Cited by 241Alcohol Consumption and Health EffectsPharmacogenetics and Drug MetabolismMicrobial metabolism and enzyme function

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Enzymatic Mechanisms of Ethanol Oxidation in the Brain

Zimatkin, Sergey M., Pronko, Sergey P., Vasiliou, Vasilis, Gonzalez, Frank J., Deitrich, Richard A.·2006·Alcoholism: Clinical and Experimental Research

DOI 10.1111/j.1530-0277.2006.00181.x

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Abstract

Background: The exact enzymatic mechanisms of ethanol oxidation in the brain are still unclear. The catalase‐mediated oxidation of ethanol was demonstrated in rat brain using incubation of brain homogenates with catalase inhibitors. The role of the alcohol dehydrogenase (ADH) or cytochrome P450–dependent system in this process is possible, but has not been confirmed. The objective of the study was to determine the contribution of the different enzymatic pathways to ethanol oxidation in brain homogenates from mice and rats. Methods: Three approaches were used to investigate the enzymatic mechanisms of ethanol oxidation in the brain of rats and mice: (1) preincubation of brain homogenates with inhibitors of the ethanol‐metabolizing enzymes (catalase, CYP2E1, ADH, and ALDH); (2) utilization of mice with genetic deficiency in ethanol‐metabolizing enzymes (catalase, CYP2E1, or both enzymes); and (3) determination of ethanol oxidation in brain subcellular fractions known to have differential activity of ethanol‐metabolizing enzymes. The ethanol‐derived acetaldehyde (AC) and acetate were determined in brain samples by gas chromatography. Results: The catalase inhibitors sodium azide (5 mM) and aminotriazole (5 mM) as well as CYP2E1 inhibitors diallyl sulfide (2 mM) and β‐phenethyl isothiocyanate (0.1 mM) lowered significantly the accumulation of the ethanol‐derived AC and acetate in brain homogenates. The ADH inhibitor 4‐methyl pyrazole (5 mM) significantly decreased the acetate but not the AC accumulation. Ethanol‐derived AC accumulation in brain homogenates of acatalasemic mice was 47% of the control value, 91% in CYP2E1‐null mice, and 24% in double mutants (with deficiency of both catalase and CYP2E1). The highest levels of ethanol oxidation were found in microsomal and peroxisomal subcellular brain fractions, where CYP2E1 and catalase are located, respectively. Conclusions: Catalase is the key enzyme of ethanol oxidation in the brain of rodents: it may be responsible for about 60% of the process. CYP2E1 plays an important role in ethanol oxidation in the rodent brains. Alcohol dehydrogenase plays a minor role, if any, in this process. Aldehyde dehydrogenase plays the crucial role in the further oxidation of ethanol‐derived AC in the brain homogenates.

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Background
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Participation of Catalase in Voluntary Ethanol Consumption in Perinatally Low‐Level Lead‐Exposed Rats
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Background
Prenatal ethanol exposure increased the susceptibility of adult offspring rats to glomerulosclerosis
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“, 2007), a potent inhibitor of catalase (DeMaster et al., 1985; Gill et al., 1992; Zimatkin and Lindros, 1996; Zimatkin et al., 2006), or using D-penicillamine, a β-mercapto-α-amino acid that efficiently reacts with acetaldehyde forming inactive adducts (Cohen et al.”
Background
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Background
Induction of brain CYP2E1 changes the effects of ethanol on dopamine release in nucleus accumbens shell
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BackgroundMethodInfluential
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“In vivo and pharmacological studies have demonstrated that brain catalase significantly contributes to local acetaldehyde formation and that inhibition of catalase decreases ethanol-derived acetaldehyde levels and attenuates several behavioural effects of ethanol [18,22,24].”
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Effects of the Acute and Chronic Ethanol Intoxication on Acetate Metabolism and Kinetics in the Rat Brain
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Ethanol
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Brain Acetaldehyde Exposure Impacts upon Neonatal Respiratory Plasticity and Ethanol-Related Learning in Rodents
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Effects of Tobacco Nicotine-Derived Nitrosamine Ketone (NNK) Exposures on Brain Alcohol Metabolizing Enzyme Activities
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Açaí juice (Euterpe oleraceae) prevents ethanol-induced motor impairments in adolescent female rats
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“About 60% of this enzymatic system is mainly responsible for metabolizing ethanol into acetaldehyde in the brain (Aragon et al., 1991b; Zimatkin et al., 2006) and its peak levels of activity occurs from late gestational period to the first week after birth (Del Maestro and McDonald, 1987).”
Background
Cyp2e1 deletion in mice increases sensitivity to ethanol‐induced motor impairment and escalation of drinking behavior in the chronic intermittent ethanol model
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Authors: Zimatkin, S. M., Pronko, S. P., Vasiliou, V., Gonzalez, F. J., & Deitrich, R. A.
Affiliations: Grodno State Medical University (BY)
University of Colorado Denver (US)
National Institutes of Health (US)
Corresponding author: Zimatkin, Sergey M.
ORCID: Zimatkin, Sergey M.
Vasiliou, Vasilis
Gonzalez, Frank J.
Venue: Alcoholism: Clinical and Experimental Research
Publisher: Wiley
Published: 2006-08-14
Volume: 30
Issue: 9
Pages: 1500-1505
ISSN: 0145-6008 (ISSN-L)
1530-0277
DOI: 10.1111/j.1530-0277.2006.00181.x
OpenAlex: W1970756197
Cited by: 241
References: 25
Citations by year: 2026: 6 · 2025: 10 · 2024: 6 · 2023: 10 · 2022: 7 · 2021: 14 · 2020: 11 · 2019: 24 · 2018: 11 · 2017: 20 · 2016: 8 · 2015: 14 · 2014: 15 · 2013: 23 · 2012: 12
FWCI: 6.76
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: Alcoholism Clinical and Experimental Research (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5p50aa003527-25, 5k05aa000093-12, 5r21aa012284-02)
National Institute on Alcohol Abuse and Alcoholism (R01AA011885, K05 AA 00093, R01 AA 12650, P50 AA03527, R21-AA12284, R01AA012650)
Topics: Health Sciences › Medicine › Pathology and Forensic Medicine › Alcohol Consumption and Health Effects
Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
Keywords: ethanol oxidation, brain, catalase, CYP2E1, alcohol dehydrogenase, aldehyde dehydrogenase, acetaldehyde, acetate, enzyme inhibitors, subcellular fractions, peroxisomes, microsomes, alcohol metabolism, rodents, mice, rats, 4-methylpyrazole, 3-amino-1,2,4-triazole
MeSH terms: Acetaldehyde, Acetates, Alcohol Dehydrogenase, Ethanol, Animals, Brain, Catalase, Central Nervous System Depressants, DNA, Enzyme Inhibitors, Genetic Markers, Male, Mice, Inbred C3H, Oxidation-Reduction, Subcellular Fractions, Genetic Variation, Rats, Wistar, Mice, Knockout, Cytochrome P-450 CYP2E1, Mice, Rats, Cytochrome P-450 CYP2E1 Inhibitors

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Enzymatic Mechanisms of Ethanol Oxidation in the Brain

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