Drug–Drug Interactions Involving Intestinal and Hepatic CYP1A Enzymes
Abstract
:1. Introduction
2. Expression
3. Regulation
3.1. Transcriptional Regulation
3.2. Impact of Gender, Age, and Diseases
3.3. Genetics and Epigenetics
4. Metabolic Function, Substrates, and Inhibitors
4.1. Metabolic Features
4.2. Substrates
4.3. Inhibitors
5. Drug–Drug Interactions
5.1. Inhibition Studies
5.2. Induction Studies
5.3. Impact of Smoking and Diet
6. Summary and Conclusions
Author Contributions
Funding
Conflicts of Interest
References
- Tanaka, E. Clinically important pharmacokinetic drug-drug interactions: Role of cytochrome P450 enzymes. J. Clin. Pharm. Ther. 1998, 23, 403–416. [Google Scholar] [CrossRef] [PubMed]
- Palleria, C.; Di Paolo, A.; Giofrè, C.; Caglioti, C.; Leuzzi, G.; Siniscalchi, A.; de Sarro, G.; Gallelli, L. Pharmacokinetic drug-drug interaction and their implication in clinical management. J. Res. Med. Sci. 2013, 18, 601–610. [Google Scholar] [PubMed]
- Paine, M.F.; Shen, D.D.; Kunze, K.L.; Perkins, J.D.; Marsh, C.L.; McVicar, J.P.; Barr, D.M.; Gillies, B.S.; Thummel, K.E. First-pass metabolism of midazolam by the human intestine. Clin. Pharmacol. Ther. 1996, 60, 14–24. [Google Scholar] [CrossRef]
- Thummel, K.E.; O’Shea, D.; Paine, M.F.; Shen, D.D.; Kunze, K.L.; Perkins, J.D.; Wilkinson, G.R. Oral first-pass elimination of midazolam involves both gastrointestinal and hepatic CYP3A-mediated metabolism. Clin. Pharmacol. Ther. 1996, 59, 491–502. [Google Scholar] [CrossRef]
- Galetin, A.; Houston, J.B. Intestinal and hepatic metabolic activity of five cytochrome P450 enzymes: Impact on prediction of first-pass metabolism. J. Pharmacol. Exp. Ther. 2006, 318, 1220–1229. [Google Scholar] [CrossRef] [Green Version]
- Eichelbaum, M.; Ingelman-Sundberg, M.; Evans, W.E. Pharmacogenomics and individualized drug therapy. Annu. Rev. Med. 2006, 57, 119–137. [Google Scholar] [CrossRef]
- Evans, W.E.; Relling, M.V. Moving towards individualized medicine with pharmacogenomics. Nature 2004, 429, 464–468. [Google Scholar] [CrossRef]
- Dresser, G.K.; Spence, J.D.; Bailey, D.G. Pharmacokinetic-pharmacodynamic consequences and clinical relevance of cytochrome P450 3A4 inhibition. Clin. Pharmacokinet. 2000, 38, 41–57. [Google Scholar] [CrossRef]
- Bahar, M.A.; Setiawan, D.; Hak, E.; Wilffert, B. Pharmacogenetics of drug-drug interaction and drug-drug-gene interaction: A systematic review on CYP2C9, CYP2C19 and CYP2D6. Pharmacogenomics 2017, 18, 701–739. [Google Scholar] [CrossRef]
- Zanger, U.M.; Schwab, M. Cytochrome P450 enzymes in drug metabolism: Regulation of gene expression, enzyme activities, and impact of genetic variation. Pharmacol. Ther. 2013, 138, 103–141. [Google Scholar] [CrossRef]
- Zhou, S.-F.; Wang, B.; Yang, L.-P.; Liu, J.-P. Structure, function, regulation and polymorphism and the clinical significance of human cytochrome P450 1A2. Drug Metab. Rev. 2010, 42, 268–354. [Google Scholar] [CrossRef] [PubMed]
- Murray, G.I.; Melvin, W.T.; Greenlee, W.F.; Burke, M.D. Regulation, function, and tissue-specific expression of cytochrome P450 CYP1B1. Annu. Rev. Pharmacol. Toxicol. 2001, 41, 297–316. [Google Scholar] [CrossRef] [PubMed]
- Schweikl, H.; Taylor, J.A.; Kitareewan, S.; Linko, P.; Nagorney, D.; Goldstein, J.A. Expression of CYP1A1 and CYP1A2 genes in human liver. Pharmacogenetics 1993, 3, 239–249. [Google Scholar] [CrossRef] [PubMed]
- Stiborová, M.; Martínek, V.; Rýdlová, H.; Koblas, T.; Hodek, P. Expression of cytochrome P450 1A1 and its contribution to oxidation of a potential human carcinogen 1-phenylazo-2-naphthol (Sudan I) in human livers. Cancer Lett. 2005, 220, 145–154. [Google Scholar] [CrossRef] [PubMed]
- Nishimura, M.; Yaguti, H.; Yoshitsugu, H.; Naito, S.; Satoh, T. Tissue distribution of mRNA expression of human cytochrome P450 isoforms assessed by high-sensitivity real-time reverse transcription PCR. Yakugaku Zasshi 2003, 123, 369–375. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Paine, M.F.; Hart, H.L.; Ludington, S.S.; Haining, R.L.; Rettie, A.E.; Zeldin, D.C. The human intestinal cytochrome P450 “pie”. Drug Metab. Dispos. 2006, 34, 880–886. [Google Scholar] [CrossRef]
- Bièche, I.; Narjoz, C.; Asselah, T.; Vacher, S.; Marcellin, P.; Lidereau, R.; Beaune, P.; de Waziers, I. Reverse transcriptase-PCR quantification of mRNA levels from cytochrome (CYP)1, CYP2 and CYP3 families in 22 different human tissues. Pharmacogenet. Genom. 2007, 17, 731–742. [Google Scholar] [CrossRef]
- Lang, D.; Radtke, M.; Bairlein, M. Highly Variable Expression of CYP1A1 in Human Liver and Impact on Pharmacokinetics of Riociguat and Granisetron in Humans. Chem. Res. Toxicol. 2019, 32, 1115–1122. [Google Scholar] [CrossRef]
- Ding, X.; Kaminsky, L.S. Human extrahepatic cytochromes P450: Function in xenobiotic metabolism and tissue-selective chemical toxicity in the respiratory and gastrointestinal tracts. Annu. Rev. Pharmacol. Toxicol. 2003, 43, 149–173. [Google Scholar] [CrossRef]
- Murray, B.P.; Edwards, R.J.; Murray, S.; Singleton, A.M.; Davies, D.S.; Boobis, A.R. Human hepatic CYP1A1 and CYP1A2 content, determined with specific anti-peptide antibodies, correlates with the mutagenic activation of PhIP. Carcinogenesis 1993, 14, 585–592. [Google Scholar] [CrossRef]
- Chang, T.K.H.; Chen, J.; Pillay, V.; Ho, J.-Y.; Bandiera, S.M. Real-time polymerase chain reaction analysis of CYP1B1 gene expression in human liver. Toxicol. Sci. 2003, 71, 11–19. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Grangeon, A.; Clermont, V.; Barama, A.; Gaudette, F.; Turgeon, J.; Michaud, V. Development and validation of an absolute protein assay for the simultaneous quantification of fourteen CYP450s in human microsomes by HPLC-MS/MS-based targeted proteomics. J. Pharm. Biomed. Anal. 2019, 173, 96–107. [Google Scholar] [CrossRef] [PubMed]
- Shrivas, K.; Mindaye, S.T.; Getie-Kebtie, M.; Alterman, M.A. Mass spectrometry-based proteomic analysis of human liver cytochrome(s) P450. Toxicol. Appl. Pharmacol. 2013, 267, 125–136. [Google Scholar] [CrossRef] [PubMed]
- Drozdzik, M.; Busch, D.; Lapczuk, J.; Müller, J.; Ostrowski, M.; Kurzawski, M.; Oswald, S. Protein Abundance of Clinically Relevant Drug-Metabolizing Enzymes in the Human Liver and Intestine: A Comparative Analysis in Paired Tissue Specimens. Clin. Pharmacol. Ther. 2018, 104, 515–524. [Google Scholar] [CrossRef]
- Drahushuk, A.T.; McGarrigle, B.P.; Larsen, K.E.; Stegeman, J.J.; Olson, J.R. Detection of CYP1A1 protein in human liver and induction by TCDD in precision-cut liver slices incubated in dynamic organ culture. Carcinogenesis 1998, 19, 1361–1368. [Google Scholar] [CrossRef] [Green Version]
- Zhang, Q.Y.; Dunbar, D.; Ostrowska, A.; Zeisloft, S.; Yang, J.; Kaminsky, L.S. Characterization of human small intestinal cytochromes P-450. Drug Metab. Dispos. 1999, 27, 804–809. [Google Scholar]
- Paine, M.F.; Schmiedlin-Ren, P.; Watkins, P.B. Cytochrome P-450 1A1 expression in human small bowel: Interindividual variation and inhibition by ketoconazole. Drug Metab. Dispos. 1999, 27, 360–364. [Google Scholar]
- Ohtsuki, S.; Schaefer, O.; Kawakami, H.; Inoue, T.; Liehner, S.; Saito, A.; Ishiguro, N.; Kishimoto, W.; Ludwig-Schwellinger, E.; Ebner, T.; et al. Simultaneous absolute protein quantification of transporters, cytochromes P450, and UDP-glucuronosyltransferases as a novel approach for the characterization of individual human liver: Comparison with mRNA levels and activities. Drug Metab. Dispos. 2012, 40, 83–92. [Google Scholar] [CrossRef] [Green Version]
- Nakamura, K.; Hirayama-Kurogi, M.; Ito, S.; Kuno, T.; Yoneyama, T.; Obuchi, W.; Terasaki, T.; Ohtsuki, S. Large-scale multiplex absolute protein quantification of drug-metabolizing enzymes and transporters in human intestine, liver, and kidney microsomes by SWATH-MS: Comparison with MRM/SRM and HR-MRM/PRM. Proteomics 2016, 16, 2106–2117. [Google Scholar] [CrossRef]
- Miyauchi, E.; Tachikawa, M.; Declèves, X.; Uchida, Y.; Bouillot, J.-L.; Poitou, C.; Oppert, J.-M.; Mouly, S.; Bergmann, J.-F.; Terasaki, T.; et al. Quantitative Atlas of Cytochrome P450, UDP-Glucuronosyltransferase, and Transporter Proteins in Jejunum of Morbidly Obese Subjects. Mol. Pharm. 2016, 13, 2631–2640. [Google Scholar] [CrossRef]
- Couto, N.; Al-Majdoub, Z.M.; Achour, B.; Wright, P.C.; Rostami-Hodjegan, A.; Barber, J. Quantification of Proteins Involved in Drug Metabolism and Disposition in the Human Liver Using Label-Free Global Proteomics. Mol. Pharm. 2019, 16, 632–647. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Clermont, V.; Grangeon, A.; Barama, A.; Turgeon, J.; Lallier, M.; Malaise, J.; Michaud, V. Activity and mRNA expression levels of selected cytochromes P450 in various sections of the human small intestine. Br. J. Clin. Pharmacol. 2019, 85, 1367–1377. [Google Scholar] [CrossRef]
- Fontana, R.J.; Lown, K.S.; Paine, M.F.; Fortlage, L.; Santella, R.M.; Felton, J.S.; Knize, M.G.; Greenberg, A.; Watkins, P.B. Effects of a chargrilled meat diet on expression of CYP3A, CYP1A, and P-glycoprotein levels in healthy volunteers. Gastroenterology 1999, 117, 89–98. [Google Scholar] [CrossRef]
- Achour, B.; Barber, J.; Rostami-Hodjegan, A. Expression of hepatic drug-metabolizing cytochrome p450 enzymes and their intercorrelations: A meta-analysis. Drug Metab. Dispos. 2014, 42, 1349–1356. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Vildhede, A.; Wiśniewski, J.R.; Norén, A.; Karlgren, M.; Artursson, P. Comparative Proteomic Analysis of Human Liver Tissue and Isolated Hepatocytes with a Focus on Proteins Determining Drug Exposure. J. Proteome Res. 2015, 14, 3305–3314. [Google Scholar] [CrossRef]
- Achour, B.; Al Feteisi, H.; Lanucara, F.; Rostami-Hodjegan, A.; Barber, J. Global Proteomic Analysis of Human Liver Microsomes: Rapid Characterization and Quantification of Hepatic Drug-Metabolizing Enzymes. Drug Metab. Dispos. 2017, 45, 666–675. [Google Scholar] [CrossRef] [Green Version]
- Achour, B.; Russell, M.R.; Barber, J.; Rostami-Hodjegan, A. Simultaneous quantification of the abundance of several cytochrome P450 and uridine 5′-diphospho-glucuronosyltransferase enzymes in human liver microsomes using multiplexed targeted proteomics. Drug Metab. Dispos. 2014, 42, 500–510. [Google Scholar] [CrossRef]
- Kawakami, H.; Ohtsuki, S.; Kamiie, J.; Suzuki, T.; Abe, T.; Terasaki, T. Simultaneous absolute quantification of 11 cytochrome P450 isoforms in human liver microsomes by liquid chromatography tandem mass spectrometry with in silico target peptide selection. J. Pharm. Sci. 2011, 100, 341–352. [Google Scholar] [CrossRef]
- Shimada, T.; Yamazaki, H.; Mimura, M.; Inui, Y.; Guengerich, F.P. Interindividual variations in human liver cytochrome P-450 enzymes involved in the oxidation of drugs, carcinogens and toxic chemicals: Studies with liver microsomes of 30 Japanese and 30 Caucasians. J. Pharmacol. Exp. Ther. 1994, 270, 414–423. [Google Scholar]
- Klein, K.; Winter, S.; Turpeinen, M.; Schwab, M.; Zanger, U.M. Pathway-Targeted Pharmacogenomics of CYP1A2 in Human Liver. Front. Pharmacol. 2010, 1, 129. [Google Scholar] [CrossRef] [Green Version]
- Jiang, Z.; Dragin, N.; Jorge-Nebert, L.F.; Martin, M.V.; Guengerich, F.P.; Aklillu, E.; Ingelman-Sundberg, M.; Hammons, G.J.; Lyn-Cook, B.D.; Kadlubar, F.F.; et al. Search for an association between the human CYP1A2 genotype and CYP1A2 metabolic phenotype. Pharmacogenet. Genom. 2006, 16, 359–367. [Google Scholar] [CrossRef]
- Ueda, R.; Iketaki, H.; Nagata, K.; Kimura, S.; Gonzalez, F.J.; Kusano, K.; Yoshimura, T.; Yamazoe, Y. A common regulatory region functions bidirectionally in transcriptional activation of the human CYP1A1 and CYP1A2 genes. Mol. Pharmacol. 2006, 69, 1924–1930. [Google Scholar] [CrossRef] [Green Version]
- Jorge-Nebert, L.F.; Jiang, Z.; Chakraborty, R.; Watson, J.; Jin, L.; McGarvey, S.T.; Deka, R.; Nebert, D.W. Analysis of human CYP1A1 and CYP1A2 genes and their shared bidirectional promoter in eight world populations. Hum. Mutat. 2010, 31, 27–40. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Nebert, D.W.; Dalton, T.P.; Okey, A.B.; Gonzalez, F.J. Role of aryl hydrocarbon receptor-mediated induction of the CYP1 enzymes in environmental toxicity and cancer. J. Biol. Chem. 2004, 279, 23847–23850. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Edwards, R.J.; Price, R.J.; Watts, P.S.; Renwick, A.B.; Tredger, J.M.; Boobis, A.R.; Lake, B.G. Induction of cytochrome P450 enzymes in cultured precision-cut human liver slices. Drug Metab. Dispos. 2003, 31, 282–288. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Madan, A.; Graham, R.A.; Carroll, K.M.; Mudra, D.R.; Burton, L.A.; Krueger, L.A.; Downey, A.D.; Czerwinski, M.; Forster, J.; Ribadeneira, M.D.; et al. Effects of prototypical microsomal enzyme inducers on cytochrome P450 expression in cultured human hepatocytes. Drug Metab. Dispos. 2003, 31, 421–431. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Moscovitz, J.E.; Kalgutkar, A.S.; Nulick, K.; Johnson, N.; Lin, Z.; Goosen, T.C.; Weng, Y. Establishing Transcriptional Signatures to Differentiate PXR-, CAR-, and AhR-Mediated Regulation of Drug Metabolism and Transport Genes in Cryopreserved Human Hepatocytes. J. Pharmacol. Exp. Ther. 2018, 365, 262–271. [Google Scholar] [CrossRef]
- Roymans, D.; van Looveren, C.; Leone, A.; Parker, J.B.; McMillian, M.; Johnson, M.D.; Koganti, A.; Gilissen, R.; Silber, P.; Mannens, G.; et al. Determination of cytochrome P450 1A2 and cytochrome P450 3A4 induction in cryopreserved human hepatocytes. Biochem. Pharmacol. 2004, 67, 427–437. [Google Scholar] [CrossRef]
- Yoshinari, K.; Ueda, R.; Kusano, K.; Yoshimura, T.; Nagata, K.; Yamazoe, Y. Omeprazole transactivates human CYP1A1 and CYP1A2 expression through the common regulatory region containing multiple xenobiotic-responsive elements. Biochem. Pharmacol. 2008, 76, 139–145. [Google Scholar] [CrossRef]
- Bapiro, T.E.; Andersson, T.B.; Otter, C.; Hasler, J.A.; Masimirembwa, C.M. Cytochrome P450 1A1/2 induction by antiparasitic drugs: Dose-dependent increase in ethoxyresorufin O-deethylase activity and mRNA caused by quinine, primaquine and albendazole in HepG2 cells. Eur. J. Clin. Pharmacol. 2002, 58, 537–542. [Google Scholar] [CrossRef]
- Dolwick, K.M.; Swanson, H.I.; Bradfield, C.A. In vitro analysis of Ah receptor domains involved in ligand-activated DNA recognition. Proc. Natl. Acad. Sci. USA 1993, 90, 8566–8570. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Sugiyama, I.; Murayama, N.; Kuroki, A.; Kota, J.; Iwano, S.; Yamazaki, H.; Hirota, T. Evaluation of cytochrome P450 inductions by anti-epileptic drug oxcarbazepine, 10-hydroxyoxcarbazepine, and carbamazepine using human hepatocytes and HepaRG cells. Xenobiotica 2016, 46, 765–774. [Google Scholar] [CrossRef]
- Ghotbi, R.; Christensen, M.; Roh, H.-K.; Ingelman-Sundberg, M.; Aklillu, E.; Bertilsson, L. Comparisons of CYP1A2 genetic polymorphisms, enzyme activity and the genotype-phenotype relationship in Swedes and Koreans. Eur. J. Clin. Pharmacol. 2007, 63, 537–546. [Google Scholar] [CrossRef] [PubMed]
- Dobrinas, M.; Cornuz, J.; Oneda, B.; Kohler Serra, M.; Puhl, M.; Eap, C.B. Impact of smoking, smoking cessation, and genetic polymorphisms on CYP1A2 activity and inducibility. Clin. Pharmacol. Ther. 2011, 90, 117–125. [Google Scholar] [CrossRef] [PubMed]
- Yoshinari, K.; Yoda, N.; Toriyabe, T.; Yamazoe, Y. Constitutive androstane receptor transcriptionally activates human CYP1A1 and CYP1A2 genes through a common regulatory element in the 5′-flanking region. Biochem. Pharmacol. 2010, 79, 261–269. [Google Scholar] [CrossRef] [PubMed]
- Feidt, D.M.; Klein, K.; Hofmann, U.; Riedmaier, S.; Knobeloch, D.; Thasler, W.E.; Weiss, T.S.; Schwab, M.; Zanger, U.M. Profiling induction of cytochrome p450 enzyme activity by statins using a new liquid chromatography-tandem mass spectrometry cocktail assay in human hepatocytes. Drug Metab. Dispos. 2010, 38, 1589–1597. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Rae, J.M.; Johnson, M.D.; Lippman, M.E.; Flockhart, D.A. Rifampin is a selective, pleiotropic inducer of drug metabolism genes in human hepatocytes: Studies with cDNA and oligonucleotide expression arrays. J. Pharmacol. Exp. Ther. 2001, 299, 849–857. [Google Scholar] [PubMed]
- Backman, J.T.; Granfors, M.T.; Neuvonen, P.J. Rifampicin is only a weak inducer of CYP1A2-mediated presystemic and systemic metabolism: Studies with tizanidine and caffeine. Eur. J. Clin. Pharmacol. 2006, 62, 451–461. [Google Scholar] [CrossRef] [PubMed]
- Parkinson, A.; Mudra, D.R.; Johnson, C.; Dwyer, A.; Carroll, K.M. The effects of gender, age, ethnicity, and liver cirrhosis on cytochrome P450 enzyme activity in human liver microsomes and inducibility in cultured human hepatocytes. Toxicol. Appl. Pharmacol. 2004, 199, 193–209. [Google Scholar] [CrossRef] [PubMed]
- Relling, M.V.; Lin, J.S.; Ayers, G.D.; Evans, W.E. Racial and gender differences in N-acetyltransferase, xanthine oxidase, and CYP1A2 activities. Clin. Pharmacol. Ther. 1992, 52, 643–658. [Google Scholar] [CrossRef]
- Ou-Yang, D.S.; Huang, S.L.; Wang, W.; Xie, H.G.; Xu, Z.H.; Shu, Y.; Zhou, H.H. Phenotypic polymorphism and gender-related differences of CYP1A2 activity in a Chinese population. Br. J. Clin. Pharmacol. 2000, 49, 145–151. [Google Scholar] [CrossRef] [PubMed]
- Backman, J.T.; Schröder, M.T.; Neuvonen, P.J. Effects of gender and moderate smoking on the pharmacokinetics and effects of the CYP1A2 substrate tizanidine. Eur. J. Clin. Pharmacol. 2008, 64, 17–24. [Google Scholar] [CrossRef] [PubMed]
- Orlando, R.; Padrini, R.; Perazzi, M.; de Martin, S.; Piccoli, P.; Palatini, P. Liver dysfunction markedly decreases the inhibition of cytochrome P450 1A2-mediated theophylline metabolism by fluvoxamine. Clin. Pharmacol. Ther. 2006, 79, 489–499. [Google Scholar] [CrossRef] [PubMed]
- Zhang, Y.; Klein, K.; Sugathan, A.; Nassery, N.; Dombkowski, A.; Zanger, U.M.; Waxman, D.J. Transcriptional profiling of human liver identifies sex-biased genes associated with polygenic dyslipidemia and coronary artery disease. PLoS ONE 2011, 6, e23506. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Chen, H.; Shen, Z.-Y.; Xu, W.; Fan, T.-Y.; Li, J.; Lu, Y.-F.; Cheng, M.-L.; Liu, J. Expression of P450 and nuclear receptors in normal and end-stage Chinese livers. World J. Gastroenterol. 2014, 20, 8681–8690. [Google Scholar] [CrossRef] [PubMed]
- Nakai, K.; Tanaka, H.; Hanada, K.; Ogata, H.; Suzuki, F.; Kumada, H.; Miyajima, A.; Ishida, S.; Sunouchi, M.; Habano, W.; et al. Decreased expression of cytochromes P450 1A2, 2E1, and 3A4 and drug transporters Na+-taurocholate-cotransporting polypeptide, organic cation transporter 1, and organic anion-transporting peptide-C correlates with the progression of liver fibrosis in chronic hepatitis C patients. Drug Metab. Dispos. 2008, 36, 1786–1793. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Hanada, K.; Nakai, K.; Tanaka, H.; Suzuki, F.; Kumada, H.; Ohno, Y.; Ozawa, S.; Ogata, H. Effect of nuclear receptor downregulation on hepatic expression of cytochrome P450 and transporters in chronic hepatitis C in association with fibrosis development. Drug Metab. Pharmacokinet. 2012, 27, 301–306. [Google Scholar] [CrossRef] [Green Version]
- Prasad, B.; Bhatt, D.K.; Johnson, K.; Chapa, R.; Chu, X.; Salphati, L.; Xiao, G.; Lee, C.; Hop, C.E.C.A.; Mathias, A.; et al. Abundance of Phase 1 and 2 Drug-Metabolizing Enzymes in Alcoholic and Hepatitis C Cirrhotic Livers: A Quantitative Targeted Proteomics Study. Drug Metab. Dispos. 2018, 46, 943–952. [Google Scholar] [CrossRef]
- Fisher, C.D.; Lickteig, A.J.; Augustine, L.M.; Ranger-Moore, J.; Jackson, J.P.; Ferguson, S.S.; Cherrington, N.J. Hepatic cytochrome P450 enzyme alterations in humans with progressive stages of nonalcoholic fatty liver disease. Drug Metab. Dispos. 2009, 37, 2087–2094. [Google Scholar] [CrossRef] [Green Version]
- Parker, A.C.; Pritchard, P.; Preston, T.; Choonara, I. Induction of CYP1A2 activity by carbamazepine in children using the caffeine breath test. Br. J. Clin. Pharmacol. 1998, 45, 176–178. [Google Scholar] [CrossRef] [Green Version]
- Buchthal, J.; Grund, K.E.; Buchmann, A.; Schrenk, D.; Beaune, P.; Bock, K.W. Induction of cytochrome P4501A by smoking or omeprazole in comparison with UDP-glucuronosyltransferase in biopsies of human duodenal mucosa. Eur. J. Clin. Pharmacol. 1995, 47, 431–435. [Google Scholar] [CrossRef]
- Diaz, D.; Fabrev, I.; Daujat, M.; Aubert, B.S.; Bories, P.; Michel, H.; Maurel, P. Omeprazole is an aryl hydrocarbon-like inducer of human hepatic cytochrome P450. Gastroenterology 1990, 99, 737–747. [Google Scholar] [CrossRef]
- Halladay, J.S.; Wong, S.; Khojasteh, S.C.; Grepper, S. An ‘all-inclusive’ 96-well cytochrome P450 induction method: Measuring enzyme activity, mRNA levels, protein levels, and cytotoxicity from one well using cryopreserved human hepatocytes. J. Pharmacol. Toxicol. Methods 2012, 66, 270–275. [Google Scholar] [CrossRef] [PubMed]
- Dixit, V.; Hariparsad, N.; Li, F.; Desai, P.; Thummel, K.E.; Unadkat, J.D. Cytochrome P450 enzymes and transporters induced by anti-human immunodeficiency virus protease inhibitors in human hepatocytes: Implications for predicting clinical drug interactions. Drug Metab. Dispos. 2007, 35, 1853–1859. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Pelkonen, O.; Pasanen, M.; Kuha, H.; Gachalyi, B.; Kairaluoma, M.; Sotaniemi, E.A.; Park, S.S.; Friedman, F.K.; Gelboin, H.V. The effect of cigarette smoking on 7-ethoxyresorufin O-deethylase and other monooxygenase activities in human liver: Analyses with monoclonal antibodies. Br. J. Clin. Pharmacol. 1986, 22, 125–134. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Gunes, A.; Dahl, M.-L. Variation in CYP1A2 activity and its clinical implications: Influence of environmental factors and genetic polymorphisms. Pharmacogenomics 2008, 9, 625–637. [Google Scholar] [CrossRef] [PubMed]
- Ingelman-Sundberg, M.; Sim, S.C.; Gomez, A.; Rodriguez-Antona, C. Influence of cytochrome P450 polymorphisms on drug therapies: Pharmacogenetic, pharmacoepigenetic and clinical aspects. Pharmacol. Ther. 2007, 116, 496–526. [Google Scholar] [CrossRef] [PubMed]
- Rasmussen, B.B.; Brix, T.H.; Kyvik, K.O.; Brøsen, K. The interindividual differences in the 3-demthylation of caffeine alias CYP1A2 is determined by both genetic and environmental factors. Pharmacogenetics 2002, 12, 473–478. [Google Scholar] [CrossRef]
- Zanger, U.M.; Klein, K.; Thomas, M.; Rieger, J.K.; Tremmel, R.; Kandel, B.A.; Klein, M.; Magdy, T. Genetics, epigenetics, and regulation of drug-metabolizing cytochrome p450 enzymes. Clin. Pharmacol. Ther. 2014, 95, 258–261. [Google Scholar] [CrossRef]
- Kisselev, P.; Schunck, W.-H.; Roots, I.; Schwarz, D. Association of CYP1A1 polymorphisms with differential metabolic activation of 17beta-estradiol and estrone. Cancer Res. 2005, 65, 2972–2978. [Google Scholar] [CrossRef] [Green Version]
- Zhou, H.; Josephy, P.D.; Kim, D.; Guengerich, F.P. Functional characterization of four allelic variants of human cytochrome P450 1A2. Arch. Biochem. Biophys. 2004, 422, 23–30. [Google Scholar] [CrossRef] [PubMed]
- Palma, B.B.; Silva E Sousa, M.; Vosmeer, C.R.; Lastdrager, J.; Rueff, J.; Vermeulen, N.P.E.; Kranendonk, M. Functional characterization of eight human cytochrome P450 1A2 gene variants by recombinant protein expression. Pharm. J. 2010, 10, 478–488. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Nakajima, M.; Yokoi, T.; Mizutani, M.; Kinoshita, M.; Funayama, M.; Kamataki, T. Genetic polymorphism in the 5′-flanking region of human CYP1A2 gene: Effect on the CYP1A2 inducibility in humans. J. Biochem. 1999, 125, 803–808. [Google Scholar] [CrossRef] [PubMed]
- Sachse, C.; Brockmöller, J.; Bauer, S.; Roots, I. Functional significance of a C--A polymorphism in intron 1 of the cytochrome P450 CYP1A2 gene tested with caffeine. Br. J. Clin. Pharmacol. 1999, 47, 445–449. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Djordjevic, N.; Ghotbi, R.; Jankovic, S.; Aklillu, E. Induction of CYP1A2 by heavy coffee consumption is associated with the CYP1A2 -163CA polymorphism. Eur. J. Clin. Pharmacol. 2010, 66, 697–703. [Google Scholar] [CrossRef]
- Han, X.-M.; Ouyang, D.-S.; Chen, X.-P.; Shu, Y.; Jiang, C.-H.; Tan, Z.-R.; Zhou, H.-H. Inducibility of CYP1A2 by omeprazole in vivo related to the genetic polymorphism of CYP1A2. Br. J. Clin. Pharmacol. 2002, 54, 540–543. [Google Scholar] [CrossRef] [Green Version]
- Sergentanis, T.N.; Economopoulos, K.P. Four polymorphisms in cytochrome P450 1A1 (CYP1A1) gene and breast cancer risk: A meta-analysis. Breast Cancer Res. Treat. 2010, 122, 459–469. [Google Scholar] [CrossRef] [Green Version]
- Yao, L.; Yu, X.; Yu, L. Lack of significant association between CYP1A1 T3801C polymorphism and breast cancer risk: A meta-analysis involving 25,087 subjects. Breast Cancer Res. Treat. 2010, 122, 503–507. [Google Scholar] [CrossRef]
- Cui, X.; Lu, X.; Hiura, M.; Omori, H.; Miyazaki, W.; Katoh, T. Association of genotypes of carcinogen-metabolizing enzymes and smoking status with bladder cancer in a Japanese population. Environ. Health Prev. Med. 2013, 18, 136–142. [Google Scholar] [CrossRef] [Green Version]
- Wang, H.; Zhang, Z.; Han, S.; Lu, Y.; Feng, F.; Yuan, J. CYP1A2 rs762551 polymorphism contributes to cancer susceptibility: A meta-analysis from 19 case-control studies. BMC Cancer 2012, 12, 528. [Google Scholar] [CrossRef] [Green Version]
- Chen, Y.; Zeng, L.; Wang, Y.; Tolleson, W.H.; Knox, B.; Chen, S.; Ren, Z.; Guo, L.; Mei, N.; Qian, F.; et al. The expression, induction and pharmacological activity of CYP1A2 are post-transcriptionally regulated by microRNA hsa-miR-132-5p. Biochem. Pharmacol. 2017, 145, 178–191. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Gill, P.; Bhattacharyya, S.; McCullough, S.; Letzig, L.; Mishra, P.J.; Luo, C.; Dweep, H.; James, L. MicroRNA regulation of CYP 1A2, CYP3A4 and CYP2E1 expression in acetaminophen toxicity. Sci. Rep. 2017, 7, 12331. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Sansen, S.; Yano, J.K.; Reynald, R.L.; Schoch, G.A.; Griffin, K.J.; Stout, C.D.; Johnson, E.F. Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2. J. Biol. Chem. 2007, 282, 14348–14355. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Tassaneeyakul, W.; Birkett, D.J.; Veronese, M.E.; McManus, M.E.; Tukey, R.H.; Quattrochi, L.C.; Gelboin, H.V.; Miners, J.O. Specificity of substrate and inhibitor probes for human cytochromes P450 1A1 and 1A2. J. Pharmacol. Exp. Ther. 1993, 265, 401–407. [Google Scholar] [PubMed]
- Tassaneeyakul, W.; Mohamed, Z.; Birkett, D.J.; McManus, M.E.; Veronese, M.E.; Tukey, R.H.; Quattrochi, L.C.; Gonzalez, F.J.; Miners, J.O. Caffeine as a probe for human cytochromes P450: Validation using cDNA-expression, immunoinhibition and microsomal kinetic and inhibitor techniques. Pharmacogenetics 1992, 2, 173–183. [Google Scholar] [CrossRef] [PubMed]
- Ma, Q.; Lu, A.Y.H. CYP1A induction and human risk assessment: An evolving tale of in vitro and in vivo studies. Drug Metab. Dispos. 2007, 35, 1009–1016. [Google Scholar] [CrossRef] [Green Version]
- Androutsopoulos, V.P.; Tsatsakis, A.M.; Spandidos, D.A. Cytochrome P450 CYP1A1: Wider roles in cancer progression and prevention. BMC Cancer 2009, 9, 187. [Google Scholar] [CrossRef] [Green Version]
- Nakamura, H.; Ariyoshi, N.; Okada, K.; Nakasa, H.; Nakazawa, K.; Kitada, M. CYP1A1 is a major enzyme responsible for the metabolism of granisetron in human liver microsomes. Curr. Drug Metab. 2005, 6, 469–480. [Google Scholar] [CrossRef]
- Mescher, M.; Tigges, J.; Rolfes, K.M.; Shen, A.L.; Yee, J.S.; Vogeley, C.; Krutmann, J.; Bradfield, C.A.; Lang, D.; Haarmann-Stemmann, T. The Toll-like receptor agonist imiquimod is metabolized by aryl hydrocarbon receptor-regulated cytochrome P450 enzymes in human keratinocytes and mouse liver. Arch. Toxicol. 2019, 93, 1917–1926. [Google Scholar] [CrossRef]
- Liu, L.; Wang, Q.; Xie, C.; Xi, N.; Guo, Z.; Li, M.; Hou, X.; Xie, N.; Sun, M.; Li, J.; et al. Drug interaction of ningetinib and gefitinib involving CYP1A1 and efflux transporters in non-small cell lung cancer patients. Br. J. Clin. Pharmacol. 2020. [Google Scholar] [CrossRef]
- Niwa, T.; Sato, R.; Yabusaki, Y.; Ishibashi, F.; Katagiri, M. Contribution of human hepatic cytochrome P450s and steroidogenic CYP17 to the N-demethylation of aminopyrine. Xenobiotica 1999, 29, 187–193. [Google Scholar] [CrossRef] [PubMed]
- Norman, T.R.; Olver, J.S. Agomelatine for depression: Expanding the horizons? Expert Opin. Pharmacother. 2019, 20, 647–656. [Google Scholar] [CrossRef] [PubMed]
- Bertilsson, L.; Carrillo, J.A.; Dahl, M.L.; Llerena, A.; Alm, C.; Bondesson, U.; Lindström, L.; La Rodriguez de Rubia, I.; Ramos, S.; BENITEZ, J. Clozapine disposition covaries with CYP1A2 activity determined by a caffeine test. Br. J. Clin. Pharmacol. 1994, 38, 471–473. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Long, L.; Dolan, M.E. Role of cytochrome P450 isoenzymes in metabolism of O(6)-benzylguanine: Implications for dacarbazine activation. Clin. Cancer Res. 2001, 7, 4239–4244. [Google Scholar]
- Lobo, E.D.; Bergstrom, R.F.; Reddy, S.; Quinlan, T.; Chappell, J.; Hong, Q.; Ring, B.; Knadler, M.P. In vitro and in vivo evaluations of cytochrome P450 1A2 interactions with duloxetine. Clin. Pharmacokinet. 2008, 47, 191–202. [Google Scholar] [CrossRef] [PubMed]
- Shet, M.S.; McPhaul, M.; Fisher, C.W.; Stallings, N.R.; Estabrook, R.W. Metabolism of the antiandrogenic drug (Flutamide) by human CYP1A2. Drug Metab. Dispos. 1997, 25, 1298–1303. [Google Scholar]
- Kalgutkar, A.S.; Nguyen, H.T.; Vaz, A.D.N.; Doan, A.; Dalvie, D.K.; McLeod, D.G.; Murray, J.C. In vitro metabolism studies on the isoxazole ring scission in the anti-inflammatory agent lefluonomide to its active alpha-cyanoenol metabolite A771726: Mechanistic similarities with the cytochrome P450-catalyzed dehydration of aldoximes. Drug Metab. Dispos. 2003, 31, 1240–1250. [Google Scholar] [CrossRef]
- Härtter, S.; Grözinger, M.; Weigmann, H.; Röschke, J.; Hiemke, C. Increased bioavailability of oral melatonin after fluvoxamine coadministration. Clin. Pharmacol. Ther. 2000, 67, 1–6. [Google Scholar] [CrossRef]
- Anttila, A.K.; Rasanen, L.; Leinonen, E.V. Fluvoxamine augmentation increases serum mirtazapine concentrations three- to fourfold. Ann. Pharmacother. 2001, 35, 1221–1223. [Google Scholar] [CrossRef]
- Turpeinen, M.; Hofmann, U.; Klein, K.; Mürdter, T.; Schwab, M.; Zanger, U.M. A predominate role of CYP1A2 for the metabolism of nabumetone to the active metabolite, 6-methoxy-2-naphthylacetic acid, in human liver microsomes. Drug Metab. Dispos. 2009, 37, 1017–1024. [Google Scholar] [CrossRef]
- Ring, B.J.; Catlow, J.; Lindsay, T.J.; Gillespie, T.; Roskos, L.K.; Cerimele, B.J.; Swanson, S.P.; Hamman, M.A.; Wrighton, S.A. Identification of the human cytochromes P450 responsible for the in vitro formation of the major oxidative metabolites of the antipsychotic agent olanzapine. J. Pharmacol. Exp. Ther. 1996, 276, 658–666. [Google Scholar] [PubMed]
- Wójcikowski, J.; Pichard-Garcia, L.; Maurel, P.; Daniel, W.A. Contribution of human cytochrome p-450 isoforms to the metabolism of the simplest phenothiazine neuroleptic promazine. Br. J. Pharmacol. 2003, 138, 1465–1474. [Google Scholar] [CrossRef] [Green Version]
- Masubuchi, Y.; Hosokawa, S.; Horie, T.; Suzuki, T.; Ohmori, S.; Kitada, M.; Narimatsu, S. Cytochrome P450 isozymes involved in propranolol metabolism in human liver microsomes. The role of CYP2D6 as ring-hydroxylase and CYP1A2 as N-desisopropylase. Drug Metab. Dispos. 1994, 22, 909–915. [Google Scholar] [PubMed]
- Obach, R.S.; Ryder, T.F. Metabolism of ramelteon in human liver microsomes and correlation with the effect of fluvoxamine on ramelteon pharmacokinetics. Drug Metab. Dispos. 2010, 38, 1381–1391. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Guay, D.R.P. Rasagiline (TVP-1012): A new selective monoamine oxidase inhibitor for Parkinson’s disease. Am. J. Geriatr. Pharmacother. 2006, 4, 330–346. [Google Scholar] [CrossRef] [PubMed]
- Sanderink, G.J.; Bournique, B.; Stevens, J.; Petry, M.; Martinet, M. Involvement of human CYP1A isoenzymes in the metabolism and drug interactions of riluzole in vitro. J. Pharmacol. Exp. Ther. 1997, 282, 1465–1472. [Google Scholar]
- Kaye, C.M.; Nicholls, B. Clinical pharmacokinetics of ropinirole. Clin. Pharmacokinet. 2000, 39, 243–254. [Google Scholar] [CrossRef]
- Oda, Y.; Furuichi, K.; Tanaka, K.; Hiroi, T.; Imaoka, S.; Asada, A.; Fujimori, M.; Funae, Y. Metabolism of a new local anesthetic, ropivacaine, by human hepatic cytochrome P450. Anesthesiology 1995, 82, 214–220. [Google Scholar] [CrossRef] [PubMed]
- Spaldin, V.; Madden, S.; Pool, W.F.; Woolf, T.F.; Park, B.K. The effect of enzyme inhibition on the metabolism and activation of tacrine by human liver microsomes. Br. J. Clin. Pharmacol. 1994, 38, 15–22. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Ha, H.R.; Chen, J.; Freiburghaus, A.U.; Follath, F. Metabolism of theophylline by cDNA-expressed human cytochromes P-450. Br. J. Clin. Pharmacol. 1995, 39, 321–326. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Granfors, M.T.; Backman, J.T.; Neuvonen, M.; Neuvonen, P.J. Ciprofloxacin greatly increases concentrations and hypotensive effect of tizanidine by inhibiting its cytochrome P450 1A2-mediated presystemic metabolism. Clin. Pharmacol. Ther. 2004, 76, 598–606. [Google Scholar] [CrossRef] [PubMed]
- Granfors, M.T.; Backman, J.T.; Neuvonen, M.; Ahonen, J.; Neuvonen, P.J. Fluvoxamine drastically increases concentrations and effects of tizanidine: A potentially hazardous interaction. Clin. Pharmacol. Ther. 2004, 75, 331–341. [Google Scholar] [CrossRef] [PubMed]
- Kroemer, H.K.; Gautier, J.C.; Beaune, P.; Henderson, C.; Wolf, C.R.; Eichelbaum, M. Identification of P450 enzymes involved in metabolism of verapamil in humans. Naunyn Schmiedebergs Arch. Pharmacol. 1993, 348, 332–337. [Google Scholar] [CrossRef] [PubMed]
- Wild, M.J.; McKillop, D.; Butters, C.J. Determination of the human cytochrome P450 isoforms involved in the metabolism of zolmitriptan. Xenobiotica 1999, 29, 847–857. [Google Scholar] [CrossRef]
- Fuhr, U.; Jetter, A.; Kirchheiner, J. Appropriate phenotyping procedures for drug metabolizing enzymes and transporters in humans and their simultaneous use in the “cocktail” approach. Clin. Pharmacol. Ther. 2007, 81, 270–283. [Google Scholar] [CrossRef]
- Nebert, D.W.; Dalton, T.P. The role of cytochrome P450 enzymes in endogenous signalling pathways and environmental carcinogenesis. Nat. Reviews Cancer 2006, 6, 947–960. [Google Scholar] [CrossRef]
- Karjalainen, M.J.; Neuvonen, P.J.; Backman, J.T. In vitro inhibition of CYP1A2 by model inhibitors, anti-inflammatory analgesics and female sex steroids: Predictability of in vivo interactions. Basic Clin. Pharmacol. Toxicol. 2008, 103, 157–165. [Google Scholar] [CrossRef]
- Pastrakuljic, A.; Tang, B.K.; Roberts, E.A.; Kalow, W. Distinction of CYP1A1 and CYP1A2 activity by selective inhibition using fluvoxamine and isosafrole. Biochem. Pharmacol. 1997, 53, 531–538. [Google Scholar] [CrossRef]
- Somers, G.I.; Harris, A.J.; Bayliss, M.K.; Houston, J.B. The metabolism of the 5HT3 antagonists ondansetron, alosetron and GR87442 I: A comparison of in vitro and in vivo metabolism and in vitro enzyme kinetics in rat, dog and human hepatocytes, microsomes and recombinant human enzymes. Xenobiotica 2007, 37, 832–854. [Google Scholar] [CrossRef]
- Kobayashi, K.; Nakajima, M.; Chiba, K.; Yamamoto, T.; Tani, M.; Ishizaki, T.; Kuroiwa, Y. Inhibitory effects of antiarrhythmic drugs on phenacetin O-deethylation catalysed by human CYP1A2. Br. J. Clin. Pharmacol. 1998, 45, 361–368. [Google Scholar] [CrossRef]
- Bapiro, T.E.; Sayi, J.; Hasler, J.A.; Jande, M.; Rimoy, G.; Masselle, A.; Masimirembwa, C.M. Artemisinin and thiabendazole are potent inhibitors of cytochrome P450 1A2 (CYP1A2) activity in humans. Eur. J. Clin. Pharmacol. 2005, 61, 755–761. [Google Scholar] [CrossRef] [PubMed]
- Masubuchi, Y.; Nakano, T.; Ose, A.; Horie, T. Differential selectivity in carbamazepine-induced inactivation of cytochrome P450 enzymes in rat and human liver. Arch. Toxicol. 2001, 75, 538–543. [Google Scholar] [CrossRef] [PubMed]
- Fuhr, U.; Anders, E.M.; Mahr, G.; Sörgel, F.; Staib, A.H. Inhibitory potency of quinolone antibacterial agents against cytochrome P450IA2 activity in vivo and in vitro. Antimicrob. Agents Chemother. 1992, 36, 942–948. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Martinez, C.; Albet, C.; Agundez, J.; Herrero, E.; Carrillo, J.; Marquez, M.; Benitez, J.; Ortiz, J. Comparative in vitro and in vivo inhibition of cytochrome P450 CYP1A2, CYP2D6, and CYP3A by H -receptor antagonists. Clin. Pharmacol. Ther. 1999, 65, 369–376. [Google Scholar] [CrossRef]
- Zhang, W.; Ramamoorthy, Y.; Kilicarslan, T.; Nolte, H.; Tyndale, R.F.; Sellers, E.M. Inhibition of cytochromes P450 by antifungal imidazole derivatives. Drug Metab. Dispos. 2002, 30, 314–318. [Google Scholar] [CrossRef] [PubMed]
- Paris, B.L.; Ogilvie, B.W.; Scheinkoenig, J.A.; Ndikum-Moffor, F.; Gibson, R.; Parkinson, A. In vitro inhibition and induction of human liver cytochrome p450 enzymes by milnacipran. Drug Metab. Dispos. 2009, 37, 2045–2054. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- von Moltke, L.L.; Greenblatt, D.J.; Schmider, J.; Duan, S.X.; Wright, C.E.; Harmatz, J.S.; Shader, R.I. Midazolam hydroxylation by human liver microsomes in vitro: Inhibition by fluoxetine, norfluoxetine, and by azole antifungal agents. J. Clin. Pharmacol. 1996, 36, 783–791. [Google Scholar] [CrossRef]
- Wen, X.; Wang, J.-S.; Neuvonen, P.J.; Backman, J.T. Isoniazid is a mechanism-based inhibitor of cytochrome P450 1A2, 2A6, 2C19 and 3A4 isoforms in human liver microsomes. Eur. J. Clin. Pharmacol. 2002, 57, 799–804. [Google Scholar] [CrossRef]
- Sai, Y.; Dai, R.; Yang, T.J.; Krausz, K.W.; Gonzalez, F.J.; Gelboin, H.V.; Shou, M. Assessment of specificity of eight chemical inhibitors using cDNA-expressed cytochromes P450. Xenobiotica 2000, 30, 327–343. [Google Scholar] [CrossRef]
- Chun, Y.J.; Kim, M.Y.; Guengerich, F.P. Resveratrol is a selective human cytochrome P450 1A1 inhibitor. Biochem. Biophys. Res. Commun. 1999, 262, 20–24. [Google Scholar] [CrossRef]
- Chang, T.K.; Chen, J.; Lee, W.B. Differential inhibition and inactivation of human CYP1 enzymes by trans-resveratrol: Evidence for mechanism-based inactivation of CYP1A2. J. Pharmacol. Exp. Ther. 2001, 299, 874–882. [Google Scholar] [PubMed]
- Augustin, M.; Schoretsanitis, G.; Pfeifer, P.; Gründer, G.; Liebe, C.; Paulzen, M. Effect of fluvoxamine augmentation and smoking on clozapine serum concentrations. Schizophr. Res. 2019, 210, 143–148. [Google Scholar] [CrossRef] [PubMed]
- Chiu, C.-C.; Lane, H.-Y.; Huang, M.-C.; Liu, H.-C.; Jann, M.W.; Hon, Y.-Y.; Chang, W.-H.; Lu, M.-L. Dose-dependent alternations in the pharmacokinetics of olanzapine during coadministration of fluvoxamine in patients with schizophrenia. J. Clin. Pharmacol. 2004, 44, 1385–1390. [Google Scholar] [CrossRef] [PubMed]
- Yao, C.; Kunze, K.L.; Kharasch, E.D.; Wang, Y.; Trager, W.F.; Ragueneau, I.; Levy, R.H. Fluvoxamine-theophylline interaction: Gap between in vitro and in vivo inhibition constants toward cytochrome P4501A2. Clin. Pharmacol. Ther. 2001, 70, 415–424. [Google Scholar] [CrossRef]
- Becquemont, L.; Ragueneau, I.; Le Bot, M.A.; Riche, C.; Funck-Brentano, C.; Jaillon, P. Influence of the CYP1A2 inhibitor fluvoxamine on tacrine pharmacokinetics in humans. Clin. Pharmacol. Ther. 1997, 61, 619–627. [Google Scholar] [CrossRef]
- Backman, J.T.; Karjalainen, M.J.; Neuvonen, M.; Laitila, J.; Neuvonen, P.J. Rofecoxib is a potent inhibitor of cytochrome P450 1A2: Studies with tizanidine and caffeine in healthy subjects. Br. J. Clin. Pharmacol. 2006, 62, 345–357. [Google Scholar] [CrossRef] [Green Version]
- Meyer, J.M.; Proctor, G.; Cummings, M.A.; Dardashti, L.J.; Stahl, S.M. Ciprofloxacin and Clozapine: A Potentially Fatal but Underappreciated Interaction. Case Rep. Psychiatry 2016, 2016, 5606098. [Google Scholar] [CrossRef] [Green Version]
- Brouwers, E.E.M.; Söhne, M.; Kuipers, S.; van Gorp, E.C.M.; Schellens, J.H.M.; Koks, C.H.W.; Beijnen, J.H.; Huitema, A.D.R. Ciprofloxacin strongly inhibits clozapine metabolism: Two case reports. Clin. Drug Investig. 2009, 29, 59–63. [Google Scholar] [CrossRef]
- Jerling, M.; Lindström, L.; Bondesson, U.; Bertilsson, L. Fluvoxamine inhibition and carbamazepine induction of the metabolism of clozapine: Evidence from a therapeutic drug monitoring service. Ther. Drug Monit. 1994, 16, 368–374. [Google Scholar] [CrossRef]
- Wetzel, H.; Anghelescu, I.; Szegedi, A.; Wiesner, J.; Weigmann, H.; Härter, S.; Hiemke, C. Pharmacokinetic interactions of clozapine with selective serotonin reuptake inhibitors: Differential effects of fluvoxamine and paroxetine in a prospective study. J. Clin. Psychopharmacol. 1998, 18, 2–9. [Google Scholar] [CrossRef]
- Raaska, K.; Neuvonen, P.J. Ciprofloxacin increases serum clozapine and N-desmethylclozapine: A study in patients with schizophrenia. Eur. J. Clin. Pharmacol. 2000, 56, 585–589. [Google Scholar] [CrossRef] [PubMed]
- Perucca, E.; Gatti, G.; Spina, E. Clinical pharmacokinetics of fluvoxamine. Clin. Pharmacokinet. 1994, 27, 175–190. [Google Scholar] [CrossRef] [PubMed]
- Jokinen, M.J.; Olkkola, K.T.; Ahonen, J.; Neuvonen, P.J. Effect of ciprofloxacin on the pharmacokinetics of ropivacaine. Eur. J. Clin. Pharmacol. 2003, 58, 653–657. [Google Scholar] [CrossRef] [PubMed]
- Batty, K.T.; Davis, T.M.; Ilett, K.F.; Dusci, L.J.; Langton, S.R. The effect of ciprofloxacin on theophylline pharmacokinetics in healthy subjects. Br. J. Clin. Pharmacol. 1995, 39, 305–311. [Google Scholar] [CrossRef] [Green Version]
- Granfors, M.T.; Backman, J.T.; Laitila, J.; Neuvonen, P.J. Oral contraceptives containing ethinyl estradiol and gestodene markedly increase plasma concentrations and effects of tizanidine by inhibiting cytochrome P450 1A2. Clin. Pharmacol. Ther. 2005, 78, 400–411. [Google Scholar] [CrossRef]
- Komoroski, B.J.; Zhang, S.; Cai, H.; Hutzler, J.M.; Frye, R.; Tracy, T.S.; Strom, S.C.; Lehmann, T.; Ang, C.Y.W.; Cui, Y.Y.; et al. Induction and inhibition of cytochromes P450 by the St. John’s wort constituent hyperforin in human hepatocyte cultures. Drug Metab. Dispos. 2004, 32, 512–518. [Google Scholar] [CrossRef] [Green Version]
- Andersson, T.; Bergstrand, R.; Cederberg, C.; Eriksson, S.; Lagerström, P.-O.; Skånberg, I. Omeprazole treatment does not affect the metabolism of caffeine. Gastroenterology 1991, 101, 943–947. [Google Scholar] [CrossRef]
- Rizzo, N.; Padoin, C.; Palombo, S.; Scherrmann, J.M.; Girre, C. Omeprazole and lansoprazole are not inducers of cytochrome P4501A2 under conventional therapeutic conditions. Eur. J. Clin. Pharmacol. 1996, 49, 491–495. [Google Scholar] [CrossRef]
- Dilger, K.; Zheng, Z.; Klotz, U. Lack of drug interaction between omeprazole, lansoprazole, pantoprazole and theophylline. Br. J. Clin. Pharmacol. 1999, 48, 438–444. [Google Scholar] [CrossRef] [Green Version]
- Henry, D.; Brent, P.; Whyte, I.; Mihaly, G.; Devenish-Meares, S. Propranolol steady-state pharmacokinetics are unaltered by omeprazole. Eur. J. Clin. Pharmacol. 1987, 33, 369–373. [Google Scholar] [CrossRef]
- Frick, A.; Kopitz, J.; Bergemann, N. Omeprazole reduces clozapine plasma concentrations. A case report. Pharmacopsychiatry 2003, 36, 121–123. [Google Scholar] [CrossRef] [PubMed]
- Lucas, R.A.; Gilfillan, D.J.; Bergstrom, R.F. A pharmacokinetic interaction between carbamazepine and olanzapine: Observations on possible mechanism. Eur. J. Clin. Pharmacol. 1998, 54, 639–643. [Google Scholar] [CrossRef] [PubMed]
- Magnusson, M.O.; Dahl, M.-L.; Cederberg, J.; Karlsson, M.O.; Sandström, R. Pharmacodynamics of carbamazepine-mediated induction of CYP3A4, CYP1A2, and Pgp as assessed by probe substrates midazolam, caffeine, and digoxin. Clin. Pharmacol. Ther. 2008, 84, 52–62. [Google Scholar] [CrossRef] [PubMed]
- Kirby, B.J.; Collier, A.C.; Kharasch, E.D.; Dixit, V.; Desai, P.; Whittington, D.; Thummel, K.E.; Unadkat, J.D. Complex drug interactions of HIV protease inhibitors 2: In vivo induction and in vitro to in vivo correlation of induction of cytochrome P450 1A2, 2B6, and 2C9 by ritonavir or nelfinavir. Drug Metab. Dispos. 2011, 39, 2329–2337. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Penzak, S.R.; Hon, Y.Y.; Lawhorn, W.D.; Shirley, K.L.; Spratlin, V.; Jann, M.W. Influence of ritonavir on olanzapine pharmacokinetics in healthy volunteers. J. Clin. Psychopharmacol. 2002, 22, 366–370. [Google Scholar] [CrossRef] [PubMed]
- Jacobs, B.S.; Colbers, A.P.H.; Velthoven-Graafland, K.; Schouwenberg, B.J.J.W.; Burger, D.M. Effect of fosamprenavir/ritonavir on the pharmacokinetics of single-dose olanzapine in healthy volunteers. Int. J. Antimicrob. Agents 2014, 44, 173–177. [Google Scholar] [CrossRef]
- Pascussi, J.-M.; Gerbal-Chaloin, S.; Duret, C.; Daujat-Chavanieu, M.; Vilarem, M.-J.; Maurel, P. The tangle of nuclear receptors that controls xenobiotic metabolism and transport: Crosstalk and consequences. Annu. Rev. Pharmacol. Toxicol. 2008, 48, 1–32. [Google Scholar] [CrossRef] [Green Version]
- Yeh, R.F.; Gaver, V.E.; Patterson, K.B.; Rezk, N.L.; Baxter-Meheux, F.; Blake, M.J.; Eron, J.J.; Klein, C.E.; Rublein, J.C.; Kashuba, A.D.M. Lopinavir/ritonavir induces the hepatic activity of cytochrome P450 enzymes CYP2C9, CYP2C19, and CYP1A2 but inhibits the hepatic and intestinal activity of CYP3A as measured by a phenotyping drug cocktail in healthy volunteers. J. Acquir. Immune Defic. Syndr. 2006, 42, 52–60. [Google Scholar] [CrossRef] [Green Version]
- Haslemo, T.; Eikeseth, P.H.; Tanum, L.; Molden, E.; Refsum, H. The effect of variable cigarette consumption on the interaction with clozapine and olanzapine. Eur. J. Clin. Pharmacol. 2006, 62, 1049–1053. [Google Scholar] [CrossRef] [Green Version]
- Seppälä, N.H.; Leinonen, E.V.; Lehtonen, M.L.; Kivistö, K.T. Clozapine serum concentrations are lower in smoking than in non-smoking schizophrenic patients. Pharmacol. Toxicol. 1999, 85, 244–246. [Google Scholar] [CrossRef] [Green Version]
- Fric, M.; Pfuhlmann, B.; Laux, G.; Riederer, P.; Distler, G.; Artmann, S.; Wohlschläger, M.; Liebmann, M.; Deckert, J. The influence of smoking on the serum level of duloxetine. Pharmacopsychiatry 2008, 41, 151–155. [Google Scholar] [CrossRef] [PubMed]
- Cassidenti, D.L.; Vijod, A.G.; Vijod, M.A.; Stanczyk, F.Z.; Lobo, R.A. Short-term effects of smoking on the pharmacokinetic profiles of micronized estradiol in postmenopausal women. Am. J. Obstet. Gynecol. 1990, 163, 1953–1960. [Google Scholar] [CrossRef]
- Sitsen, J.; Maris, F.; Timmer, C. Drug-drug interaction studies with mirtazapine and carbamazepine in healthy male subjects. Eur. J. Drug Metab. Pharmacokinet. 2001, 26, 109–121. [Google Scholar] [CrossRef] [PubMed]
- Lind, A.-B.; Reis, M.; Bengtsson, F.; Jonzier-Perey, M.; Powell Golay, K.; Ahlner, J.; Baumann, P.; Dahl, M.-L. Steady-state concentrations of mirtazapine, N-desmethylmirtazapine, 8-hydroxymirtazapine and their enantiomers in relation to cytochrome P450 2D6 genotype, age and smoking behaviour. Clin. Pharmacokinet. 2009, 48, 63–70. [Google Scholar] [CrossRef] [PubMed]
- Sun, L.; McDonnell, D.; Yu, M.; Kumar, V.; Moltke, L. von. A Phase I Open-Label Study to Evaluate the Effects of Rifampin on the Pharmacokinetics of Olanzapine and Samidorphan Administered in Combination in Healthy Human Subjects. Clin. Drug Investig. 2019, 39, 477–484. [Google Scholar] [CrossRef]
- Wu, T.-H.; Chiu, C.-C.; Shen, W.W.; Lin, F.-W.; Wang, L.-H.; Chen, H.-Y.; Lu, M.-L. Pharmacokinetics of olanzapine in Chinese male schizophrenic patients with various smoking behaviors. Prog. Neuropsychopharmacol. Biol. Psychiatry 2008, 32, 1889–1893. [Google Scholar] [CrossRef] [PubMed]
- Zevin, S.; Benowitz, N.L. Drug interactions with tobacco smoking. An update. Clin. Pharmacokinet. 1999, 36, 425–438. [Google Scholar] [CrossRef]
- Fuhr, U.; Woodcock, B.G.; Siewert, M. Verapamil and drug metabolism by the cytochrome P450 isoform CYP1A2. Eur. J. Clin. Pharmacol. 1992, 42, 463–464. [Google Scholar] [CrossRef]
- Jungmann, N.A.; Lang, D.; Saleh, S.; van der Mey, D.; Gerisch, M. In vitro-in vivo correlation of the drug-drug interaction potential of antiretroviral HIV treatment regimens on CYP1A1 substrate riociguat. Expert Opin. Drug Metab. Toxicol. 2019, 15, 975–984. [Google Scholar] [CrossRef] [Green Version]
- Kroon, L.A. Drug interactions with smoking. Am. J. Health Syst. Pharm. 2007, 64, 1917–1921. [Google Scholar] [CrossRef]
- Hiemke, C.; Bergemann, N.; Clement, H.W.; Conca, A.; Deckert, J.; Domschke, K.; Eckermann, G.; Egberts, K.; Gerlach, M.; Greiner, C.; et al. Consensus Guidelines for Therapeutic Drug Monitoring in Neuropsychopharmacology: Update 2017. Pharmacopsychiatry 2018, 51, 9–62. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Faber, M.S.; Fuhr, U. Time response of cytochrome P450 1A2 activity on cessation of heavy smoking. Clin. Pharmacol. Ther. 2004, 76, 178–184. [Google Scholar] [CrossRef] [PubMed]
- Faber, M.S.; Jetter, A.; Fuhr, U. Assessment of CYP1A2 activity in clinical practice: Why, how, and when? Basic Clin. Pharmacol. Toxicol. 2005, 97, 125–134. [Google Scholar] [CrossRef]
- Chochol, M.D.; Kataria, L.; O’Rourke, M.C.; Lamotte, G. Clozapine-Associated Myoclonus and Stuttering Secondary to Smoking Cessation and Drug Interaction: A Case Report. J. Clin. Psychopharmacol. 2019, 39, 275–277. [Google Scholar] [CrossRef] [PubMed]
- Kocar, T.; Freudenmann, R.W.; Spitzer, M.; Graf, H. Switching From Tobacco Smoking to Electronic Cigarettes and the Impact on Clozapine Levels. J. Clin. Psychopharmacol. 2018, 38, 528–529. [Google Scholar] [CrossRef]
- Larsen, J.T.; Brøsen, K. Consumption of charcoal-broiled meat as an experimental tool for discerning CYP1A2-mediated drug metabolism in vivo. Basic Clin. Pharmacol. Toxicol. 2005, 97, 141–148. [Google Scholar] [CrossRef] [PubMed]
- Hakooz, N.; Hamdan, I. Effects of dietary broccoli on human in vivo caffeine metabolism: A pilot study on a group of Jordanian volunteers. Curr. Drug Metab. 2007, 8, 9–15. [Google Scholar] [CrossRef]
- Charron, C.S.; Novotny, J.A.; Jeffery, E.H.; Kramer, M.; Ross, S.A.; Seifried, H.E. Consumption of baby kale increased cytochrome P450 1A2 (CYP1A2) activity and influenced bilirubin metabolism in a randomized clinical trial. J. Funct. Foods 2020, 64, 103624. [Google Scholar] [CrossRef]
- Lake, B.G.; Tredger, J.M.; Renwick, A.B.; Barton, P.T.; Price, R.J. 3,3′-Diindolylmethane induces CYP1A2 in cultured precision-cut human liver slices. Xenobiotica 1998, 28, 803–811. [Google Scholar] [CrossRef]
Liver | Small Intestine | |||||||
---|---|---|---|---|---|---|---|---|
CYP1A1 | CYP1A2 | CYP1A1 | CYP1A2 | |||||
Gene | Protein (Method) | Gene | Protein (Method) | Gene | Protein (Method) | Gene | Protein (Method) | Reference |
- | n.d. (WB) | - | + (WB) | - | - | - | - | [20] |
+ | - | + | + (WB) | - | - | - | - | [13] |
- | + (WB) | - | - | - | - | - | - | [25] |
- | - | - | - | + | + (WB) | n.d. | - | [26] |
- | - | - | - | - | + (WB) | - | - | [27] |
+ | - | + | - | + | - | n.d. | - | [15] |
+ | n.d. (WB) | + | + (WB) | - | - | - | - | [21] |
- | + (WB) | - | + (WB) | - | - | - | - | [14] |
- | + (WB) | - | - | - | + (WB) | - | - | [16] |
+ | - | + | - | + | - | n.d. | - | [17] |
- | - | + | + (PTC) | - | - | - | - | [28] |
- | + (PTCs) | - | + (PTC) | - | - | - | - | [23] |
- | - | - | + (PTC) | - | - | - | n.d. (PTC) | [29] |
- | - | - | - | - | + (PTC) | - | +, traces (PTC) | [30] |
- | - | + | + (PTC) | - | - | n.d. | n.d. (PTC) | [24] |
- | - | - | + (PTC) | - | - | - | - | [31] |
- | - | - | - | + | - | n.d. | - | [32] |
- | n.d. (PTC) | + (PTC) | - | n.d. (PTC) | - | n.d. (PTC) | [22] | |
- | + (PTC) | - | + (PTC) | - | - | - | - | [18] |
Drug | Object of Investigation | Induction Effect | Reference |
---|---|---|---|
Albendazole (5–30 µM) | HepG2 cells | ↑CYP1A1 (32-fold) and CYP1A2 mRNA (5.6-fold); ↑EROD-activity (4-fold) | [49,50] |
Carbamazepine (7–183 µM) | HepaRG cells | ↑CYP1A2 mRNA (10-fold) | [52] |
Carbamazepine | Pediatric patients | ↑hepatic CYP1A2 activity (CBT, 2.2-fold) | [55] |
Lansoprazole (50 µM) | Human hepatocytes | ↑CYP1A2 mRNA (26-fold); ↑CYP1A2 protein (32-fold); ↑EROD activity (32-fold) | [48] |
Omeprazole (0.03–3 µM) | Human hepatocytes | ↑CYP1A1 mRNA (37-fold) | [47] |
Omeprazole (50 µM) | Human hepatocytes | ↑CYP1A2 mRNA (12-fold); ↑CYP1A2 protein (4.6-fold); ↑EROD activity (39-fold) | [48] |
Omeprazole (25 µM) | HepG2 cells | ↑CYP1A1 and CYP1A2 mRNA | [49] |
Omeprazole (treatment) | Human duodenal biopsies | ↑CYP1A1 protein; ↑EROD activity (2.2-fold) | [56] |
Omeprazole (20 mg SID, 4 d) | Human liver biopsies | ↑CYP1A2 protein (3.4-fold); ↑EROD activity (6-fold) | [57] |
Phenobarbital (100–250 µM) | Human hepatocytes | ↑EROD activity (1.9-fold) | [46] |
Phenobarbital (1 mM) | Human hepatocytes | ↑CYP1A2 mRNA (1.5-fold); ↑CYP1A2 protein (1.8-fold); ↑POD activity (3.1-fold) | [58] |
Primaquine (10–30 µM) | HepG2 cells | ↑CYP1A1 (~7-fold) and CYP1A2 (~3-fold) mRNA; ↑EROD-activity (7.5-fold) | [49,50] |
Quinine (30 µM) | HepG2 cells | ↑CYP1A1 (~9-fold) and CYP1A2 mRNA (2.4-fold); ↑EROD-activity (5.5-fold) | [50] |
Rifampicin (10/33 µM) | Human hepatocytes | ↑CYP1A1 (2.2-fold) and CYP1A2 mRNA (2.2-fold) | [47,59,60,61] |
Rifampicin (20/50 µM) | Human hepatocytes | ↑EROD-activity (2.3-fold) | [46] |
Ritonavir (0.1–5 µM) | Human hepatocytes | ±CYP1A2 mRNA (0.8-fold); ±CYP1A2 protein (1.0-fold); ↑POD activity (1.6-fold) | [58] |
Ritonavir (1–25 µM) | Human hepatocytes | ↑CYP1A2 mRNA (4-fold); ↑POD activity (2-fold) | [61] |
Rosiglitazone (10 µM) | Human hepatocytes | ↑CYP1A2 mRNA (11-fold); ↑CYP1A2 protein (7-fold); ↑EROD activity (37-fold) | [48] |
Smoking | Human liver biopsies | ↑EROD activity (3.3-fold) | [62] |
Smoking (3–30/d), 7d | Human duodenal biopsies | ↑EROD activity (4.2-fold) | [56] |
Chargrilled meat diet (7 d) | Human duodenal biopsies | ↑CYP1A1 protein, ↑hepatic CYP1A2 activity (CBT, 1.9-fold) | [33] |
Substrate | Drug Class | Metabolic Reaction | Contribution of CYP1A2 (Other CYPs) | Reference |
---|---|---|---|---|
Aminopyrine | Analgesic drug | N-demethylation | 40–50% (CYP2C8/2C19) | [98] |
Agomelatine | melatonin receptor agonist (antidepressant) | hydroxylation and demethylation | 90% (10% CYP2C9) | [99] |
Caffeine | CNS stimulant | N-demethylation | >95% | [94,95] |
Clozapine | Atypical antipsychotic drug | N-demethylation and N-oxidation | 40–55% (CYP3A4/2C19) | [100] |
Dacarbazine | Anticancer drug | N-demethylation | 20–40% (CYP1A1/2E1) | [101] |
Duloxetine | Antidepressant | 4-, 5- and 6-hydroxylation major extent substrate | 30–40% (CYP2D6/2C9) | [102] |
Flutamide | Non-steroidal antiandrogen | 2-Hydroxylation | ~25% (CYP3A4/2C19) | [103] |
Leflunomide | Disease-modifying anti-inflammatory drug | N-O bond cleavage | 40–55% | [104] |
Melatonin | Pineal hormone | 6-hydroxylation and O-demethylation | 40–60% (CYP1A1/1B1) | [105] |
Mirtazapine | Antidepressant | 8-hydroxylation and N-demethylation | 30–50% (CYP3A4/2D6) | [106] |
Nabumetone | NSAID | aliphatic hydroxylation | 30–40% (CYP2C9) | [107] |
Olanzapine | Atypical antipsychotic drug | N-demethylation and 7-hydroxylation | 30–40% (CYP2D6) | [108] |
Phenacetin | Analgesic drug | O-deethylation and C-hydroxylation | 86% | [94] |
Promazine | Antipsychotic drug | N-demethylation and 5-sulfoxidation | 30–45% (CYP2C19/3A4) | [109] |
Propranolol | β-Blocker | N-deisopropylation, and 4- and 5-hydroxylation | 30–50% (CYP2D6) | [110] |
Ramelteon | Melatonin receptor agonist (hypnotic) | Aliphatic hydroxylation | ~50% (CYP2C19/3A4) | [111] |
Rasagiline | Antiparkinson drug | N-dealkylation and hydroxylation | >50% | [112] |
Riluzole | Antiglutamate agent (treatment of ALS) | N-hydroxylation | ~80% | [113] |
Ropinirole | Antiparkinson drug | N-depropylation and hydroxylation (major) | 30–45% | [114] |
Ropivacaine | Local anesthetic drug | 3-, 4-hydroxylation | 50–65% (CYP3A4) | [115] |
Tacrine | cholinesterase inhibitor (Alzheimer’s disease) | 1-, 2-, 4- and 7-Hydroxylation | 50–65% | [116] |
Theophylline | Bronchodilator (Asthma/COPD) | N-demethylation | 90–95% | [117] |
Tizanidine | Muscle relaxant | Hydroxylation | 80–95% | [118,119] |
Verpamil | Calcium channel blocker | N-demethylation and N-dealkylation | 20–30% (CYP2C8/3A4) | [120] |
Zolmitriptan | Selective 5-HT1B/1D (treatment of migraine) | N-demethylation and O-demethlyation | 30–40% | [121] |
Drug | Drug Class | In Vitro System | Inhibitory Effect (Isoenzyme) | Reference |
---|---|---|---|---|
Alosetron 1 | 5HT3-receptor antagonist (irritable bowel syndrome) | HLM | IC50 = 2 µM (CYP1A2) | [129] |
Amiodarone 1 | Antiarrhythmic drug | HLM | IC50 = 86 µM | [130] |
Artemesinin 1 | Antimalaria drug | HLM | Ki = 0.43 μM (CYP1A2) | [131] |
Carbamazepine 2 | Anticonvulsant | HLM | n.d. (CYP1A2) | [132] |
Celecoxib 1 | COX-2 inhibitor | HLM | Ki = 25.4 µM (CYP1A2) | [127] |
Ciprofloxacin 1 | Antibiotic (fluoroquinolone) | HLM HLM | 70.4% (CYP1A2) Ki = 144 nM (CYP1A2) | [133] [127] |
Cimetidine 1 | H2-receptor antagonist | HLM | Ki = 200 µM (CYP1A2) | [134] |
Clotrimazole 1 | Antifungal agent | human lymphoblast cells | Ki = 7.9 µM (CYP1A2) | [135] |
Desogestrel 1 | Hormone (oral contraceptive) | HLM | Ki = 39.4 µM (CYP1A2) | [127] |
Duloxetine 2 | Antidepressant (SSRI) | HLM | n.d. (CYP1A2) | [136] |
Enoxacin 1 | Antibiotic (fluoroquinolone) | HLM | 74.9% (CYP1A2) | [133] |
Ethinyl estradiol 1 | Hormone (oral contraceptive) | HLM | Ki = 10.6 µM (CYP1A2) | [127] |
Fluoxetine 1 | Antidepressant (SSRI) | HLM | Ki = 4.4 µM (CYP1A2) | [137] |
Fluvoxamine 1 | Antidepressant (SSRI) | HLM | Ki = 33 µM (CYP1A1) Ki = 40 nM (CYP1A2) Ki = 11 nM (CYP1A2) | [128] [128] [127] |
Isoniazid 2 | Antibiotic | HLM | Ki = 285 µM (CYP1A2) | [138] |
Ketoconazole 1 | Antifungal agent | HIM HLM | Ki = 40 nM (CYP1A1) IC50 = 0.33 µM CYP1A2) | [27] [139] |
Miconazole 1 | Antifungal agent | human lymphoblast cells | Ki = 3.2 µM (CYP1A2) | [135] |
Nifedipine 1 | Calcium channel blocker | HLM | n.d. (CYP1A1) n.d. (CYP1A2) | [94] |
Norfloxacin 1 | Antibiotic (fluoroquinolone) | HLM | 55.7% (CYP1A2) | [133] |
Paroxetine 1 | Antidepressant (SSRI) | HLM | Ki = 5.5 µM (CYP1A2) | [137] |
Propafenone 1 | Antiarrhythmic drug | HLM | IC50 = 29 µM | [130] |
Propranolol | Beta blocker | HLM | n.d. (CYP1A1) n.d. (CYP1A2) | [94] |
Resveratrol 2 | Natural compound | HLM | IC50 = 23 µM (CYP1A1) Ki = 2.2 µM (CYP1A2) | [140] [141] |
Riluzole 1 | Amyotrophic lateral sclerosis drug | HLM | Ki = 12.1 µM (CYP1A2) | [113] |
Rofecoxib 2 | COX-2 inhibitor | HLM | Ki = 6.2 µM (CYP1A2) | [127] |
Sertraline 1 | Antidepressant (SSRI) | HLM | Ki = 8.8 µM (CYP1A2) | [137] |
Sulconazole | Antifungal agent | human lymphoblast cells | Ki = 0.4 µM (CYP1A2) | [135] |
Thiabendazol 2 | Antifungal/antiparasitic agent | HLM | Ki = 1.54 μM (CYP1A2) | [131] |
Tioconazole 1 | Antifungal agent | human lymphoblast cells | Ki = 0.4 µM (CYP1A2) | [135] |
Tolfenamic acid 1 | NSAID | HLM | Ki= 1.4 µM (CYP1A2) | [127] |
Substrate (Victim Drug) | Perpetrator (Inhibitor) | PK Change | Reference |
---|---|---|---|
Agomelatine | Fluvoxamine | AUC ↑ 60-fold | Product information |
Caffeine (137 mg, SD) | Thiabendazol (500 mg, SD) | AUC ↑ 1.6-fold t1/2 ↑ 2.4-fold | [131] |
Clozapine (50–700 mg) | Fluvoxamine (50–100 mg, SID, MD) | CSS ↑ 5-10-fold | [149] |
Clozapine (2.5–3.0 mg/kg) | Fluvoxamine (50 mg, SID, MD) | CSS ↑ 3-fold | [150] |
Clozapine (200–350 mg) | Fluvoxamine (50 mg, SID, MD) | CSS ↑ 2.2-fold | [142] |
Clozapine (150–400 mg) | Ciprofloxacin (250 mg BID, 7 d) | CSS ↑ 1.3-fold | [151] |
Duloxetine (60 mg, SD) | Fluvoxamine (100 mg SID, 16 d) | AUC ↑ 5.6-fold CMAX ↑ 2.4-fold | [102] |
Melatonin (5 mg, SD) | Fluvoxamine (50 mg, SD) | AUC ↑ 17-fold CMAX ↑ 12-fold | [105] |
Mirtazapin (15–30 mg) | Fluvoxamine (50–100 mg, SID, MD) | CSS ↑ 1.3-fold | [106] |
Olanzapine (10 mg, SD) | Fluvoxamine (100 mg, SID, 14 d) | AUC ↑ 1.5-fold CMAX ↑ 1.6-fold | [143] |
Propranolol (160 mg, SID) | Fluvoxamine (100 mg) | CMAX ↑ 5-fold | [152] |
Ramelteon (16 mg, SD) | Fluvoxamine (100 mg BID, 3 d) | AUC ↑ 190-fold CMAX ↑ 70-fold | Product information [111] |
Ropivacaine (0.6 mg/kg, iv) | Ciprofloxacin (500 mg BID, 2.5 d) | CL ↓ 31% | [153] |
Tacrine (40 mg, SD) | Fluvoxamine (100 mg SID, 6 d) | AUC ↑ 8.3-fold CMAX ↑ 5.6-fold | [145] |
Theophylline (250 mg, SD) | Fluvoxamine (75 mg, SD) | AUC ↑ 2.4-fold t1/2 ↑ 2.5-fold | [144] |
Theophylline (3.4 mg/kg, SD) | Ciprofloxacin (500 mg BID, 3 d) | CL ↓ 19% t1/2 ↑ 26% | [154] |
Tizanidine (4 mg, SD) | Rofecoxib (25 mg SID, 4d) | AUC ↑ 13.6-fold CMAX ↑ 6.1-fold | [146] |
Tizanidine (4 mg, SD) | Ciprofloxacin (500 mg BID, 3 d) | AUC ↑ 10-fold CMAX ↑ 7-fold | [118] |
Tizanidine (4 mg, SD) | Fluvoxamine (100 mg SID, 4d) | AUC ↑ 33-fold CMAX ↑ 12-fold | [119] |
Tizanidine (4 mg, SD) | Ethinyl estradiol 20–30 µg, gestodene 75 µg | AUC ↑ 3.9-fold CMAX ↑ 3-fold | [155] |
Ropivacaine (0.6 mg/kg, iv) | Ciprofloxacin (500 mg BID, 2.5 d) | CL ↓ 31% | [153] |
Substrate (Victim Drug) | Perpetrator | PK Change | Reference |
---|---|---|---|
Antipyrine (20 mg/kg, SD) | Smoking | CL ↑ 46% | [62] |
Caffeine (100 mg, SD) | Carbamazepine (400 mg, SID, 14 d) | CL ↑ 27–47% | [163] |
Caffeine (2 mg/mg, SD) | Lopinavir (400 mg)/Ritonavir (100 mg), BID, 14 d | MR ↑ 43% | [168] |
Caffeine (200 mg, SD) | Rifampicin (400 mg BID, 14 d) | AUC ↓ 60% CL ↑ 214% | [164] |
Caffeine (200 mg, SD) | Ritonavir (400 mg BID, 14 d) | AUC ↓ 75% CL ↑ 290% | [164] |
Clozapine (150–900 mg) | Smoking (7–>20/d) | CSS ↓ 50% CSS ↓ 40% | [169] [170] |
Clozapine (325 mg) | Omeprazole (40–60 mg, MD) | CSS ↓ 42–45% | [161] |
Clozapine | Carbamazepine | CSS ↓ 50% | [149] |
Duloxetine (86–102 mg, MD) | Smoking | CSS ↓ 53% | [171] |
Estradiol (1–2 mg) | Smoking | CSS ↓ 43% | [172] |
Mirtazapine (15–30 mg, SID, 7 d) | Carbamazepine (200-400 mg, BID, 21 d) | AUC ↓ 63% Cmax ↓ 44% | [173] |
Mirtazapine (30 mg, SID, 28 d) | Smoking | CSS ↓ 41% | [174] |
Olanzapine | Carbamazepine | CL ↑ 46% t1/2 ↓ 20% | [162] |
Olanzapine (10 mg, SD) | Rifampicin, 600 mg, SID, 7 d | AUC ↓ 48% Cmax ↓ 11% | [175] |
Olanzapine | Ritonavir (300–500 mg BID, 3–5 d) | AUC ↓ 53% CMAX ↓ 40% | [165] |
Olanzapine | Smoking (light, 1–4/d) Smoking (medium, >5) Smoking (heavy, 7–>20) | AUC ↓ 45% AUC ↓ 68% CSS ↓ 67% | [176] [176] [169] |
Theophylline | Smoking | CL ↑ 58–100% t1/2 ↓ 63% | [177] |
Tizanidine | Rifampicin, 500 mg, SID, 5 d | AUC ↓ 53% | [64] |
Tizanidine | Smoking | AUC ↓ 33% | [68] |
Verapamil | Smoking | AUC ↓ 20% | [178] |
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Klomp, F.; Wenzel, C.; Drozdzik, M.; Oswald, S. Drug–Drug Interactions Involving Intestinal and Hepatic CYP1A Enzymes. Pharmaceutics 2020, 12, 1201. https://doi.org/10.3390/pharmaceutics12121201
Klomp F, Wenzel C, Drozdzik M, Oswald S. Drug–Drug Interactions Involving Intestinal and Hepatic CYP1A Enzymes. Pharmaceutics. 2020; 12(12):1201. https://doi.org/10.3390/pharmaceutics12121201
Chicago/Turabian StyleKlomp, Florian, Christoph Wenzel, Marek Drozdzik, and Stefan Oswald. 2020. "Drug–Drug Interactions Involving Intestinal and Hepatic CYP1A Enzymes" Pharmaceutics 12, no. 12: 1201. https://doi.org/10.3390/pharmaceutics12121201