Induction of CYP1A1 and CYP1A2 expressions by prototypic and atypical inducers in the human lung

Wei, Cindy; Caccavale, Robert J.; Weyand, Eric H.; Chen, Suzie; Iba, Michael M.

doi:10.1016/s0304-3835(01)00809-6

Cited by 48 publications

(27 citation statements)

References 40 publications

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“…Several studies have also reported the presence of CYP1A2 in the brain, with its distribution also being regioselective (reviewed in Hedlund et al 2001;Strobel et al 2001). The reported presence of CYP1A2 in the brain is at variance with the common opinion that expression of the enzyme is exclusive to the liver, but is in agreement with reports of the expression of the enzyme in several peripheral, extrahepatic tissues in humans (Lechevrel et al 1999;Mace et al 1998;McDonnell et al 1992;Tatemichi et al 1999;Wei et al 2001Wei et al , 2002Williams et al 2000) and experimental animals (Beebe et al 1995;Iba and Fung 2001).…”

Section: Introductionsupporting

confidence: 66%

Constitutive and inducible levels of CYP1A1 and CYP1A2 in rat cerebral cortex and cerebellum

Iba

Storch

Ghosal

et al. 2003

Archives of Toxicology

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We examined the constitutive and inducible levels of microsomal cytochromes P450 1A1 and 1A2 (CYP1A) in rat cerebral cortex and cerebellum at the level of proteins by western blot analysis, and by catalytic activities via ethoxyresorufin O-deethylase (EROD) and methoxyresorufin O-demethylase (MROD). In the cerebral cortex, cytochrome P450 1A1 (CYP1A1) protein was more abundant than cytochrome P450 1A2 (CYP1A2) protein. Treatment with beta-naphthoflavone (beta-NF) caused a slight decrease in the level of the former but induced the latter 5.8-fold. In the cerebellum, in contrast to the cerebral cortex, CYP1A1 protein was less abundant than CYP1A2 protein in untreated rats, and while beta-NF treatment caused a 3.3-fold induction of CYP1A1 protein, it resulted in a 10-fold decrease in CYP1A2 protein. The CYP1A-preferential activity EROD was 2.3-fold higher in the cerebellum than in the cerebral cortex, and was induced 1.5-fold and 1.9-fold in the cerebellum and cerebral cortex, respectively, by beta-NF treatment. The CYP1A2-preferential activity MROD was 3-fold higher in the cerebellum than in the cerebral cortex, and was repressed 2.2-fold in the cerebellum but induced 3.7-fold in the cerebral cortex following beta-NF treatment. The results show that CYP1A1 and CYP1A2 proteins and catalytic activities are constitutively expressed in brain but are differentially inducible in the rat cerebral cortex and cerebellum.

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Section: Introductionsupporting

confidence: 66%

Constitutive and inducible levels of CYP1A1 and CYP1A2 in rat cerebral cortex and cerebellum

Iba

Storch

Ghosal

et al. 2003

Archives of Toxicology

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“…Enhanced pulmonary CYP1A1 and hepatic CYP1A2 mRNA expression that is seen in parallel with corresponding increases in enzyme activities provides evidence that omeprazole induces pulmonary CYP1A1 and hepatic CYP1A2 expression by transcriptional activation of CYP1A1 and CYP1A2 gene expression in WT mice. Wei et al (2002) also observed that omeprazole induces pulmonary CYP1A1 in human lung samples using an explant culture system. Although hyperoxia decreased pulmonary and hepatic CYP1A enzyme activities and mRNA expression compared with their corresponding room air groups, CYP1A activities and mRNA expression were higher in omeprazole-treated animals exposed to hyperoxia compared with room air-breathing, corn oil-treated animals.…”

Section: Omeprazole Decreases Oxidant Lung Injury 109mentioning

confidence: 77%

Omeprazole Attenuates Hyperoxic Lung Injury in Mice via Aryl Hydrocarbon Receptor Activation and Is Associated with Increased Expression of Cytochrome P4501A Enzymes

Shivanna

Jiang²,

Wang³

et al. 2011

J Pharmacol Exp Ther

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Hyperoxia contributes to lung injury in experimental animals and bronchopulmonary dysplasia (BPD) in preterm infants. Cytochrome P4501A (CYP1A) enzymes, which are regulated by the aryl hydrocarbon receptor (AhR), have been shown to attenuate hyperoxic lung injury in rodents. Omeprazole, a proton pump inhibitor, used in humans to treat gastric acid-related disorders, induces hepatic CYP1A in vitro. However, the mechanism by which omeprazole induces CYP1A and its impact on CYP1A expression in vivo and hyperoxic lung injury are unknown. Therefore, we tested the hypothesis that omeprazole attenuates hyperoxic lung injury in adult wild-type (WT) C57BL/6J mice by an AhR-mediated induction of pulmonary and hepatic CYP1A enzymes. Accordingly, we determined the effects of omeprazole on pulmonary and hepatic CYP1A expression and hyperoxic lung injury in adult WT and AhR dysfunctional (AhRd) mice. We found that omeprazole attenuated lung injury in WT mice. Attenuation of lung injury by omeprazole paralleled enhanced pulmonary CYP1A1 and hepatic CYP1A2 expression in the omeprazole-treated mice. On the other hand, omeprazole failed to enhance pulmonary CYP1A1 and hepatic CYP1A2 expression and protect against hyperoxic lung injury in AhRd mice. In conclusion, our results suggest that omeprazole attenuates hyperoxic lung injury in mice by AhR-mediated mechanisms, and this phenomenon is associated with induction of CYP1A enzymes. These studies have important implications for the prevention and/or treatment of hyperoxia-induced disorders such as BPD in infants and acute respiratory distress syndrome in older children and adults.

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“…There is evidence of the role of nicotine in the induction of CYP1A1 and CYP1A2 enzymes in vitro in rat lung [4], and in vivo in rat lung, kidney and liver [5][6][7], liver and placenta of pregnant rats [8] and in brains of mice and rats [9,10], probably through mechanisms not involving AHR. Some evidence exists for the induction of CYP1A1 by nicotine in human pulmonary explant culture [11].We recently published a study on the effects of 10 day dosing of nicotine on human CYP2A6 and CYP2E1 activities [12]. An additional aim of that study was to determine the effects of high dose nicotine on the pharmacokinetics of oral caffeine and to test the hypothesis that nicotine induces CYP1A2-mediated metabolism of caffeine to paraxanthine, a well-established probe reaction of CYP1A2 activity [13].…”

mentioning

confidence: 99%

Effect of nicotine on cytochrome P450 1A2 activity

Hukkanen

Jacob

Peng

et al. 2011

Brit J Clinical Pharma

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Cigarette smoking accelerates the metabolism of certain drugs, particularly those primarily metabolized by cytochrome P450 1A2 (CYP1A2) and, to a lesser extent, CYP2E1 and some UDP-glucuronosyltransferases [1,2]. The induction of CYP1A2 is mediated by binding of polycyclic aromatic hydrocarbons of the tobacco smoke to the aryl hydrocarbon receptor (AHR) with consequent transcriptional activation of the CYP1A2 gene. Furthermore, CYP1A1 and CYP1B1 enzymes are induced by tobacco smoking via AHR in various human tissues such as lung and placenta [3]. As CYP1A1 and CYP1B1 are mostly expressed in extrahepatic tissues, their induction by smoking is not known to affect the pharmacokinetics of any medication. There is evidence of the role of nicotine in the induction of CYP1A1 and CYP1A2 enzymes in vitro in rat lung [4], and in vivo in rat lung, kidney and liver [5][6][7], liver and placenta of pregnant rats [8] and in brains of mice and rats [9,10], probably through mechanisms not involving AHR. Some evidence exists for the induction of CYP1A1 by nicotine in human pulmonary explant culture [11].We recently published a study on the effects of 10 day dosing of nicotine on human CYP2A6 and CYP2E1 activities [12]. An additional aim of that study was to determine the effects of high dose nicotine on the pharmacokinetics of oral caffeine and to test the hypothesis that nicotine induces CYP1A2-mediated metabolism of caffeine to paraxanthine, a well-established probe reaction of CYP1A2 activity [13]. No previous study has studied the effects of nicotine on CYP1A2 activity in humans in vivo.The details of the experimental protocol and the subject characteristics are described in a prior report [12]. Briefly, 12 healthy smokers were given two 21 mg transdermal patches delivering a total of 42 mg nicotine day -1 or placebo patches, each for 10 days in a randomized and crossover design. Subjects were not allowed to smoke or to use any tobacco products during hospitalization. At noon on the eighth hospital day, 200 mg of oral caffeine was given. Blood samples were collected for measurement of caffeine and metabolites at 0, 30 and 60 min, and then 2, 3, 4, 6, 8, 12, 20, 32, 44 and 52 h after ingestion of caffeine. In addition, deuterium-labelled nicotine-D2 and cotinine-D4 phenotyping for CYP2A6, bupropion phenotyping for CYP2B6 and chlorzoxazone phenotyping for CYP2E1 were performed on the seventh and eighth hospital days as previously described [12].Concentrations of caffeine, paraxanthine, theobromine and theophylline in plasma were determined using liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS). Stable isotope-labelled analogues of paraxanthine and caffeine were used as internal standards. Following protein precipitation, samples (0.2 ml) were treated with phosphate buffer and extracted with a mixture of methylene chloride, ethyl acetate and isopropyl alcohol. The extracts were evaporated, reconstituted in the LC mobile phase, and injected into the LC-MS/MS system. The mass spectrometer was operated using ...

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Induction of CYP1A1 and CYP1A2 expressions by prototypic and atypical inducers in the human lung

Cited by 48 publications

References 40 publications

Constitutive and inducible levels of CYP1A1 and CYP1A2 in rat cerebral cortex and cerebellum

Constitutive and inducible levels of CYP1A1 and CYP1A2 in rat cerebral cortex and cerebellum

Omeprazole Attenuates Hyperoxic Lung Injury in Mice via Aryl Hydrocarbon Receptor Activation and Is Associated with Increased Expression of Cytochrome P4501A Enzymes

Effect of nicotine on cytochrome P450 1A2 activity

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