Cited by 277Pharmacogenetics and Drug MetabolismDrug-Induced Hepatotoxicity and ProtectionMetal-Catalyzed Oxygenation Mechanisms

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Induction of Rat Hepatic N-Nitrosodimethylamine Demethylase by Acetone Is Due to Protein Stabilization

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Song, B J, Veech, R L, Park, S S, Gelboin, H V, Gonzalez, F J·1989·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(18)94103-7

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Abstract

The N-nitrosodimethylamine demethylase (P450I-IE1) is induced severalfold in liver by giving rats ethanol, acetone, pyrazole, and other related small molecular weight compounds. This induction is not the result of an increase in IIE1 mRNA, but could be due to either an increase in translation rate or a decrease in protein degradation. To determine the mechanism of induction, we measured IIE1 synthesis and degradation rates in untreated and acetone-treated rats. This was accomplished by immunopurification of radiolabeled IIE1 protein using a specific monoclonal antibody subsequent to in vivo labeling of total cellular protein with either NaH14CO3 or [3H]leucine. We found that in rats fed acetone, the rate of IIE1 synthesis was not changed; however, IIE1 degradation was markedly altered. In untreated rats, IIE1 protein was degraded via a biphasic pathway consisting of both a rapid and slow component with approximate half-lives of 7 and 37 h, respectively. However, in acetone-treated rats, only a monophasic curve with a half-life of 37 h was observed. The abolition of the rapid degradation component of the IIE1 turnover cycle indicates that induction of IIE1 by acetone is primarily due to specific stabilization of IIE1 protein. Since acetone is also metabolized by IIE1, we believe that this may be a substrate-induced enzyme stabilization.

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Authors: Song, B. J., Veech, R. L., Park, S. S., Gelboin, H. V., & Gonzalez, F. J.
Affiliations: National Institutes of Health (US)
ORCID: Song, B J
Veech, R L
Park, S S
Gonzalez, F J
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1989-02
Volume: 264
Issue: 6
Pages: 3568-3572
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(18)94103-7
OpenAlex: W1577117187
Cited by: 277
References: 25
Citations by year: 2025: 2 · 2023: 2 · 2022: 1 · 2021: 3 · 2020: 2 · 2019: 3 · 2018: 4 · 2017: 4 · 2016: 2 · 2015: 4 · 2014: 6 · 2013: 5 · 2012: 9
FWCI: 19.95
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 11588 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Drug-Induced Hepatotoxicity and Protection
Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Keywords: CYP1A1, acetone, enzyme induction, protein stabilization, protein degradation, protein synthesis, enzyme turnover, hepatic cytochrome P450, rat liver
MeSH terms: Acetone, Animals, Autoradiography, Electrophoresis, Polyacrylamide Gel, Enzyme Induction, Kinetics, Leucine, Male, Microsomes, Liver, Oxidoreductases, N-Demethylating, Pyrazoles, Rats, Inbred Strains, Protein Biosynthesis, Cytochrome P-450 CYP2E1, Rats

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Induction of Rat Hepatic N-Nitrosodimethylamine Demethylase by Acetone Is Due to Protein Stabilization

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