In vivo drug metabolism model for human cytochrome P450 enzyme using chimeric mice with humanized liver

2007 ◽  
Vol 96 (2) ◽  
pp. 428-437 ◽  
Author(s):  
Miki Katoh ◽  
Toshiro Sawada ◽  
Yoshinori Soeno ◽  
Miki Nakajima ◽  
Chise Tateno ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Drug Metabolism ◽  
Cytochrome P450 Enzyme ◽  
Chimeric Mice ◽  
Human Cytochrome ◽  
P450 Enzyme ◽  
Metabolism Model ◽  
In Vivo Drug Metabolism ◽  
Human Cytochrome P450 Enzyme

Assessing orally bioavailable commercial silver nanoparticle product on human cytochrome P450 enzyme activity

2014 ◽  
Vol 9 (4) ◽  
pp. 474-481 ◽  
Author(s):  
Mark A. Munger ◽  
Greg Hadlock ◽  
Greg Stoddard ◽  
Matthew H. Slawson ◽  
Diana G. Wilkins ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Cytochrome P450 ◽  
Silver Nanoparticle ◽  
Cytochrome P450 Enzyme ◽  
Human Cytochrome ◽  
P450 Enzyme ◽  
Orally Bioavailable ◽  
Human Cytochrome P450 Enzyme

Metabolism and mechanism of human cytochrome P450 enzyme 1A2

2021 ◽  
Vol 21 ◽  
Author(s):  
Jingchao Guo ◽  
Xiaohui Zhu ◽  
Sara Badawy ◽  
Awais Ihsan ◽  
Zhenli Liu ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Aromatic Hydrocarbon ◽  
Personalised Medicine ◽  
Cytochrome P450 Enzyme ◽  
Cyp Enzymes ◽  
Human Cytochrome ◽  
P450 Enzyme ◽  
Metabolic Mechanism ◽  
Clinical Drugs ◽  
Human Cytochrome P450 Enzyme

Abstract: Human cytochrome P450 enzyme 1A2 (CYP1A2) is one of the most important cytochrome P450 (CYP) enzymes in the liver, accounting for 13% to 15% of hepatic CYP enzymes. CYP1A2 metabolises many clinical drugs, such as phenacetin, caffeine, clozapine, tacrine, propranolol, and mexiletine. CYP1A2 also metabolises certain precarcinogens such as aflatoxins, mycotoxins, nitrosamines, and endogenous substances such as steroids. The regulation of CYP1A2 is influenced by many factors. The transcription of CYP1A2 involves not only the aromatic hydrocarbon receptor pathway, but also many additional transcription factors, and CYP1A2 expression may be affected by transcription coactivators and compression factors. Degradation of CYP1A2 mRNA and protein, alternative splicing, RNA stability, regulatory microRNAs, and DNA methylation are also known to affect the regulation of CYP1A2. Many factors can lead to changes in the activity of CYP1A2. Smoking, polycyclic aromatic hydrocarbon ingestion, and certain drugs (e.g., omeprazole) increase its activity, while many clinical drugs such as theophylline, fluvoxamine, quinolone antibiotics, verapamil, cimetidine, and oral contraceptives can inhibit CYP1A2 activity. Here, we review the drugs metabolised by CYP1A2, the metabolic mechanism of CYP1A2, and various factors that influence CYP1A2 metabolism. The metabolic mechanism of CYP1A2 is of great significance in the development of personalised medicine and CYP1A2 target-based drugs.

Conversion of chenodeoxycholic acid to cholic acid by human CYP8B1

2019 ◽  
Vol 400 (5) ◽  
pp. 625-628 ◽  
Author(s):  
Linbing Fan ◽  
Jan Felix Joseph ◽  
Pradeepraj Durairaj ◽  
Maria Kristina Parr ◽  
Matthias Bureik
Keyword(s):  
Cytochrome P450 ◽  
Cholic Acid ◽  
Chenodeoxycholic Acid ◽  
Test System ◽  
Cytochrome P450 Enzyme ◽  
Human Cytochrome ◽  
P450 Enzyme ◽  
Derivatives Of ◽  
Human Cytochrome P450 Enzyme

Abstract The human cytochrome P450 enzyme CYP8B1 is a crucial regulator of the balance of cholic acid (CA) and chenodeoxycholic acid (CDCA) in the liver. It was previously shown to catalyze the conversion of 7α-hydroxycholest-4-en-3-one, a CDCA precursor, to 7α,12α-dihydroxycholest-4-en-3-one, which is an intermediate of CA biosynthesis. In this study we demonstrate that CYP8B1 can also convert CDCA itself to CA. We also show that five derivatives of luciferin are metabolized by CYP8B1 and established a rapid and convenient inhibitor test system. In this way we were able to identify four new CYP8B1 inhibitors, which are aminobenzotriazole, exemestane, ketoconazole and letrozole.

Interaction of pefloxacin and enoxacin with the human cytochrome P450 enzyme CYP1A2

1999 ◽  
Vol 65 (3) ◽  
pp. 262-274 ◽  
Author(s):  
M KINZIGSCHIPPERS ◽  
U FUHR ◽  
M ZAIGLER ◽  
J DAMMEYER ◽  
G RUSING ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome P450 Enzyme ◽  
Human Cytochrome ◽  
P450 Enzyme ◽  
Human Cytochrome P450 Enzyme

Human Cytochrome P450 Enzyme Specificity for the Bioactivation of Estragole and Related Alkenylbenzenes

2007 ◽  
Vol 20 (5) ◽  
pp. 798-806 ◽  
Author(s):  
Suzanne M. F. Jeurissen ◽  
Ans Punt ◽  
Marelle G. Boersma ◽  
Jan J. P. Bogaards ◽  
Yiannis C. Fiamegos ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome P450 Enzyme ◽  
Enzyme Specificity ◽  
Human Cytochrome ◽  
P450 Enzyme ◽  
Human Cytochrome P450 Enzyme

Human Cytochrome P450 Enzyme Specificity for Bioactivation of Safrole to the Proximate Carcinogen 1‘-Hydroxysafrole

2004 ◽  
Vol 17 (9) ◽  
pp. 1245-1250 ◽  
Author(s):  
Suzanne M. F. Jeurissen ◽  
Jan J. P. Bogaards ◽  
Hanem M. Awad ◽  
Marelle G. Boersma ◽  
Walter Brand ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome P450 Enzyme ◽  
Enzyme Specificity ◽  
Human Cytochrome ◽  
P450 Enzyme ◽  
Human Cytochrome P450 Enzyme
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