Genotoxic activation of 2-phenylbenzotriazole-type compounds by human cytochrome P4501A1 and N-acetyltransferase expressed in Salmonella typhimurium umu strains

Yoshimitsu Oda; Tetsushi Watanabe; Yoshiyasu Terao; Haruo Nukaya; Keiji Wakabayashi

doi:10.1016/j.mrgentox.2008.04.013

Genotoxic activation of 2-phenylbenzotriazole-type compounds by human cytochrome P4501A1 and N-acetyltransferase expressed in Salmonella typhimurium umu strains

Mutation Research/Genetic Toxicology and Environmental Mutagenesis ◽

10.1016/j.mrgentox.2008.04.013 ◽

2008 ◽

Vol 654 (1) ◽

pp. 52-57 ◽

Cited By ~ 9

Author(s):

Yoshimitsu Oda ◽

Tetsushi Watanabe ◽

Yoshiyasu Terao ◽

Haruo Nukaya ◽

Keiji Wakabayashi

Keyword(s):

Salmonella Typhimurium ◽

Cytochrome P4501a1 ◽

Human Cytochrome

Metabolic activation of heterocyclic amines and other procarcinogens in Salmonella typhimurium umu tester strains expressing human cytochrome P4501A1, 1A2, 1B1, 2C9, 2D6, 2E1, and 3A4 and human NADPH-P450 reductase and bacterial O-acetyltransferase

Mutation Research/Genetic Toxicology and Environmental Mutagenesis ◽

10.1016/s1383-5718(01)00154-1 ◽

2001 ◽

Vol 492 (1-2) ◽

pp. 81-90 ◽

Cited By ~ 53

Author(s):

Yoshimitsu Oda ◽

Pramod Aryal ◽

Takao Terashita ◽

Elizabeth M.J Gillam ◽

F.Peter Guengerich ◽

...

Keyword(s):

Salmonella Typhimurium ◽

Metabolic Activation ◽

Heterocyclic Amines ◽

Cytochrome P4501a1 ◽

P450 Reductase ◽

Human Cytochrome

Metabolism of 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by human cytochrome P4501A1, P4501A2 and P4501B1

Carcinogenesis ◽

10.1093/carcin/19.11.1969 ◽

1998 ◽

Vol 19 (11) ◽

pp. 1969-1973 ◽

Cited By ~ 88

Author(s):

F. Crofts

Keyword(s):

Cytochrome P4501a1 ◽

Human Cytochrome

Expression of human cytochrome P4501A1 (CYP1A1) in Saccharomyces cerevisiae inhibits cell division

Xenobiotica ◽

10.3109/00498259609167419 ◽

1996 ◽

Vol 26 (10) ◽

pp. 1013-1023

Author(s):

A. P. Beresford ◽

R. J. Taylor ◽

J.-A. Ashcroft ◽

J. Ayrton ◽

G. T. Tucker ◽

...

Keyword(s):

Saccharomyces Cerevisiae ◽

Cell Division ◽

Cytochrome P4501a1 ◽

Human Cytochrome

Differential protection by human glutathione S-transferase P1 against cytotoxicity of benzo[a]pyrene, dibenzo[a,l]pyrene, or their dihydrodiol metabolites, in bi-transgenic cell lines that co-express rat versus human cytochrome P4501A1

Chemico-Biological Interactions ◽

10.1016/j.cbi.2009.01.010 ◽

2009 ◽

Vol 179 (2-3) ◽

pp. 240-246 ◽

Cited By ~ 10

Author(s):

Sandra L. Kabler ◽

Albrecht Seidel ◽

Juergen Jacob ◽

Johannes Doehmer ◽

Charles S. Morrow ◽

...

Keyword(s):

Cell Lines ◽

Differential Protection ◽

Glutathione S Transferase ◽

Cytochrome P4501a1 ◽

Transgenic Cell ◽

Human Cytochrome

Expression of human cytochrome P4501A1 (CYP1A1) in Saccharomyces cerevisiae inhibits cell division

Xenobiotica ◽

10.3109/00498259609062802 ◽

1996 ◽

Vol 26 (1) ◽

pp. 1013-1023 ◽

Cited By ~ 1

Author(s):

A. P. Beresford ◽

R. J. Taylor ◽

J.-A. Ashcroft ◽

J. Ayrton ◽

G. T. Tucker ◽

...

Keyword(s):

Saccharomyces Cerevisiae ◽

Cell Division ◽

Cytochrome P4501a1 ◽

Human Cytochrome

Mutagenic activation of betel quid-specific N-nitrosamines catalyzed by human cytochrome P450 coexpressed with NADPH-cytochrome P450 reductase in Salmonella typhimurium YG7108

Mutation Research/Genetic Toxicology and Environmental Mutagenesis ◽

10.1016/j.mrgentox.2004.12.002 ◽

2005 ◽

Vol 581 (1-2) ◽

pp. 165-171 ◽

Cited By ~ 20

Author(s):

Masafumi Miyazaki ◽

Eika Sugawara ◽

Teruki Yoshimura ◽

Hiroshi Yamazaki ◽

Tetsuya Kamataki

Keyword(s):

Cytochrome P450 ◽

Salmonella Typhimurium ◽

Betel Quid ◽

Cytochrome P450 Reductase ◽

Nadph Cytochrome ◽

P450 Reductase ◽

Human Cytochrome ◽

Nadph Cytochrome P450 Reductase

Role of human cytochrome P450 (CYP) in the metabolic activation of N-alkylnitrosamines: application of genetically engineered Salmonella typhimurium YG7108 expressing each form of CYP together with human NADPH-cytochrome P450 reductase

Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis ◽

10.1016/s0027-5107(01)00223-8 ◽

2001 ◽

Vol 483 (1-2) ◽

pp. 35-41 ◽

Cited By ~ 40

Author(s):

Ken-ichi Fujita ◽

Tetsuya Kamataki

Keyword(s):

Cytochrome P450 ◽

Salmonella Typhimurium ◽

Metabolic Activation ◽

Genetically Engineered ◽

Cytochrome P450 Reductase ◽

Nadph Cytochrome ◽

P450 Reductase ◽

Human Cytochrome ◽

Nadph Cytochrome P450 Reductase

MECHANISMS OF ARSENITE-MEDIATED DECREASES IN BENZO[K]FLUORANTHENE-INDUCED HUMAN CYTOCHROME P4501A1 LEVELS IN HEPG2 CELLS

Drug Metabolism and Disposition ◽

10.1124/dmd.104.002212 ◽

2004 ◽

Vol 33 (3) ◽

pp. 312-320 ◽

Cited By ~ 20

Author(s):

Erin E. Bessette ◽

Michael J. Fasco ◽

Brian T. Pentecost ◽

Laurence S. Kaminsky

Keyword(s):

Hepg2 Cells ◽

Cytochrome P4501a1 ◽

Human Cytochrome

Biphasic effects of the flavonoids quercetin and naringenin on the metabolic activation of 2-amino-3,5-dimethylimidazo[4,5-f]quinoline by Salmonella typhimurium TA1538 co-expressing human cytochrome P450 1A2, NADPH-cytochrome P450 reductase, and cytochrome b5

Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis ◽

10.1016/j.mrfmmm.2003.08.002 ◽

2004 ◽

Vol 545 (1-2) ◽

pp. 37-47 ◽

Cited By ~ 21

Author(s):

I Kang

Keyword(s):

Cytochrome P450 ◽

Salmonella Typhimurium ◽

Cytochrome B5 ◽

Metabolic Activation ◽

Cytochrome P450 Reductase ◽

Cytochrome P450 1A2 ◽

Nadph Cytochrome ◽

P450 Reductase ◽

Human Cytochrome ◽

Nadph Cytochrome P450 Reductase

Regulation of Human Cytochrome P4501A1 (hCYP1A1): A Plausible Target for Chemoprevention?

BioMed Research International ◽

10.1155/2016/5341081 ◽

2016 ◽

Vol 2016 ◽

pp. 1-17 ◽

Cited By ~ 24

Author(s):

Rebeca Santes-Palacios ◽

Diego Ornelas-Ayala ◽

Noel Cabañas ◽

Ana Marroquín-Pérez ◽

Alexis Hernández-Magaña ◽

...

Keyword(s):

Cytochrome P450 ◽

Cytochrome P450 1A1 ◽

Functional Characteristics ◽

Cytochrome P4501a1 ◽

Important Protein ◽

Physiological Processes ◽

Human Cytochrome ◽

Object Of Study ◽

Expression And Activity ◽

Rule Out

Human cytochrome P450 1A1 (hCYP1A1) has been an object of study due to its role in precarcinogen metabolism; for this reason it is relevant to know more in depth the mechanisms that rule out its expression and activity, which make this enzyme a target for the development of novel chemiopreventive agents. The aim of this work is to review the origin, regulation, and structural and functional characteristics of CYP1A1 letting us understand its role in the bioactivation of precarcinogen and the consequences of its modulation in other physiological processes, as well as guide us in the study of this important protein.