Cytochrome P450 2E1 and its roles in disease.


Journal

Chemico-biological interactions
ISSN: 1872-7786
Titre abrégé: Chem Biol Interact
Pays: Ireland
ID NLM: 0227276

Informations de publication

Date de publication:
01 May 2020
Historique:
received: 01 07 2019
revised: 12 12 2019
accepted: 10 03 2020
pubmed: 22 3 2020
medline: 14 4 2020
entrez: 22 3 2020
Statut: ppublish

Résumé

Cytochrome P450 (P450) 2E1 is the major P450 enzyme involved in ethanol metabolism. That role is shared with two other enzymes that oxidize ethanol, alcohol dehydrogenase and catalase. P450 2E1 is also involved in the bioactivation of a number of low molecular weight cancer suspects, as validated in vivo in mouse models where cancers could be attenuated by deletion of Cyp2e1. P450 2E1 does not have a role in global production of reactive oxygen species but localized roles are possible, e.g. in mitochondria. The structures, conformations, and catalytic mechanisms of P450 2E1 have some unusual features among P450s. The concentration of hepatic P450 varies ≥10-fold among humans, possibly in part due to single nucleotide variants. The level of P450 2E1 may have relevance in the rates of oxidation of drugs, particularly acetaminophen and anesthetics.

Identifiants

pubmed: 32198084
pii: S0009-2797(19)31126-3
doi: 10.1016/j.cbi.2020.109056
pmc: PMC7217708
mid: NIHMS1578610
pii:
doi:

Substances chimiques

Carcinogens 0
Reactive Oxygen Species 0
Acetaminophen 362O9ITL9D
Ethanol 3K9958V90M
Cytochrome P-450 CYP2E1 EC 1.14.13.-

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

109056

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM118122
Pays : United States
Organisme : NIAAA NIH HHS
ID : R13 AA027725
Pays : United States

Informations de copyright

Copyright © 2020 Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

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Auteurs

F Peter Guengerich (FP)

Department of Biochemistry, Vanderbilt University School of Medicine, 638 Robinson Research Building, 2200 Pierce Avenue, Nashville, TN, 37232-0146, USA. Electronic address: f.guengerich@vanderbilt.edu.

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Classifications MeSH