DISTRIBUTION OF CATALASE IN RAT BRAIN: AMINERGIC NEURONS AS POSSIBLE TARGETS FOR ETHANOL EFFECTS
Abstract
Ethanol is metabolized at a slow but measurable rate in rodent brain. Recent studies indicate that this process is mediated mainly by catalase. The spatial distribution of this enzyme in different brain structures is poorly known. To explore possible local imbalances between the production and elimination of ethanol-derived acetaldehyde, we investigated the regional and cellular distribution of catalase, histo- and immunohistochemically, using serial cryostat sections from male Wistar rats. Compared to the strong peroxisomal staining seen in liver, brain catalase staining was weak and was not immunologically detected with an anti-sheep bovine catalase antibody. Activity was observed only in microperoxisomes, mainly in perikaryons of aminergic neurons, in the known groups of adrenergic, nonadrenergic and serotonergic neurons of the brain stem. Little peroxisomal staining was seen in other types of brain structures. This result contrasted to that of aldehyde dehydrogenase, which we previously observed to be widely distributed in brain structures, but with low activity in perikaryons of aminergic (especially catecholaminergic) neurons, as compared to cholinergic neurons. Our data indicate that catalase-mediated oxidation of ethanol to acetaldehyde takes place mainly in aminergic neurons, which seem to have a limited capacity for the subsequent removal via aldehyde dehydrogenase. This suggests that locally produced acetaldehyde could mediate CNS effects of ethanol in these structures.
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Catalase may have a limited role in ethanol metabolism in certain brain regions, except for aminergic neurons, where it is present in high concentrations.
“However, catalase may have a limited role in ethanol metabolism in certain brain regions, except for aminergic neurons, where it is present in high concentrations134,148–150.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [150]
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- Authors
- ZIMATKIN, S. M., & LINDROS, K. O.
- Affiliations
- National Academy of Sciences of Belarus (BY)
- Corresponding author
- LINDROS, K. O.
- ORCID
- ZIMATKIN, S. M.
- Venue
- Alcohol and Alcoholism
- Publisher
- Oxford University Press (OUP)
- Published
- 1996-03-01
- Volume
- 31
- Issue
- 2
- Pages
- 167-174
- ISSN
- 0735-0414 (ISSN-L)
- 1464-3502
- OpenAlex
- W2033604860
- Cited by
- 93
- References
- 39
- Citations by year
- 2026: 1 · 2025: 2 · 2023: 2 · 2022: 2 · 2021: 3 · 2020: 1 · 2019: 2 · 2018: 2 · 2017: 4 · 2016: 3 · 2015: 4 · 2014: 5 · 2013: 10 · 2012: 1
- FWCI
- 1.40
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Alcohol and Alcoholism (publishedVersion)
- PubMed (publishedVersion)
- STM:n Hallinnonalan avoin julkaisuarkisto (Julkari) (submittedVersion)
- Funders
- European Science Foundation
- Topics
- Health Sciences › Medicine › Pathology and Forensic Medicine › Alcohol Consumption and Health Effects
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- catalase, alcohol metabolism, acetaldehyde, aminergic neurons, brainstem, adrenergic neurons, serotonergic neurons, catecholaminergic neurons, cholinergic neurons, aldehyde dehydrogenase, microperoxisomes, peroxisomes, ethanol neurotoxicity, regional enzyme distribution
- MeSH terms
- Acetaldehyde, Aldehyde Dehydrogenase, Animals, Brain, Brain Mapping, Brain Stem, Catalase, Cattle, Epinephrine, Liver, Male, Nerve Fibers, Norepinephrine, Serotonin, Sheep, Rats, Wistar, Rats
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