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Toxicol Res. 2017 Apr;33(2):79-96. doi: 10.5487/TR.2017.33.2.079. Epub 2017 Apr 15.

Inhibition of Carcinogen-Activating Cytochrome P450 Enzymes by Xenobiotic Chemicals in Relation to Antimutagenicity and Anticarcinogenicity.

Toxicological research

Tsutomu Shimada

Affiliations

  1. Laboratory of Cellular and Molecular Biology, Graduate School of Life and Environmental Sciences, Veterinary Sciences, Osaka Prefecture University, Osaka, Japan.

PMID: 28443179 PMCID: PMC5402866 DOI: 10.5487/TR.2017.33.2.079

Abstract

A variety of xenobiotic chemicals, such as polycyclic aromatic hydrocarbons (PAHs), aryl- and heterocyclic amines and tobacco related nitrosamines, are ubiquitous environmental carcinogens and are required to be activated to chemically reactive metabolites by xenobiotic-metabolizing enzymes, including cytochrome P450 (P450 or CYP), in order to initiate cell transformation. Of various human P450 enzymes determined to date, CYP1A1, 1A2, 1B1, 2A13, 2A6, 2E1, and 3A4 are reported to play critical roles in the bioactivation of these carcinogenic chemicals.

Keywords: Chemical carcinogenesis; Cytochrome P450; Enzyme inhibition; Metabolic activation; Polycyclic aromatic hydrocarbons; Tobacco-related nitrosamines

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