Mouse lung CYP1A1 catalyzes the metabolic activation of 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP)

2-Amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP) carcinogenesis is initiated by N2-hydroxylation, mediated by several cytochromes P450, including CYP1A1. However, the role of CYP1A1 in PhIP metabolic activation in vivo is unclear. In this study, Cyp1a1-null and wild-type (WT) mice were used to...

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Bibliographic Details
Published in:Carcinogenesis (New York) 2007-03, Vol.28 (3), p.732-737
Main Authors: Ma, Xiaochao, Idle, Jeffrey R., Malfatti, Michael A., Krausz, Kristopher W., Nebert, Daniel W., Chen, Chong-Sheng, Felton, James S., Waxman, David J., Gonzalez, Frank J.
Format: Article
Language:English
Subjects:
Animals
BASIC BIOLOGICAL SCIENCES
Biological and medical sciences
BIOLOGY
Carcinogenesis, carcinogens and anticarcinogens
Carcinogens - metabolism
Cytochrome P-450 CYP1A1 - deficiency
Cytochrome P-450 CYP1A1 - genetics
Cytochrome P-450 CYP1A1 - metabolism
Enzyme Activation
Female
Imidazoles - metabolism
Imidazoles - pharmacokinetics
LAWRENCE LIVERMORE NATIONAL LABORATORY
Lung - enzymology
LUNGS
Medical sciences
METABOLIC ACTIVATION
Mice
Mice, Knockout
Tissue Distribution
Tumors
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Summary:2-Amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP) carcinogenesis is initiated by N2-hydroxylation, mediated by several cytochromes P450, including CYP1A1. However, the role of CYP1A1 in PhIP metabolic activation in vivo is unclear. In this study, Cyp1a1-null and wild-type (WT) mice were used to investigate the potential role of CYP1A1 in PhIP metabolic activation in vivo. PhIP N2-hydroxylation was actively catalyzed by lung homogenates of WT mice, at a rate of 14.9 ± 5.0 pmol/min/g tissue, but
ISSN:0143-3334
1460-2180
DOI:10.1093/carcin/bgl184