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Induction of CYP2E1 in Liver, Kidney, Brain and Intestine During Chronic Ethanol Administration and Withdrawal: Evidence That CYP2E1 Possesses a Rapid Phase Half-Life of 6 Hours or Less
Abstract
Controversy exists as to whether the induction of CYP2E1 by ethanol occurs via increased protein synthesis or protein stabilization. To address these issues in vivo, we chronically administered ethanol to rats and determined levels of immunoreactive CYP2E1 in liver, kidney, brain and upper gastro-intestinal tract (GI). Our data shows that chronic ethanol administration induces hepatic (5-6-fold over pair-fed controls) and extra-hepatic CYP2E1, an effect which is strikingly absent 12 hours after ethanol withdrawal. No changes in CYP2E1 mRNA were observed at any time, suggesting these changes are mainly post-translational at a blood ethanol concentration of 0.15% w/v. Our experimental data indicates that CYP2E1 possesses a half-life of 6 hours or less in the liver and is rapidly degraded following the removal of ethanol. This pattern of CYP2E1 turnover was also observed in other tissues, suggestive of a similar mode of regulation.
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“The formation of adduct proteins can prolong protein half-lives and accumulate as aggregated proteins.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [184]
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Summary of information on human CYP enzymes: human P450 metabolism data
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CYP2E1 and oxidative liver injury by alcohol
Lu, Y., & Cederbaum, A. I. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.11.004 · Cited by 805
Role of oxidative stress in alcohol-induced liver injury
Cederbaum, A. I., Lu, Y., & Wu, D. (2009) · Archives of Toxicology · doi:10.1007/s00204-009-0432-0 · Cited by 600
“Using an in vivo rat model of alcohol withdrawal, Roberts et al. (1994, 1995a) reported that ethanol increases CYP2E1 by protein stabilization.”
MethodAlcohol and mitochondria: a dysfunctional relationship
Hoek, J. B., Cahill, A., & Pastorino, J. G. (2002) · Gastroenterology · doi:10.1053/gast.2002.33613 · Cited by 553
Rungratanawanich, W., Qu, Y., Wang, X., Essa, M. M., & Song, B.-J. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00561-7 · Cited by 411
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Metadata
- Authors
- Roberts, B. J., Shoaf, S. E., Jeong, K. S., & Song, B. J.
- Affiliations
- National Institute on Alcohol Abuse and Alcoholism (US)
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 1994-12
- Volume
- 205
- Issue
- 2
- Pages
- 1064-1071
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W2140725636
- Cited by
- 116
- References
- 0
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 5 · 2023: 4 · 2022: 1 · 2021: 4 · 2020: 1 · 2019: 7 · 2018: 1 · 2017: 4 · 2016: 1 · 2015: 4 · 2014: 3 · 2013: 4 · 2012: 2
- FWCI
- 4.72
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Health Sciences › Medicine › Pathology and Forensic Medicine › Alcohol Consumption and Health Effects
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Drug-Induced Hepatotoxicity and Protection
- Keywords
- CYP2E1, chronic ethanol exposure, ethanol withdrawal, enzyme induction, protein stabilization, protein synthesis, protein turnover, half-life, liver, kidney, brain, intestine, blood alcohol concentration
- MeSH terms
- Acetone, Activity Cycles, Alcoholism, Animals, Brain, Cytochrome P-450 Enzyme System, Enzyme Induction, Half-Life, Intestine, Small, Kidney, Male, Microsomes, Microsomes, Liver, Oxidoreductases, N-Demethylating, RNA, Messenger, Substance Withdrawal Syndrome, Blotting, Northern, Rats, Sprague-Dawley, Cytochrome P-450 CYP2E1, Rats
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