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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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Shim, H. J., Kim, Y. C., Kim, E. J., et al. (2004) · Biopharmaceutics & Drug Disposition · doi:10.1002/bdd.389 · Cited by 3
Cytochrome P450 in the Central Nervous System
Warner, M. N., & Gustafsson, J.-Α. (1999) · Humana Press eBooks · doi:10.1007/978-1-59259-693-5_3 · Cited by 3
Chronic Alcohol Intake is a Possible Risk Factor for Kidney Injury
Pati, P. (2024) · Open Access Journal of Urology & Nephrology · doi:10.23880/oajun-16000260 · Cited by 2
He, L., Kwon, D., Trnka, M. J., Liu, Y., Yang, J., Li, K. H., Totah, R. A., Johnson, E. F., Burlingame, A. L., & Correia, M. A. (2025) · Molecular Pharmacology · doi:10.1016/j.molpha.2025.100061 · Cited by 2
Yim, S.-K., Ahn, T., Jung, H.-C., et al. (2005) · Archives of Pharmacal Research · doi:10.1007/bf02977672 · Cited by 2
Daiker, D. H., Ward, J. B., Schoenfeld, H. A., et al. (1999) · International Journal of Toxicology · doi:10.1080/109158199225242 · Cited by 2
“Cyp2e1 is expressed in numerous tissues with highest constitutive expression in the liver and lower levels in the kidney, lung, brain, nasal mucosa, intestine, and peripheral lymphocytes (Porter, Khani, and Coon 1989; Roberts et al. 1994; Raucy, Gerald, and Carpenter 1995; Soh et al. 1996).”
BackgroundMathematical Model of Ethanol Metabolism in Liver
Pande, P. M. (2007) · OhioLink ETD Center (Ohio Library and Information Network) · Cited by 1
Wu, D., & Cederbaum, A. I. (2001) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)09248-4 · Cited by 1
Orellana, M., Rodrigo, R., Thielemann, L. E., et al. (1998) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/s0305-0491(98)10134-7
Role of phosphodiesterase-4 in alcohol-induced organ injury.
Avila, D. V. (2016) · ThinkIR: The University of Louisville's Institutional Repository (University of Louisville) · doi:10.18297/etd/2405
“alcohol prevents CYP2E1 proteolytic degradation by binding to CYP2E1 and inducing conformational changes [108, 109].”
BackgroundDíaz, M. L., Casañas‐Sánchez, V., Quinto‐Alemany, D., & Pérez, J. A. P. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813125-1.00048-9
Rahman, M. A. (2019) · doi:10.21007/etd.cghs.2019.0474
“The mechanism of CYP2E1 induction appears to be predominantly via a post-translational protein stabilization pathway [37, 38].”
Background(2000) · Time to knit · doi:10.1016/s1155-1941(19)30234-3
R., P., & Thakur, S. (2025) · International Journal of Science and Research (IJSR) · doi:10.21275/sr25614110820
Opposing Roles of CYP2E1 and ALDH2 in Binge Alcohol-Mediated Cerebellar Damage
Ruiter-Lopez, L., Rungratanawanich, W., & Song, B. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27156825
“…neurons and Purkinje cells) expresses the classical ethanol metabolizing enzymes catalase and cytochrome P450-2E1 (CYP2E1), which is inducible by alcohol exposure [10,11], and is sensitive to oxidative stress-mediated damage, as shown by its selective degeneration from chronic alcohol intake [12].”
Self-citation
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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