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Tytuł:
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Aryl hydrocarbon receptor activation and CYP1A induction by cooked food-derived carcinogenic heterocyclic amines in human HepG2 cell lines.
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Autorzy:
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Sekimoto M; Laboratory of Environmental Hygiene, Department of Environmental Science, School of Life and Environmental Science, Azabu University, 1-17-71 Fuchinobe, Chuo-ku, Sagamihara 252-5201, Japan; Department of Molecular Toxicology, School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Suruga-ku, Shizuoka 422-8526, Japan. Electronic address: .
Sumi H; Department of Molecular Toxicology, School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Suruga-ku, Shizuoka 422-8526, Japan.
Hosaka T; Department of Molecular Toxicology, School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Suruga-ku, Shizuoka 422-8526, Japan.
Umemura T; Division of Pathology, National Institute of Health Sciences, 1-18-1 Kamiyoga, Setagaya-ku, Tokyo 158-8501, Japan.
Nishikawa A; Biological Safety Research Center, National Institute of Health Sciences, 1-18-1, Tokyo 158-8501, Japan.
Degawa M; Department of Molecular Toxicology, School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Suruga-ku, Shizuoka 422-8526, Japan.
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Źródło:
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Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association [Food Chem Toxicol] 2016 Nov; Vol. 97, pp. 256-264. Date of Electronic Publication: 2016 Sep 16.
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Typ publikacji:
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Journal Article
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Język:
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English
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Imprint Name(s):
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Publication: Exeter : Elsevier Science Ltd
Original Publication: Oxford ; New York : Pergamon Press, c1982-
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MeSH Terms:
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Cooking*
Amines/*adverse effects
Basic Helix-Loop-Helix Transcription Factors/*metabolism
Carcinogens/*toxicity
Cytochrome P-450 CYP1A1/*metabolism
Heterocyclic Compounds/*adverse effects
Meat/*adverse effects
Receptors, Aryl Hydrocarbon/*metabolism
Basic Helix-Loop-Helix Transcription Factors/antagonists & inhibitors ; Basic Helix-Loop-Helix Transcription Factors/genetics ; Blotting, Western ; Cell Proliferation/drug effects ; Cytochrome P-450 CYP1A1/genetics ; Hep G2 Cells ; Humans ; RNA, Messenger/genetics ; RNA, Small Interfering/genetics ; Real-Time Polymerase Chain Reaction ; Receptors, Aryl Hydrocarbon/antagonists & inhibitors ; Receptors, Aryl Hydrocarbon/genetics ; Reverse Transcriptase Polymerase Chain Reaction
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Contributed Indexing:
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Keywords: Aryl hydrocarbon receptor; Carcinogenic heterocyclic amine; Cytochrome P4501A (CYP1A); HepG2 cells; Reporter gene assay
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Substance Nomenclature:
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0 (AHR protein, human)
0 (Amines)
0 (Basic Helix-Loop-Helix Transcription Factors)
0 (Carcinogens)
0 (Heterocyclic Compounds)
0 (RNA, Messenger)
0 (RNA, Small Interfering)
0 (Receptors, Aryl Hydrocarbon)
EC 1.14.14.1 (CYP1A1 protein, human)
EC 1.14.14.1 (Cytochrome P-450 CYP1A1)
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Entry Date(s):
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Date Created: 20160921 Date Completed: 20170309 Latest Revision: 20170309
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Update Code:
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20240104
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DOI:
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10.1016/j.fct.2016.09.021
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PMID:
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27644595
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The ability of nine cooked food-derived heterocyclic aromatic amines (HCAs), such as 3-amino-1,4-dimethyl-5H-pyrido[4,3-b]indole (Trp-P-1), 3-amino-1-methyl-5H-pyrido[4,3-b]indole (Trp-P-2), 2-amino-6-methylpyrido[12-a:3',2'-d]imidazole (Glu-P-1), 2-amino-pyrido[12-a:3',2'-d]imidazole hydrochloride (Glu-P-2), 2-amino-9H-pyrido[2,3-b]indole (AαC), 2-amino-3-methyl-9H-pyrido[2,3-b]indole (MeAαC), 2-amino-3-methylimidazo[4,5-f]quinolone (IQ), 2-amino-3,8-dimethylimidazo[4,5-f]quinoxaline (MeIQx) and 2-amino-1-methyl-6-phenyl-1H-imidazo[4,5-b]pyridine (PhIP), to activate human aryl hydrocarbon receptor (hAhR) was examined using a HepG2-A10 cell line, which has previously established from human hepatocarcinoma-derived HepG2 cells for use in hAhR-based luciferase reporter gene assays. Trp-P-1, Trp-P-2, AαC, MeAαC, IQ and MeIQx showed a definite ability to induce not only luciferase (hAhR activation) in HepG2-A10 cells but also cytochrome P450 (CYP)1A1/1A2 mRNAs in HepG2 cells, while such the ability of Glu-P-1, Glu-P-2, and PhIP was very low. In addition, all the HCAs examined, especially MeAαC and MeIQx, had a definite capacity for inhibiting the activity of ethoxyresorfin O-deethylase (CYP1As, especially CYP1A1). The present findings demonstrate that all the HCAs examined have the ability to activate hAhR and its target genes, and further confirm that these HCAs become good substrates for human CYP1A subfamily enzyme(s).
(Copyright © 2016 Elsevier Ltd. All rights reserved.)
