Retinol was the only detectable metabolite of retinyl palmitate in both hairless guinea pig and human skin. In human skin, 44% of the absorbed retinyl palmitate was hydrolyzed to retinol. The use of retinyl palmitate in cosmetic formulations may result in significant delivery of retinol into the skin.
 ...
PMID:Characterization of esterase and alcohol dehydrogenase activity in skin. Metabolism of retinyl palmitate to retinol (vitamin A) during percutaneous absorption. 797 17

Sulfur mustard (HD), a vesicating chemical warfare compound, has been shown to deplete the nicotinamide adenine dinucleotide (NAD+) content in several cell systems and tissues. This NAD+ depletion has been proposed as an indicator of HD exposure and can be used to evaluate potential antivesicant compounds. To examine NAD+ levels, an automated method based on the alcohol dehydrogenase cycling assay of Jacobson and Jacobson and utilizing a Cobas FARA clinical analyzer has been developed. Automation of this assay led to smaller sample volumes and more efficient use of personnel and resources. The usefulness of this automated method was tested by evaluating the protection, if any, by the topical application of vitamin D or betamethasone against HD-induced NAD+ depletion in skin punches from the hairless guinea pig. The results showed that the samples exposed to HD exhibited significant decreases in NAD+ levels when compared with controls. However, neither vitamin D nor betamethasone demonstrated protection against HD-induced NAD+ depletion. In fact, betamethasone exacerbated the NAD+ depletion when compared with the HD exposed group. This assay appears to be useful for testing potential antivesicant compounds using both in vivo and in vitro exposure systems.
 ...
PMID:Automated assay for nicotinamide adenine dinucleotide (NAD+). 1142 35