PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 2628419-0 1989 Role of growth hormone in modulating the constitutive and phenobarbital-induced levels of two P-450(6)beta (testosterone 6 beta-hydroxylase) mRNAs in rat livers. Phenobarbital 58-71 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 94-139 3785219-17 1986 P450PCN2 mRNA was not significantly induced by PCN or dexamethasone but was readily induced by phenobarbital. Phenobarbital 95-108 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 0-8 3266213-1 1988 Characteristics of a typical male-dominant reaction, dealkylation of n-propoxycoumarin, in rat livers were studied in relation to microsomal testosterone 6 beta-hydroxylase. n-propoxycoumarin 69-86 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 141-172 3785219-18 1986 Testosterone 6 beta-hydroxylase activity was also induced severalfold by PCN, dexamethasone, and phenobarbital. Pregnenolone Carbonitrile 73-76 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 0-31 3785219-18 1986 Testosterone 6 beta-hydroxylase activity was also induced severalfold by PCN, dexamethasone, and phenobarbital. Dexamethasone 78-91 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 0-31 3785219-18 1986 Testosterone 6 beta-hydroxylase activity was also induced severalfold by PCN, dexamethasone, and phenobarbital. Phenobarbital 97-110 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 0-31 31317804-2 2020 We investigated whether bergamottin would be useful for evaluating CYP3A-mediated intestinal metabolism in rats utilising its characteristics as a mechanism-based inhibitor of CYP3A.2. bergamottin 24-35 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 176-183 32663714-8 2020 We found that cytochrome P450 (CYP) (i.e. CYP2C11, CYP2D2 and CYP3A2 enzymes and carboxylesterases) is responsible for the enantioselective metabolism of IFP in liver. methyl isofenphos 154-157 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 62-68 32738202-2 2020 The aim of the present study was to investigate the effects of acacetin on the activities of the cytochrome P450 family members CYP1A2, CYP2B1, CYP2C11, CYP2D1, CYP2E1, and CYP3A2 in rat liver microsomes in vitro and rats in vivo to evaluate potential herb-drug interactions by using a cocktail approach. acacetin 63-71 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 173-179 32738202-5 2020 In vitro, the mode of acacetin inhibition of CYP2B1, CYP2C11, and CYP2E1 was competitive, while mixed inhibition was observed for CYP1A2 and CYP3A2. acacetin 22-30 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 141-147 32874920-3 2020 As a result, 4-MeMBI and 5-MeMBI (>=12.5 muM) inhibited CYP3A2 activity. 4-membi 13-20 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 56-62 32874920-3 2020 As a result, 4-MeMBI and 5-MeMBI (>=12.5 muM) inhibited CYP3A2 activity. 5-membi 25-32 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 56-62 32898626-10 2021 Screening experiments using recombinant rat cytochrome P450 (CYP) isoforms showed that CYP1A1, CYP2C6, CYP2C11, CYP2D1, and CYP3A2 were involved in GM metabolism. geissoschizine methylether 148-150 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 124-130 32898626-11 2021 Of these CYP isoforms, the use of anti-rat CYP antibodies indicated that male-dependent CYP2C11 and CYP3A2 were predominantly involved in the liver microsomal GM metabolism with gender differences. geissoschizine methylether 159-161 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 100-106 32898626-12 2021 CONCLUSIONS: These results suggest that the cause of gender differences in plasma GM pharmacokinetics in rats is most likely because of male-dependent CYP2C11 and CYP3A2, and provide also useful information to further evaluate the pharmacological and toxicological effects in future. geissoschizine methylether 82-84 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 163-169 32860801-4 2020 The pharmacokinetics data for P450-metabolizing substrates showed that the clearance of substrates for Cyp1A2 and Cyp3A2 in the stored PRC resuscitation group were decreased compared to sham group. UNII-Q8SP783P3P 135-138 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 114-120 31925794-7 2020 SqRT-PCR analysis results showed that medium and high doses of OST (20, and 40 mg/kg, respectively) had inhibitory effect on Cyp3a1 mRNA expression but not on Cyp3a2 mRNA expression. osthol 63-66 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 159-165 31820026-8 2020 PCB exposure also reduced body weight, serum IGF-1, and hepatic expression of mRNAs encoding the male-specific GH-pattern-regulated CYP2C11 and CYP3A2 relative to controls (P < 0.05). Polychlorinated Biphenyls 0-3 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 144-150 31925794-8 2020 Western blot analysis results indicated that the inhibitory effect of the medium, high OST doses on Cyp3a1 and Cyp3a2 protein expression was significantly different. osthol 87-90 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 111-117 31925794-5 2020 Semi-quantitative RT-PCR (SqRT-PCR) analysis was used to study the effect of OST on Cyp3a1 and Cyp3a2 mRNA expression and Western blot analysis was used to investigate the effect of OST on Cyp3a1 and Cyp3a2 protein expression. osthol 77-80 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 95-101 32016858-8 2020 The content of CYP3A1 protein was increased by the dose of 100 mg/kg/day and CYP3A2 protein was increased by all administered doses of lycopene. Lycopene 135-143 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 77-83 32009949-11 2019 According to the pharmacokinetic parameters, SNS had moderate inhibitory effects in the reserpine-induced depression model on CYP1A2, CYP2D1, CYP2E1, and CYP3A2, but no significant metabolic changes to CYP2C6 and CYP2D2. shigyaku-san 45-48 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 154-160 32009949-11 2019 According to the pharmacokinetic parameters, SNS had moderate inhibitory effects in the reserpine-induced depression model on CYP1A2, CYP2D1, CYP2E1, and CYP3A2, but no significant metabolic changes to CYP2C6 and CYP2D2. Reserpine 88-97 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 154-160 31787743-0 2019 Vitamin D3 Is Transformed into 1,25(OH)2D3 by Triggering CYP3A11(CYP3A4) Activity and Hydrolyzing Midazolam. Cholecalciferol 0-10 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 57-64 31787743-0 2019 Vitamin D3 Is Transformed into 1,25(OH)2D3 by Triggering CYP3A11(CYP3A4) Activity and Hydrolyzing Midazolam. Calcitriol 31-42 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 57-64 31787743-3 2019 This study aimed to investigate effects of vitamin D3 (VD3) on CYP3A11 activity. Cholecalciferol 43-53 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 63-70 31787743-10 2019 Expressions of hepatic CYP3A11 were more than 10-fold higher in rats treated with vitamin D3 compared to Control rats (p<0.05). Cholecalciferol 82-92 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 23-30 31787743-12 2019 CYP3A11 expressions in vitamin D3-treated groups were significantly higher compared to the Control group (p<0.05). Cholecalciferol 23-33 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 0-7 31787743-15 2019 CONCLUSIONS Vitamin D3 was transformed into 1,25(OH)2D3 by triggering CYP3A11 and CYP3A11 activity and by hydrolyzing MDZ. Cholecalciferol 12-22 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 70-77 31787743-15 2019 CONCLUSIONS Vitamin D3 was transformed into 1,25(OH)2D3 by triggering CYP3A11 and CYP3A11 activity and by hydrolyzing MDZ. Cholecalciferol 12-22 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 82-89 30825074-4 2019 METHODS: This study was performed to investigate the inhibitory effects of myricetin on human CYP3A4, CYP2B6, CYP2C9, CYP2D6 and rat CYP3A2, CYP2B1, CYP2C11, CYP2D1 through the cocktail approach using ultra-performance liquid chromatography tandem mass spectrometry. myricetin 75-84 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 133-139 31867158-8 2019 In rats, intestinal Cyp3a1 and Cyp3a2 mRNAs were induced by 1,25-D3 or lithocholic acid (LCA), whereas hepatic Cyp3a2, but not Cyp3a1 and Cyp3a9, was modulated to 1,25-D3 treatment. Calcitriol 60-67 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 31-37 31867158-8 2019 In rats, intestinal Cyp3a1 and Cyp3a2 mRNAs were induced by 1,25-D3 or lithocholic acid (LCA), whereas hepatic Cyp3a2, but not Cyp3a1 and Cyp3a9, was modulated to 1,25-D3 treatment. Lithocholic Acid 71-87 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 31-37 31867158-8 2019 In rats, intestinal Cyp3a1 and Cyp3a2 mRNAs were induced by 1,25-D3 or lithocholic acid (LCA), whereas hepatic Cyp3a2, but not Cyp3a1 and Cyp3a9, was modulated to 1,25-D3 treatment. Lithocholic Acid 89-92 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 31-37 31481128-12 2019 Furthermore, PRHE increased CYP1A1 and 1A2 activities while decreasing CYP3A2 activity in the livers of AFB1-treated rats. Aflatoxin B1 104-108 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 71-77 31321577-6 2019 Although no PK change was noticed after a single coadministration, significantly decreased plasma and brain concentrations of CBZ and CBZE with inhibited rat liver Cyp3a2 were demonstrated after long-term combined administration. carbamazepine epoxide 134-138 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 164-170 31145889-11 2019 In addition, mHA11 dose-dependently inhibited the activities of rat CYP isozymes, including CYP1A2, CYP2C6, CYP2C11, CYP2D2, CYP2E1 and CYP3A2. mha11 13-18 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 136-142 31092394-6 2019 In vitro studies showed that hepatic levels of CES1 protein and activity and Ces1e mRNA were significantly lower in ZDF than in control rats, as were the mRNA levels of CYP2B1/2, CYP2C11, and CYP3A2, and levels of CYP2B6-, CYP2C19-, and CYP3A4-related proteins and enzymatic activities in liver microsomes of ZDF rats. zdf 116-119 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 192-198 30632627-6 2019 CsA was used as a CYP3A1/2 and transporter inhibitor, and olive oil was used as a vehicle. Cyclosporine 0-3 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 18-26 31321577-6 2019 Although no PK change was noticed after a single coadministration, significantly decreased plasma and brain concentrations of CBZ and CBZE with inhibited rat liver Cyp3a2 were demonstrated after long-term combined administration. Carbamazepine 126-129 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 164-170 30927680-14 2019 The enhancement in Cmax, AUC0-t, T1/2, and MRT and the reduction in Kel and CL/F values resulted from the significant inhibition of CYP3 A2, the CYP2C11-mediated metabolism of CBZ in the liver, and the inhibition of intestinal P-glycoprotein/MDR1, which enhanced the rate of CBZ absorption. Carbamazepine 176-179 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 132-139 30927680-14 2019 The enhancement in Cmax, AUC0-t, T1/2, and MRT and the reduction in Kel and CL/F values resulted from the significant inhibition of CYP3 A2, the CYP2C11-mediated metabolism of CBZ in the liver, and the inhibition of intestinal P-glycoprotein/MDR1, which enhanced the rate of CBZ absorption. Carbamazepine 275-278 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 132-139 30927680-0 2019 Effects of sinapic acid on hepatic cytochrome P450 3A2, 2C11, and intestinal P-glycoprotein on the pharmacokinetics of oral carbamazepine in rats: Potential food/herb-drug interaction. Carbamazepine 124-137 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 35-54 29979512-2 2017 Tolbutamide, chlorzoxazone, theophylline, midazolam, omeprazole and dextromethorphanwere used as substrates of CYP2C6, CYP2E1, CYP1A2, CYP3A2, CYP2D1, and CYP2D2 to test the depressionimpact on drug metabolism. Tolbutamide 0-11 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 135-141 31105024-0 2019 Dexamethasone changes the pharmacokinetics of amitriptyline and reduces its accumulation in rat brain: The roles of P-gp and cyp3a2. Dexamethasone 0-13 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 125-131 31105024-6 2019 We propose that cyp3a2 and P-gp could be upregulated in the liver and blood-brain barrier (BBB) when using DEX. Dexamethasone 107-110 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 16-22 30648588-2 2019 This study aimed to investigate the effect of orally administered sinapic acid (SA) on the pharmacokinetics of aripiprazole (APZ) in rats and its possible modulatory effects on hepatic cytochrome P450 (CYP3A2 and CYP2D6) expression in the liver tissues. sinapinic acid 66-78 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 202-208 30648588-2 2019 This study aimed to investigate the effect of orally administered sinapic acid (SA) on the pharmacokinetics of aripiprazole (APZ) in rats and its possible modulatory effects on hepatic cytochrome P450 (CYP3A2 and CYP2D6) expression in the liver tissues. sinapinic acid 80-82 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 202-208 30648588-21 2019 This was associated with a reduction in CYP3A2 and CYP2D6 protein expressions by 33-43% and -71-68% after the single and multiple co-administration, which are two enzymes responsible of the metabolism of APZ. Aripiprazole 204-207 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 40-46 30334444-2 2018 We previously demonstrated that female offspring of obese rats have increased serum estradiol levels during early postnatal life, probably because of decreased hepatic cytochrome P450 3A2 levels, which could lead to early onset of puberty and polycystic ovary condition in adulthood. Estradiol 84-93 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 168-187 30334444-4 2018 We found that metformin prevented an increase in serum estradiol levels at postnatal day 14 in female offspring of obese mothers, which was associated with a restoration of hepatic cytochrome P450 3A2 levels to control values. Metformin 14-23 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 181-200 30138636-3 2018 The purpose of this study is to evaluate the inhibition effects of apatinib on human and rat cytochrome P450, including CYP3A2/4, CYP2B1/6, CYP2C9/11, CYP2D1/6, and CYP2E1. apatinib 67-75 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 120-126 30369879-5 2018 CYP1A2, CYP2C11, CYP2D1, and CYP3A2 were involved in the metabolism of LB and the relative strength was: CYP3A2 > CYP2C11 > CYP2D1 > CYP1A2. loureirin B 71-73 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 29-35 30369879-5 2018 CYP1A2, CYP2C11, CYP2D1, and CYP3A2 were involved in the metabolism of LB and the relative strength was: CYP3A2 > CYP2C11 > CYP2D1 > CYP1A2. loureirin B 71-73 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 105-111 29090414-7 2018 The group treated with tamoxifen-loaded SLN showed significantly increased gene expression of CYP3A2 in comparison with the control, healthy, and group treated with free tamoxifen. Tamoxifen 23-32 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 94-100 29090414-7 2018 The group treated with tamoxifen-loaded SLN showed significantly increased gene expression of CYP3A2 in comparison with the control, healthy, and group treated with free tamoxifen. Tamoxifen 170-179 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 94-100 29090414-10 2018 Encapsulation of tamoxifen inside solid lipid nanoparticles increased the gene expression of CYP3A2 and decreased the gene expression of FMO1. Tamoxifen 17-26 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 93-99 28253826-8 2017 This result indicates that the 14 day-intragastric administration of codeine may inhibit the metabolism of bupropion (CYP2B1) and midazolam (CYP3A2) in rat. Codeine 69-76 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 141-147 28253826-8 2017 This result indicates that the 14 day-intragastric administration of codeine may inhibit the metabolism of bupropion (CYP2B1) and midazolam (CYP3A2) in rat. Midazolam 130-139 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 141-147 28941798-6 2017 The aim of this study was to investigate the potential inhibition of shikonin against CYP1A2, CYP2B1/6, CYP2C9/11, CYP2D1/6, CYP2E1 and CYP3A2/4 activities in human and rat liver microsomes through cocktail approach in vitro. shikonin 69-77 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 136-142 28941798-10 2017 Interestingly, shikonin presented an atypical kinetic inhibition of CYP3A2-mediated midazolam 1-hydroxylation in rats. Midazolam 84-93 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 68-74 30785057-6 2019 The effects of dasatinib on CYP3A2 mRNA and protein expression levels were also investigated. Dasatinib 15-24 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 28-34 30785057-7 2019 RESULTS: Dasatinib significantly reduced the maximum blood concentration (Cmax) of cyclosporine by 85.7%, and increased hepatic and intestinal CYP3A2 mRNA and protein expression levels by 2.4- and 1.25-fold, respectively, compared to those in the controls (p < 0.05). Dasatinib 9-18 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 143-149 29090414-1 2018 The objective of this study was to investigate the effect of free tamoxifen and tamoxifen-loaded solid lipid nanoparticles (SLN) on cytochrome P450 (CYP3A2) and flavin-containing monooxygenase1 (FMO1) genes expression in the liver of female Wistar rats. Tamoxifen 66-75 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 149-155 29090414-1 2018 The objective of this study was to investigate the effect of free tamoxifen and tamoxifen-loaded solid lipid nanoparticles (SLN) on cytochrome P450 (CYP3A2) and flavin-containing monooxygenase1 (FMO1) genes expression in the liver of female Wistar rats. Tamoxifen 80-89 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 149-155 29979512-2 2017 Tolbutamide, chlorzoxazone, theophylline, midazolam, omeprazole and dextromethorphanwere used as substrates of CYP2C6, CYP2E1, CYP1A2, CYP3A2, CYP2D1, and CYP2D2 to test the depressionimpact on drug metabolism. dextromethorphanwere 68-88 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 135-141 29979512-2 2017 Tolbutamide, chlorzoxazone, theophylline, midazolam, omeprazole and dextromethorphanwere used as substrates of CYP2C6, CYP2E1, CYP1A2, CYP3A2, CYP2D1, and CYP2D2 to test the depressionimpact on drug metabolism. Chlorzoxazone 13-26 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 135-141 29979512-2 2017 Tolbutamide, chlorzoxazone, theophylline, midazolam, omeprazole and dextromethorphanwere used as substrates of CYP2C6, CYP2E1, CYP1A2, CYP3A2, CYP2D1, and CYP2D2 to test the depressionimpact on drug metabolism. Theophylline 28-40 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 135-141 29979512-2 2017 Tolbutamide, chlorzoxazone, theophylline, midazolam, omeprazole and dextromethorphanwere used as substrates of CYP2C6, CYP2E1, CYP1A2, CYP3A2, CYP2D1, and CYP2D2 to test the depressionimpact on drug metabolism. Omeprazole 53-63 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 135-141 26913515-5 2017 Therefore, in this study, we investigated the expressions of hepatic CYP1A2, CYP2B1, CYP2D1, and CYP3A2 in rats suffering bTBI. btbi 122-126 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 97-103 26913515-7 2017 The results showed that bTBI could significantly reduce mRNA expressions of CYP1A2, CYP2D1, and CYP3A2 at the early stage and induce the expressions from 48 h to 1 week after injury. btbi 24-28 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 96-102 26913515-11 2017 In conclusion, our work has, for the first time, indicated that bTBI has significant impact on the expressions of CYP1A2, CYP2B1, CYP2D1, and CYP3A2, which may be related to the cytokines induced by the injury. btbi 64-68 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 142-148 29911377-0 2017 [Induction study of CYP3A2 in male rats by zolmitriptan]. zolmitriptan 43-55 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 20-26 27919644-4 2017 Methionine and Metovitan regulated the level of CYP2E1 and CYP3A2 mRNA expression. Methionine 0-10 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 59-65 27919644-4 2017 Methionine and Metovitan regulated the level of CYP2E1 and CYP3A2 mRNA expression. metovitan 15-24 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 59-65 29911377-1 2017 In our preliminary studies, we observed zolmitriptan (ZOL) treatment led to induction of CYP3A2 in male not female rats. zolmitriptan 40-52 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 89-95 29911377-1 2017 In our preliminary studies, we observed zolmitriptan (ZOL) treatment led to induction of CYP3A2 in male not female rats. zolmitriptan 54-57 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 89-95 29911377-9 2017 These findings demonstrated CYP3A2 inducibility by ZOL was gender-selective. zolmitriptan 51-54 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 28-34 27882225-7 2016 The expression of peroxidase, catalase, CYP1A2, CYP3A2 and CYP2C11 in the liver were upregulated following SDC. S-[2-(Aminosulfonyl)ethyl]-D-Cysteine 107-110 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 48-54 27228199-8 2016 In vivo experiment demonstrated that both HM-1 and ethyl acetate extracts could inhibit Cyp3a2 in rats. ethyl acetate 51-64 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 88-94 27228199-9 2016 In conclusion, the metabolism of xanthones from the origin herb involved multiple CYP450 isoforms; in vitro, metabolism of HM-5 was similar to that of its parent drug HM-1, but their inhibition effects upon CYP450s were different; in vivo, Cyp3a2 could be inhibited by HM-1 and ethyl acetate extracts. Xanthones 33-42 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 240-246 27228199-9 2016 In conclusion, the metabolism of xanthones from the origin herb involved multiple CYP450 isoforms; in vitro, metabolism of HM-5 was similar to that of its parent drug HM-1, but their inhibition effects upon CYP450s were different; in vivo, Cyp3a2 could be inhibited by HM-1 and ethyl acetate extracts. hm-5 123-127 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 240-246 26463278-10 2015 Quantification of CYP2B3, CYP3A2 and CYP1A2 mRNA identified significant effects of nicotine and PCB 95 co-exposure on hepatic CYP3A2 and hippocampal CYP1A2 transcripts. Nicotine 83-91 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 26-32 27523289-5 2016 Hepatic levels of cytochrome b5, CYP2B1, CYP2C11, CYP2E1, and CYP3A2 were decreased in 5-week-old ZDF rats, but not in 11-week-old ZDF rats. zdf 98-101 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 62-68 26959552-6 2016 RESULTS: The IC50 values in inhibition studies were found to be 59.42 muM (CYP1A2), >100 muM (CYP2C11, CYP2D6, CYP3A2) for lupeol, 52.24 muM (CYP1A2), and >100 muM (CYP2C9, CYP2D6, CYP3A2) for betulin. betulin 199-206 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 114-120 26806536-4 2016 The rank order of Cyp3a2 mRNA expression mirrored its protein expression, i.e., DA>BN>SD>WI, and was similar to the CYP3A2-dependent warfarin metabolic activity, i.e., DA>SD>BN>WI. Warfarin 142-150 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 125-131 26869434-8 2016 The inhibitor of CYP3A2 had strong inhibitory effect on OMT metabolism in a concentration-dependent manner, and value was reduced to 29.73% of control. oxymatrine 56-59 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 17-23 26869434-9 2016 The 2 perfusion techniques indicated that poor bioavailability of OMT in rats is due mostly to poor absorption and higher hepatic elimination and CYP3A2 appears to contribute to OMT metabolism in rat liver. oxymatrine 178-181 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 146-152 26463278-10 2015 Quantification of CYP2B3, CYP3A2 and CYP1A2 mRNA identified significant effects of nicotine and PCB 95 co-exposure on hepatic CYP3A2 and hippocampal CYP1A2 transcripts. Nicotine 83-91 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 126-132 25430796-7 2015 The gender difference in corydaline hepatic metabolic clearance was supported by a significantly slower metabolism of corydaline in hepatic microsomes of female rats mediated via male-specific (CYP2C11 and CYP3A2) or male-dominant (CYP3A1) CYP isozymes. corydaline 118-128 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 206-212 26037413-2 2015 Rat primary hepatocytes were incubated with midazolam (which is metabolized mainly by CYP3A2) at 37, 32 or 28 C. The Michaelis-Menten constant (Km) and maximum velocity (Vmax) of midazolam were estimated using the Michaelis-Menten equation. Midazolam 44-53 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 86-92 26037413-3 2015 The Km of CYP3A2 midazolam remained unchanged, but the Vmax decreased at 28 C. In rats, whose temperature was maintained at 37, 32 or 28 C by a heat lamp or ice pack, the plasma concentrations of midazolam were higher, whereas those in the brain and liver were unchanged at 28 C. The tissue/plasma concentration ratios were, however, increased significantly. Midazolam 17-26 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 10-16 26037413-3 2015 The Km of CYP3A2 midazolam remained unchanged, but the Vmax decreased at 28 C. In rats, whose temperature was maintained at 37, 32 or 28 C by a heat lamp or ice pack, the plasma concentrations of midazolam were higher, whereas those in the brain and liver were unchanged at 28 C. The tissue/plasma concentration ratios were, however, increased significantly. Midazolam 198-207 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 10-16 26037413-4 2015 The unbound fraction of midazolam in serum at 28 C was half that at 37 C. These pharmacokinetic changes associated with hypothermic conditions were due to reductions in CYP3A2 activity and protein binding. Midazolam 24-33 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 171-177 26434126-5 2015 Furthermore, diabetic rats treated with thymoquinone demonstrated a marked decrease in hepatic protein expressions of CYP3A2 and CYP2C 11 enzymes that are responsible for the metabolism of glibenclamide. thymoquinone 40-52 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 118-124 26434126-5 2015 Furthermore, diabetic rats treated with thymoquinone demonstrated a marked decrease in hepatic protein expressions of CYP3A2 and CYP2C 11 enzymes that are responsible for the metabolism of glibenclamide. Glyburide 189-202 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 118-124 25430796-7 2015 The gender difference in corydaline hepatic metabolic clearance was supported by a significantly slower metabolism of corydaline in hepatic microsomes of female rats mediated via male-specific (CYP2C11 and CYP3A2) or male-dominant (CYP3A1) CYP isozymes. corydaline 25-35 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 206-212 25430017-0 2015 Change in pharmacokinetic behavior of intravenously administered midazolam due to increased CYP3A2 expression in rats treated with menthol. Midazolam 65-74 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 92-98 25430017-0 2015 Change in pharmacokinetic behavior of intravenously administered midazolam due to increased CYP3A2 expression in rats treated with menthol. Menthol 131-138 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 92-98 25430017-9 2015 The expression levels of mRNA and protein for hepatic CYP3A2 were more than 2.5-fold higher than the control levels when the rats were treated with menthol, whereas no changes were observed in the expression levels of CYP3A1. Menthol 148-155 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 54-60 25430017-10 2015 These results indicate that menthol enhanced the elimination clearance of midazolam by inducing hepatic CYP3A2 and that careful attention should be paid when menthol is ingested in combination with drugs that act as substrates for CYP3A. Menthol 28-35 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 104-110 25430017-10 2015 These results indicate that menthol enhanced the elimination clearance of midazolam by inducing hepatic CYP3A2 and that careful attention should be paid when menthol is ingested in combination with drugs that act as substrates for CYP3A. Midazolam 74-83 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 104-110 25548518-10 2014 A molecular docking study showed that XKB bound to the active site of human cytochrome P450 3A4 and rat Cyp3a2 homology model via the formation of hydrogen bonds. Hydrogen 147-155 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 104-110 22186153-6 2012 Additionally, human CYP3A4 and rat CYP3A2 were the primary enzymes for PA production via heteroatom dealkylation of MEHP. phthalic acid 71-73 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 35-41 25030308-6 2014 On the contrary, the inducing effect of DEX on gene and protein expressions and enzyme activity of CYP3A2 was preserved in moderate liver insufficiency, whereas it was greatly curtailed when liver insufficiency became severe. Dexamethasone 40-43 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 99-105 25038063-0 2014 Aspartame Administration and Insulin Treatment Altered Brain Levels of CYP2E1 and CYP3A2 in Streptozotocin-Induced Diabetic Rats. Aspartame 0-9 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 82-88 25038063-0 2014 Aspartame Administration and Insulin Treatment Altered Brain Levels of CYP2E1 and CYP3A2 in Streptozotocin-Induced Diabetic Rats. Streptozocin 92-106 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 82-88 25038063-1 2014 This study demonstrates that aspartame consumption and insulin treatment in a juvenile diabetic rat model leads to increase in cytochrome P450 (CYP) 2E1 and CYP3A2 isozymes in brain. Aspartame 29-38 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 157-163 25038063-5 2014 Our results indicate that combined treatment with insulin and aspartame in juvenile diabetic rats significantly induced CYP2E1 in the cerebrum and cerebellum without modifying it in the liver, while CYP3A2 protein activity increased both in the brain and in the liver. Insulin 50-57 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 199-205 25038063-5 2014 Our results indicate that combined treatment with insulin and aspartame in juvenile diabetic rats significantly induced CYP2E1 in the cerebrum and cerebellum without modifying it in the liver, while CYP3A2 protein activity increased both in the brain and in the liver. Aspartame 62-71 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 199-205 24647745-4 2014 Moreover, we suggest that CYP2C11 and CYP3A2 are key players in the metabolism to N-demethylate in rat TAECs using the respective anti-rat CYP antibodies (anti-CYP2C11 and anti-CYP3A2). n-demethylate 82-95 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 38-44 24647745-4 2014 Moreover, we suggest that CYP2C11 and CYP3A2 are key players in the metabolism to N-demethylate in rat TAECs using the respective anti-rat CYP antibodies (anti-CYP2C11 and anti-CYP3A2). n-demethylate 82-95 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 177-183 24144799-4 2014 Inhibition of rat CYP isoforms (IC50) by celastrol in potency order was CYP2C11 (10.2 muM)>CYP3A2 (23.2 muM)>CYP1A2 (52.8 muM)>CYP2E1 (74.2 muM)>CYP2D6 (76.4 muM). celastrol 41-50 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 94-100 24144799-5 2014 Enzyme kinetic studies showed that the celastrol was not only a competitive inhibitor of CYP1A2 and 2C11, but also a mixed-type inhibitor of CYP3A2, with Ki of 39.2 muM, 7.05 muM and 14.2 muM, respectively. celastrol 39-48 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 141-147 25866300-8 2014 The hepatic expression of cytochrome P450 4F2 (CYP4F2) and CYP3A2 genes in STZ rats also decreased. Streptozocin 75-78 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 59-65 23312000-2 2013 The immunosuppressant tacrolimus (TAC) is a substrate of cytochrome P450 3A2 (CYP3A2) and P-glycoprotein (P-gp) in rats. Tacrolimus 22-32 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 57-76 23312000-2 2013 The immunosuppressant tacrolimus (TAC) is a substrate of cytochrome P450 3A2 (CYP3A2) and P-glycoprotein (P-gp) in rats. Tacrolimus 22-32 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 78-84 23312000-3 2013 Amlodipine (AML) is an inhibitor of CYP3A2 in rats. Amlodipine 0-10 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 36-42 24133982-5 2013 Because TP is mainly metabolized by CYP3A2 in male rats, the present work indicated that TP-induced increase of CYP3A activity might be an important reason for the rapidly metabolic clearance of TP in rat liver, and GA can reduce the hepatotoxicity of TP by promoting its hepatic metabolic clearance. triptolide 8-10 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 36-42 24133982-5 2013 Because TP is mainly metabolized by CYP3A2 in male rats, the present work indicated that TP-induced increase of CYP3A activity might be an important reason for the rapidly metabolic clearance of TP in rat liver, and GA can reduce the hepatotoxicity of TP by promoting its hepatic metabolic clearance. triptolide 89-91 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 36-42 24133982-5 2013 Because TP is mainly metabolized by CYP3A2 in male rats, the present work indicated that TP-induced increase of CYP3A activity might be an important reason for the rapidly metabolic clearance of TP in rat liver, and GA can reduce the hepatotoxicity of TP by promoting its hepatic metabolic clearance. Glycyrrhetinic Acid 216-218 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 36-42 24133982-5 2013 Because TP is mainly metabolized by CYP3A2 in male rats, the present work indicated that TP-induced increase of CYP3A activity might be an important reason for the rapidly metabolic clearance of TP in rat liver, and GA can reduce the hepatotoxicity of TP by promoting its hepatic metabolic clearance. triptolide 89-91 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 36-42 22445624-0 2012 Silymarin regulates the cytochrome P450 3A2 and glutathione peroxides in the liver of streptozotocin-induced diabetic rats. Silymarin 0-9 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 24-43 22445624-0 2012 Silymarin regulates the cytochrome P450 3A2 and glutathione peroxides in the liver of streptozotocin-induced diabetic rats. Streptozocin 86-100 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 24-43 22445624-1 2012 This study aimed to investigate the protective and regulatory effects of silymarin (SMN) and melatonin (MEL) on streptozotocin (STZ)-induced diabetic changes in cytochrome P450 3A2 (CYP 3A2) and glutathione peroxidase (GPX) expression and antioxidant status in the liver. Silymarin 73-82 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 161-180 22445624-1 2012 This study aimed to investigate the protective and regulatory effects of silymarin (SMN) and melatonin (MEL) on streptozotocin (STZ)-induced diabetic changes in cytochrome P450 3A2 (CYP 3A2) and glutathione peroxidase (GPX) expression and antioxidant status in the liver. Silymarin 73-82 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 182-189 22445624-1 2012 This study aimed to investigate the protective and regulatory effects of silymarin (SMN) and melatonin (MEL) on streptozotocin (STZ)-induced diabetic changes in cytochrome P450 3A2 (CYP 3A2) and glutathione peroxidase (GPX) expression and antioxidant status in the liver. Silymarin 84-87 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 161-180 22445624-1 2012 This study aimed to investigate the protective and regulatory effects of silymarin (SMN) and melatonin (MEL) on streptozotocin (STZ)-induced diabetic changes in cytochrome P450 3A2 (CYP 3A2) and glutathione peroxidase (GPX) expression and antioxidant status in the liver. Melatonin 93-102 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 161-180 22445624-1 2012 This study aimed to investigate the protective and regulatory effects of silymarin (SMN) and melatonin (MEL) on streptozotocin (STZ)-induced diabetic changes in cytochrome P450 3A2 (CYP 3A2) and glutathione peroxidase (GPX) expression and antioxidant status in the liver. Melatonin 93-102 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 182-189 22445624-1 2012 This study aimed to investigate the protective and regulatory effects of silymarin (SMN) and melatonin (MEL) on streptozotocin (STZ)-induced diabetic changes in cytochrome P450 3A2 (CYP 3A2) and glutathione peroxidase (GPX) expression and antioxidant status in the liver. Melatonin 104-107 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 161-180 22445624-1 2012 This study aimed to investigate the protective and regulatory effects of silymarin (SMN) and melatonin (MEL) on streptozotocin (STZ)-induced diabetic changes in cytochrome P450 3A2 (CYP 3A2) and glutathione peroxidase (GPX) expression and antioxidant status in the liver. Streptozocin 112-126 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 161-180 22445624-1 2012 This study aimed to investigate the protective and regulatory effects of silymarin (SMN) and melatonin (MEL) on streptozotocin (STZ)-induced diabetic changes in cytochrome P450 3A2 (CYP 3A2) and glutathione peroxidase (GPX) expression and antioxidant status in the liver. Streptozocin 112-126 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 182-189 22445624-1 2012 This study aimed to investigate the protective and regulatory effects of silymarin (SMN) and melatonin (MEL) on streptozotocin (STZ)-induced diabetic changes in cytochrome P450 3A2 (CYP 3A2) and glutathione peroxidase (GPX) expression and antioxidant status in the liver. Streptozocin 128-131 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 161-180 22445624-12 2012 Moreover, the diabetes-up regulated CYP 3A2 and down regulated GPX, returned to normal values after SMN treatment. Silymarin 100-103 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 36-43 22445624-14 2012 Our data suggest that the STZ-induced diabetes in addition of disturbing the antioxidant status, alters the expression levels of CYP 3A2 and GPX. Streptozocin 26-29 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 129-136 22445624-15 2012 Moreover, the SMN and SMN plus MEL treatment was able to normalize both the antioxidant status and the expression of CYP 3A2 and GPX in the liver of diabetic rats. Silymarin 14-17 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 117-124 24329500-6 2014 Triacontanol preferentially induced protein expression level of CYP3A2 in a dose-dependent manner and of CYP 3A1 at dosage of 120 and 180 mg kg(-1). 1-triacontanol 0-12 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 64-70 24625403-3 2014 DBDPE induced oxidative stress, elevated blood glucose levels, increased CYP2B2 mRNA, CYP2B1/2 protein, 7-pentoxyresorufin O-depentylase (PROD) activity, and induced CYP3A2 mRNA, CYP3A2 protein, and luciferin benzylether debenzylase (LBD) activity. decabromodiphenyl ethane 0-5 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 166-172 24625403-3 2014 DBDPE induced oxidative stress, elevated blood glucose levels, increased CYP2B2 mRNA, CYP2B1/2 protein, 7-pentoxyresorufin O-depentylase (PROD) activity, and induced CYP3A2 mRNA, CYP3A2 protein, and luciferin benzylether debenzylase (LBD) activity. decabromodiphenyl ethane 0-5 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 179-185 23929256-7 2013 The mRNA expression of CYP3A2 in the LN group on day 21 was higher than in rats of the same age in the NN group (P<0.01). nn 103-105 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 23-29 22710810-4 2013 RESULTS: At the low dose only, a modest increase was noted in the hepatic dealkylations of methoxy-, ethoxy-, pentoxyresorufin and benzyloxyquinoline that was accompanied by elevated expression of CYP1 and CYP3A2 apoprotein levels. methoxy-, ethoxy-, pentoxyresorufin 91-126 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 206-212 22710810-4 2013 RESULTS: At the low dose only, a modest increase was noted in the hepatic dealkylations of methoxy-, ethoxy-, pentoxyresorufin and benzyloxyquinoline that was accompanied by elevated expression of CYP1 and CYP3A2 apoprotein levels. 2-(benzyloxy)quinoline 131-149 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 206-212 23710212-7 2013 Multiple doses of baicalin decreased the expression of hepatic CYP3A2 by approximately 58% (P < 0.01) and reduced midazolam 1"-hydroxylation by 23% (P < 0.001) and 4"-hydroxylation by 21% (P < 0.01) in the liver. baicalin 18-26 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 63-69 22416981-9 2012 Cap decreased the absorption of digoxin by inducing CYP3A2 mRNA expression via indirect activation of PXR in LPS-treated rats. Digoxin 32-39 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 52-58 22445624-15 2012 Moreover, the SMN and SMN plus MEL treatment was able to normalize both the antioxidant status and the expression of CYP 3A2 and GPX in the liver of diabetic rats. Silymarin 22-25 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 117-124 22445624-15 2012 Moreover, the SMN and SMN plus MEL treatment was able to normalize both the antioxidant status and the expression of CYP 3A2 and GPX in the liver of diabetic rats. Melatonin 31-34 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 117-124 22331496-5 2012 A transplacental effect of BDE-99, evidenced by the activation of nuclear hormones receptors that induce the upregulation of CYP1A1, CYP1A2, CYP2B1, and CYP3A2 isoforms, was also found in fetal liver. 2,2',4,4',5-brominated diphenyl ether 27-33 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 153-159 22067624-14 2012 CONCLUSIONS: Mild hypothermia reduces the systemic clearances of fentanyl and midazolam in rats after cardiac arrest through alterations in cytochrome P450 3a2 metabolic capacity rather than enzyme affinity as observed with other cytochrome P450s. Fentanyl 65-73 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 140-159 22067624-14 2012 CONCLUSIONS: Mild hypothermia reduces the systemic clearances of fentanyl and midazolam in rats after cardiac arrest through alterations in cytochrome P450 3a2 metabolic capacity rather than enzyme affinity as observed with other cytochrome P450s. Midazolam 78-87 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 140-159 22159698-0 2012 Inhibition of heme oxygenase-1 partially reverses the arsenite-mediated decrease of CYP1A1, CYP1A2, CYP3A23, and CYP3A2 catalytic activity in isolated rat hepatocytes. arsenite 54-62 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 100-106 22186153-6 2012 Additionally, human CYP3A4 and rat CYP3A2 were the primary enzymes for PA production via heteroatom dealkylation of MEHP. mono-(2-ethylhexyl)phthalate 116-120 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 35-41 21474682-4 2011 The evaluation of metabolic rate using recombinant P450s suggested that CYP3A2 and CYP2C11 contributed to 89 and 11% of MDZ metabolism, respectively. Midazolam 120-123 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 72-78 21742899-7 2011 Expression of relevant transporters, such as Multidrug resistance protein 1 (Mdr1), and cytochrome P450 3a2 (Cyp3a2), which metabolizes LPV in rodents, was measured in maternal liver via quantitative reverse transcriptase polymerase chain reaction and Western blot analysis. Lopinavir 136-139 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 88-107 21742899-7 2011 Expression of relevant transporters, such as Multidrug resistance protein 1 (Mdr1), and cytochrome P450 3a2 (Cyp3a2), which metabolizes LPV in rodents, was measured in maternal liver via quantitative reverse transcriptase polymerase chain reaction and Western blot analysis. Lopinavir 136-139 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 109-115 21718207-5 2011 In vitro metabolism studies utilizing hepatic microsomes and recombinant cytochrome (CYP) isoforms clearly indicated that major metabolites of cilostazol were generated extensively with hepatic microsomes of male rats and that male-predominant CYP3A2 and male-specific CYP2C11 were mainly responsible for the hepatic metabolism of cilostazol. Cilostazol 143-153 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 244-250 21945367-5 2011 Expression of phase I (CYP3A2, CYP3A1, CYP2B2) and phase II (SULT2A1) proteins and/or mRNAs was variably affected by alpha-tocopherol injections; however, expression of phase III transporter genes was consistently changed by alpha-tocopherol. alpha-Tocopherol 117-133 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 23-29 21575666-12 2011 These results suggested that CLB-induced hepatomegaly in male rats is mainly attributable to microsomal enzyme induction associated with Cyp2b1, Cyp3a1, Cyp3a2, and Ugt2b2 gene upregulation, but does not cause any toxicological concerns. Clobazam 29-32 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 153-159 21474682-5 2011 Inactivation studies of mibefradil against the two isozymes showed that the maximal inactivation rate constants (k(inact)) were considerable in both isozymes (0.231-0.565 min(-1)), whereas the inhibitor concentration producing half the k(inact) (K(I, app)) of CYP3A2 (0.263-0.410 muM) was a good deal lower than that for CYP2C11 (6.82-11.4 muM). Mibefradil 24-34 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 260-266 21262326-0 2011 Inhibitory effect of tanshinones on rat CYP3A2 and CYP2C11 activity and its structure-activity relationship. tanshinone 21-32 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 40-46 21262326-2 2011 Cryptotanshinone, tanshinone I and tanshinone IIA were competitive CYP3A2 inhibitors (K(i) = 199-243 muM) and CYP2C11 inhibitors (K(i) = 91-118 muM). cryptotanshinone 0-16 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 67-73 21262326-2 2011 Cryptotanshinone, tanshinone I and tanshinone IIA were competitive CYP3A2 inhibitors (K(i) = 199-243 muM) and CYP2C11 inhibitors (K(i) = 91-118 muM). tanshinone 18-30 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 67-73 21262326-2 2011 Cryptotanshinone, tanshinone I and tanshinone IIA were competitive CYP3A2 inhibitors (K(i) = 199-243 muM) and CYP2C11 inhibitors (K(i) = 91-118 muM). tanshinone 35-49 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 67-73 21262326-3 2011 Dihydrotanshinone was not only a noncompetitive inhibitor of CYP3A2 (K(i) = 110 muM), but also a competitive CYP2C11 inhibitor (K(i) = 55 muM). DIHYDROTANSHINONE 0-17 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 61-67 21084653-6 2011 The induction by DEX of CYP3A2 mRNA was 1- to 3-fold greater in rats fed SPI compared with those fed CAS on PND25 (P < 0.05). Dexamethasone 17-20 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 24-30 21428244-1 2011 Triptolide (CAS 38748-32-2), a major active component of Tripterygium wilfordii Hook F (TWHF), was reported to be sex-dependently metabolized mainly due to sex-related expression of CYP3A2. triptolide 0-10 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 182-188 21428244-8 2011 This suggested that neonatal MSG treatment could eliminate the sex-dependent difference in metabolism of triptolide by suppressing CYP3A2 expression and activity in males to the same extent as females. triptolide 105-115 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 131-137 20888898-3 2011 LCA induced rCYP3A1 and rCYP3A9 in the rat jejunum, ileum and colon, rCYP3A2 only in the ileum, rCYP3A9 expression in the liver, and CYP3A4 in the human ileum but not in liver. Lithocholic Acid 0-3 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 69-76 20166883-7 2010 There was a strong correlation between the microsomal ROS generation and total P450 content, CYP3A2 activity or CYP2B1 activity. Reactive Oxygen Species 54-57 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 93-99 20223271-10 2010 In addition, since CYP3A2 is a male-predominant form in rats, significant sex difference in the metabolism of triptolide disappeared in vitro after anti-rat CYP3A2 antibody pretreatment. triptolide 110-120 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 19-25 20223271-10 2010 In addition, since CYP3A2 is a male-predominant form in rats, significant sex difference in the metabolism of triptolide disappeared in vitro after anti-rat CYP3A2 antibody pretreatment. triptolide 110-120 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 157-163 20223271-11 2010 Results suggested that CYP3A2 made an important contribution to the sex-related metabolism of triptolide, which may result in the sex differences in triptolide toxicity. triptolide 94-104 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 23-29 20223271-11 2010 Results suggested that CYP3A2 made an important contribution to the sex-related metabolism of triptolide, which may result in the sex differences in triptolide toxicity. triptolide 149-159 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 23-29 21784028-5 2009 Most of XME analysed were induced by APAP treatment at the gene expression level but at the protein level only CYP3A2 was significantly increased 3h after APAP treatment in DU-exposed rats whereas it remained at a basal level in unexposed rats. Tritium 146-148 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 111-117 20006981-7 2010 The VDR mediated induction of its target genes CYP3A1 and CYP3A2 by 1,25(OH)(2)D(3) or LCA in the rat ileum was strongly reduced in the presence of CDCA despite the higher VDR expression. Lithocholic Acid 87-90 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 58-64 20006981-7 2010 The VDR mediated induction of its target genes CYP3A1 and CYP3A2 by 1,25(OH)(2)D(3) or LCA in the rat ileum was strongly reduced in the presence of CDCA despite the higher VDR expression. Chenodeoxycholic Acid 148-152 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 58-64 20487198-0 2010 Repeated administration of oxycodone modifies the gene expression of several drug metabolising enzymes in the hepatic tissue of male Sprague-Dawley rats, including glutathione S-transferase A-5 (rGSTA5) and CYP3A2. Oxycodone 27-36 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 207-213 20487198-7 2010 KEY FINDINGS: The expression of several drug metabolising enzymes was modulated by oxycodone treatment: cytochrome P450 (CYP) 2B2, CYP2C13, CYP17A1, epoxide hydrolase 2, carboxylesterase 2, flavin-containing monooxygenase 1, glutathione S-transferase alpha 5 (rGSTA5) and CYP3A2. Oxycodone 83-92 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 272-278 20487198-11 2010 In addition, the microsomal activity of CYP3A2, measured via 6beta-hydroxylation of testosterone, was significantly decreased in oxycodone-treated rats. Testosterone 84-96 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 40-46 20487198-11 2010 In addition, the microsomal activity of CYP3A2, measured via 6beta-hydroxylation of testosterone, was significantly decreased in oxycodone-treated rats. Oxycodone 129-138 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 40-46 20487198-12 2010 CONCLUSIONS: Repeated oxycodone administration is associated with a significant up-regulation of rGSTA5 and concomitant down-regulation of CYP3A2 mRNA, protein expression and functionality. Oxycodone 22-31 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 139-145 21784028-5 2009 Most of XME analysed were induced by APAP treatment at the gene expression level but at the protein level only CYP3A2 was significantly increased 3h after APAP treatment in DU-exposed rats whereas it remained at a basal level in unexposed rats. du 173-175 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 111-117 21784028-6 2009 In conclusion, these results showed that a chronic non-nephrotoxic DU exposure specially modify CYP3A2 after a single therapeutic APAP treatment. du 67-69 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 96-102 19504632-5 2009 The positive, middle level and low level zolmitriptan groups exhibited a significant induction effect on CYP 3A2, the activity increase to 2.51, 2.10 and 1.63 times, respectively (P<0.01, <0.05 ). zolmitriptan 41-53 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 105-112 19504632-6 2009 CONCLUSION: Zolmitriptan can significantly induce CYP 3A2 in low and middle concentrations and induce CYP 3A1 in high concentration.PXR is involved in the induction of CYP 3A1/2 by zolmitriptan. zolmitriptan 12-24 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 50-57 20027145-9 2009 Among recombinant rat and human CYP enzymes tested in this study, rat CYP3A2 and human CYP3A4/5, followed by CYP1A1 of both organisms were the most effective enzymes converting 3-ABA. 3-aminobenzanthrone 177-182 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 70-76 19255942-3 2009 In the liver there was a significant enhancement of the hydroxylation of midazolam in the microsomes and expression of cytochrome P450 (CYP) 3A1 messenger RNA (mRNA) and CYP3A2 mRNA. Midazolam 73-82 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 170-176 18823965-4 2009 Neither compound influenced the O-depentylation of pentoxyresorufin or CYP2B apoprotein levels, but sulforaphane caused a modest increase in CYP3A2 apoprotein levels. sulforaphane 100-112 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 141-147 18948380-9 2009 Rat cytochrome P450 (P450) isoforms that showed activity toward several pyrethroids included CYP1A1, CYP1A2, CYP2C6, CYP2C11, CYP3A1, and CYP3A2. Pyrethrins 72-83 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 138-144 19126296-6 2009 CONCLUSIONS: These findings could help explain possible pharmacokinetic changes of furosemide in various rat disease models (where CYP2C11, 2E1, 3A1 and/or CYP3A2 are altered) and drug-drug interactions between furosemide and other drugs (mainly metabolized via CYP2C11, 2E1, 3A1 and/or 3A2). Furosemide 83-93 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 156-162 18670095-0 2008 Effect of thalidomide on endotoxin-induced decreases in activity and expression of hepatic cytochrome P450 3A2. Thalidomide 10-21 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 91-110 19000364-0 2008 Male-specific induction of CYP3A2 in rats by zolmitriptan. zolmitriptan 45-57 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 27-33 19000364-1 2008 We report here a novel observation that zolmitriptan induced CYP3A2 in male but not female rats. zolmitriptan 40-52 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 61-67 19000364-5 2008 Zolmitriptan preferentially induced CYP3A2 in male but not female rats. zolmitriptan 0-12 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 36-42 19000364-7 2008 Thus, we concluded that the observed sex-dependent induction of CYP3A by zolmitriptan was largely due to induction of CYP3A2 in male rats. zolmitriptan 73-85 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 118-124 18789379-5 2008 The activity of hepatic drug-metabolizing enzymes and expression of hepatic cytochrome P450 (CYP) 1A2, CYP3A2 and CYP2D1, which oxidize DZN to DZN-oxon, a potent ChE inhibitor, were measured before DZN injection. Diazinon 136-139 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 103-109 18789379-5 2008 The activity of hepatic drug-metabolizing enzymes and expression of hepatic cytochrome P450 (CYP) 1A2, CYP3A2 and CYP2D1, which oxidize DZN to DZN-oxon, a potent ChE inhibitor, were measured before DZN injection. diazoxon 143-151 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 103-109 18789379-5 2008 The activity of hepatic drug-metabolizing enzymes and expression of hepatic cytochrome P450 (CYP) 1A2, CYP3A2 and CYP2D1, which oxidize DZN to DZN-oxon, a potent ChE inhibitor, were measured before DZN injection. Diazinon 143-146 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 103-109 18809653-3 2008 In addition, to assess the effects on CYP3A2 activities, the pharmacokinetics of midazolam (CYP3A2 substrate) and 1-OH-midazolam (metabolite of midazolam) were investigated. Midazolam 81-90 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 92-98 18827444-6 2008 CYP3A2 mRNA was more strongly induced by dexamethasone, a typical inducer of CYP3A, together with CYP3A1 mRNA, in WI rats than in SD rats (by 2-fold), whereas the CYP1A1 and CYP1A2 mRNA expression induced by beta-naphtoflavone, a typical inducer of CYP1A, did not differ between the two strains. Dexamethasone 41-54 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 0-6 18827444-6 2008 CYP3A2 mRNA was more strongly induced by dexamethasone, a typical inducer of CYP3A, together with CYP3A1 mRNA, in WI rats than in SD rats (by 2-fold), whereas the CYP1A1 and CYP1A2 mRNA expression induced by beta-naphtoflavone, a typical inducer of CYP1A, did not differ between the two strains. beta-naphtoflavone 208-226 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 0-6 18773935-7 2008 CYP3A2 apoprotein levels were modestly elevated in rat liver by both isothiocyanates both of which, however, failed to influence CYP3A4 expression in human liver. Isothiocyanates 69-84 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 0-6 18670095-2 2008 In the present study, we investigated the effects of thalidomide on endotoxin-induced decreases in the activity and expression of hepatic CYP3A2 in rats. Thalidomide 53-64 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 138-144 18670095-7 2008 Western blot analysis revealed that thalidomide had no effect on the protein levels of hepatic CYP3A2, whereas it enhanced the down-regulation of hepatic CYP3A2 by endotoxin. Thalidomide 36-47 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 154-160 18670095-9 2008 The present findings suggest that thalidomide enhances endotoxin-induced decreases in the activity and expression of hepatic CYP3A2. Thalidomide 34-45 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 125-131 18828448-6 2008 Profenofos downregulated levels of hepatic and testicular CYP2C11 and CYP3A2 mRNA and protein expression. profenofos 0-10 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 70-76 18080289-5 2008 RESULTS: In the presence of bromadiolone, the Cyp2e1, Cyp2c13, Cyp3a2 and Cyp3a3 genes were significantly overexpressed, while Cyp2c12 expression was suppressed in resistant female rats compared with susceptible females. bromadiolone 28-40 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 63-69 18279840-6 2008 At higher substrate concentrations, the contribution of CYP1A2 to the metabolism of caffeine decreased in favor of CYP2C11 (N-demethylations) and CYP3A2 (mainly 8-hydroxylation). Caffeine 84-92 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 146-152 18079364-5 2008 Nimesulide, a preferential COX-2 inhibitor, protected rats with TNBS-induced colitis (TNBS-colitis) against the down-regulation of hepatic CYP3A2. nimesulide 0-10 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 139-145 18079364-6 2008 Polymyxin B, which neutralizes endotoxin, curcumin, which has anti-inflammatory properties, and gadolinium chloride, which inactivates macrophages, attenuated the down-regulation of CYP3A2. gadolinium chloride 96-115 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 182-188 21783825-8 2007 CYP1A1/2 and CYP3A2 were induced in hepatic and duodenum microsomes by treatment with CH/ABZ. 4-[4-AMINO-6-(5-CHLORO-1H-INDOL-4-YLMETHYL)-[1,3,5]TRIAZIN-2-YLAMINO]-BENZONITRILE 89-92 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 13-19 17765393-5 2007 Female Sprague-Dawley rats treated with N,N-didesmethyltamoxifen had a 44% decrease (p >0.05) in CYP 3A2 content (the CYP isoform responsible for tamoxifen alpha-hydroxylation), an 18% decrease (p =0.010) in CYP 3A activity, and higher blood levels of tamoxifen and N-desmethyltamoxifen compared to rats treated with solvent. N-desmethyltamoxifen 269-289 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 100-107 17980859-6 2008 Kinetic and inhibition studies indicated that the side-chain N-dealkylation is mediated by CYP2C11 and CYP3A2, whereas the aromatic ring O-demethylation is mediated by CYP2D2 and CYP2C6 in untreated male rats. Nitrogen 61-62 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 103-109 18202523-2 2007 Gd treatment significantly suppressed styrene-inducible cytochrome P4502B1 (CYP2B1), CYP2B2, CYP2E1, and CYP3A2 mRNA expressions to 48.6%, 69.8%, 61.1%, and 38.5%, accompanying with the reduction of proteins expression to 1.42%, 31.2%, 21.1% and 21.1%, respectively, compared with styrene alone treatment. Styrene 38-45 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 105-111 17765393-5 2007 Female Sprague-Dawley rats treated with N,N-didesmethyltamoxifen had a 44% decrease (p >0.05) in CYP 3A2 content (the CYP isoform responsible for tamoxifen alpha-hydroxylation), an 18% decrease (p =0.010) in CYP 3A activity, and higher blood levels of tamoxifen and N-desmethyltamoxifen compared to rats treated with solvent. N,N-didesmethyltamoxifen 40-64 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 100-107 17765393-5 2007 Female Sprague-Dawley rats treated with N,N-didesmethyltamoxifen had a 44% decrease (p >0.05) in CYP 3A2 content (the CYP isoform responsible for tamoxifen alpha-hydroxylation), an 18% decrease (p =0.010) in CYP 3A activity, and higher blood levels of tamoxifen and N-desmethyltamoxifen compared to rats treated with solvent. Tamoxifen 55-64 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 100-107 17765393-5 2007 Female Sprague-Dawley rats treated with N,N-didesmethyltamoxifen had a 44% decrease (p >0.05) in CYP 3A2 content (the CYP isoform responsible for tamoxifen alpha-hydroxylation), an 18% decrease (p =0.010) in CYP 3A activity, and higher blood levels of tamoxifen and N-desmethyltamoxifen compared to rats treated with solvent. Tamoxifen 149-158 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 100-107 17576809-4 2007 Rat P450 isoforms CYP1A1, CYP2C6, CYP2C11, and CYP3A2 and human P450 isoforms CYP2C8, CYP2C19, and CYP3A5 were capable of metabolizing either pyrethroid. Pyrethrins 142-152 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 47-53 17505019-8 2007 Withdrawal of the CYP3A11 substrate testosterone prevented AR activation, whereas AR mRNA expression remained up-regulated. Testosterone 36-48 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 18-25 17484520-6 2007 Myclobutanil and triadimefon treatment at their MTD levels significantly increased rat hepatic mRNA expression of CYP2B1 (14.3- and 54.6-fold), CYP3A23/3A1 (2.2- and 7.3-fold), and CYP3A2 (1.5- and 1.7-fold). systhane 0-12 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 144-150 17442507-2 2007 Hepatic drug-metabolizing enzyme activity was also estimated by measuring the systemic clearance of antipyrine, and the expression of hepatic cytochrome P450 (CYP) 3A2 and CYP1A2, which is closely related to the metabolism from DZN to DZN-oxon, a strong inhibitor of both ChE and AChE. diazoxon 235-243 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 142-167 17484520-6 2007 Myclobutanil and triadimefon treatment at their MTD levels significantly increased rat hepatic mRNA expression of CYP2B1 (14.3- and 54.6-fold), CYP3A23/3A1 (2.2- and 7.3-fold), and CYP3A2 (1.5- and 1.7-fold). triadimefon 17-28 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 144-150 17484520-8 2007 Triadimefon also increased CYP3A2 immunoreactive protein levels 1.8-fold. triadimefon 0-11 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 27-33 17012541-6 2007 Western blot analysis indicated that the level of CYP3A2 expression in warfarin-resistant rats was significantly larger than in warfarin-sensitive rats. Warfarin 71-79 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 50-56 17012541-6 2007 Western blot analysis indicated that the level of CYP3A2 expression in warfarin-resistant rats was significantly larger than in warfarin-sensitive rats. Warfarin 128-136 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 50-56 17125810-6 2007 Western blot and qRT-PCR analysis of CYP1A1, CYP2B1 and CYP3A11 protein and mRNA levels, respectively, further revealed that TSA acts at the transcriptional level. trichostatin A 125-128 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 56-63 16891075-2 2006 A significant decrease (65%) of CYP3A2-related activity (midazolam oxidation) was observed in all senescent rats. Midazolam 57-66 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 32-38 16868070-5 2006 Immunoblot analysis indicated that cryopreserved SHs constitutively expressed CYP1A1/2, CYP2E1, and CYP3A2 as much as 26 days after plating. shs 49-52 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 100-106 17209515-6 2006 The gene expression of CYP3A2 in the simultaneous exposure group was significantly higher than that in the toluene exposure group. Toluene 107-114 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 23-29 16795019-7 2006 These results suggest that bile acids have a pivotal role for bioavailability of FPFS-410 after oral administration of the FPFS-410 complex with HP-beta-CyD through CYP3A2 activity in liver of rats. Bile Acids and Salts 27-37 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 165-171 16795019-7 2006 These results suggest that bile acids have a pivotal role for bioavailability of FPFS-410 after oral administration of the FPFS-410 complex with HP-beta-CyD through CYP3A2 activity in liver of rats. 2-Hydroxypropyl-beta-cyclodextrin 145-156 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 165-171 16872554-2 2006 The formation rate of the major lidocaine metabolite monoethylglycinxylidide (MEGX) has been shown to reflect the activity of CYP3A2 and CYP1A2. Lidocaine 32-41 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 126-132 16858123-3 2006 Of six cDNA-expressed rat P450 isoforms tested, CYP3A2 and CYP2C11 had high rates for N-debutlylation and 3"-hydroxylation of bupivacaine, respectively. Nitrogen 9-10 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 48-54 16872554-2 2006 The formation rate of the major lidocaine metabolite monoethylglycinxylidide (MEGX) has been shown to reflect the activity of CYP3A2 and CYP1A2. monoethylglycinxylidide 53-76 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 126-132 16872554-2 2006 The formation rate of the major lidocaine metabolite monoethylglycinxylidide (MEGX) has been shown to reflect the activity of CYP3A2 and CYP1A2. monoethylglycinexylidide 78-82 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 126-132 16872554-9 2006 The observed changes indicate an impairment of N-deethylation metabolic pathway in streptozotocin-induced diabetic rats, i.e. a possible decrease in the enzymatic activity of CYP3A2 and CYP1A2. Nitrogen 47-48 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 175-181 16872554-9 2006 The observed changes indicate an impairment of N-deethylation metabolic pathway in streptozotocin-induced diabetic rats, i.e. a possible decrease in the enzymatic activity of CYP3A2 and CYP1A2. Streptozocin 83-97 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 175-181 16621933-7 2006 Additionally, both SNP and ISDN significantly reduced the metabolism of DEM to 3-hydroxymorphinan, which is mostly regulated by CYP3A2. Dextromethorphan 72-75 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 128-134 16621933-7 2006 Additionally, both SNP and ISDN significantly reduced the metabolism of DEM to 3-hydroxymorphinan, which is mostly regulated by CYP3A2. norlevorphanol 79-97 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 128-134 16805961-4 2006 Because both drugs are transported via P-glycoprotein and breast cancer resistance protein and metabolized by cytochrome P450 3A2, the interaction of imatinib mesilate with these proteins may be responsible for the increased intestinal absorption of ciclosporin in rats. Imatinib Mesylate 150-158 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 110-129 16805961-4 2006 Because both drugs are transported via P-glycoprotein and breast cancer resistance protein and metabolized by cytochrome P450 3A2, the interaction of imatinib mesilate with these proteins may be responsible for the increased intestinal absorption of ciclosporin in rats. Cyclosporine 250-261 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 110-129 16485119-8 2006 Protection of rats against cisplatin-induced ARF by dimethylthiourea, a hydroxyl radical scavenger, also protected rats against the decrease in serum testosterone levels and the down-regulation of CYP2C11 and CYP3A2. Cisplatin 27-36 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 209-215 16485119-8 2006 Protection of rats against cisplatin-induced ARF by dimethylthiourea, a hydroxyl radical scavenger, also protected rats against the decrease in serum testosterone levels and the down-regulation of CYP2C11 and CYP3A2. 1,3-dimethylthiourea 52-68 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 209-215 16564546-4 2006 To evaluate in vivo the effect of PVL on hepatic drug metabolism, the narcotic activity (sleep time) of midazolam, a specific substrate for CYP3A2, was measured. Midazolam 104-113 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 140-146 16673044-2 2006 Western blotting studies showed that pretreatment with CYP3A inducer such as pregnenolone-16alpha -carbonitrile (PCN) significantly increased the cross reactivity comigrating with hepatic CYP3A1 and CYP3A2 in rat brain microsomes. Pregnenolone Carbonitrile 77-111 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 199-205 16673044-2 2006 Western blotting studies showed that pretreatment with CYP3A inducer such as pregnenolone-16alpha -carbonitrile (PCN) significantly increased the cross reactivity comigrating with hepatic CYP3A1 and CYP3A2 in rat brain microsomes. Pregnenolone Carbonitrile 113-116 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 199-205 16734724-7 2006 In addition, a drastic increase in the gene expression of cytochrome P4503A2 (CYP3A2), an activation enzyme of TAM, by the 8-week treatment with TAM might have contributed to the increased formation of DNA adducts. Tamoxifen 111-114 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 78-84 16734724-7 2006 In addition, a drastic increase in the gene expression of cytochrome P4503A2 (CYP3A2), an activation enzyme of TAM, by the 8-week treatment with TAM might have contributed to the increased formation of DNA adducts. Tamoxifen 145-148 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 78-84 16858123-3 2006 Of six cDNA-expressed rat P450 isoforms tested, CYP3A2 and CYP2C11 had high rates for N-debutlylation and 3"-hydroxylation of bupivacaine, respectively. Bupivacaine 126-137 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 48-54 16423372-8 2006 Pretreatment with telithromycin significantly decreased the activity of 7-ethoxyresorufin O-deethylation and testosterone 6 beta-hydroxylation, suggesting that telithromycin decreases the activity of hepatic CYP1A2 and CYP3A2. telithromycin 18-31 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 219-225 16423372-8 2006 Pretreatment with telithromycin significantly decreased the activity of 7-ethoxyresorufin O-deethylation and testosterone 6 beta-hydroxylation, suggesting that telithromycin decreases the activity of hepatic CYP1A2 and CYP3A2. telithromycin 160-173 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 219-225 16423372-9 2006 Western blot analysis revealed that telithromycin significantly decreased the protein levels of CYP1A2 and CYP3A2 in the liver, which could explain the observed decreases in the systemic clearance of theophylline and metabolic clearance of 1-methyluric acid and 1,3-dimethyluric acid. telithromycin 36-49 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 107-113 16423372-9 2006 Western blot analysis revealed that telithromycin significantly decreased the protein levels of CYP1A2 and CYP3A2 in the liver, which could explain the observed decreases in the systemic clearance of theophylline and metabolic clearance of 1-methyluric acid and 1,3-dimethyluric acid. Theophylline 200-212 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 107-113 16423372-9 2006 Western blot analysis revealed that telithromycin significantly decreased the protein levels of CYP1A2 and CYP3A2 in the liver, which could explain the observed decreases in the systemic clearance of theophylline and metabolic clearance of 1-methyluric acid and 1,3-dimethyluric acid. 1-methyluric acid 240-257 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 107-113 16423372-9 2006 Western blot analysis revealed that telithromycin significantly decreased the protein levels of CYP1A2 and CYP3A2 in the liver, which could explain the observed decreases in the systemic clearance of theophylline and metabolic clearance of 1-methyluric acid and 1,3-dimethyluric acid. 1,3-dimethyluric acid 262-283 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 107-113 16423372-10 2006 The present study suggests that telithromycin at the dose used in this study alters the pharmacokinetics and metabolism of theophylline, due to reductions in the activity and expression of hepatic CYP1A2 and CYP3A2. telithromycin 32-45 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 208-214 16423372-10 2006 The present study suggests that telithromycin at the dose used in this study alters the pharmacokinetics and metabolism of theophylline, due to reductions in the activity and expression of hepatic CYP1A2 and CYP3A2. Theophylline 123-135 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 208-214 15946133-8 2005 CYP1A1/2, CYP2B1, CYP3A2, CYP4A1, and CYP2E1 were induced by the addition of 3-methylcholanthrene, phenobarbital, pregnenolone-16alpha-carbonitrile, clofibric acid, and ethanol, respectively. Methylcholanthrene 77-97 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 18-24 16626521-9 2006 CYP2C7, CYP2D1 and CYP3A2 might contribute to PTS metabolism in the rat liver. 4-toluenesulfonamide 46-49 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 19-25 16400709-3 2006 It was reported that the metabolism of DA-8159 and the formation of DA-8164 (a metabolite of DA-8159) were mainly mediated via CYP3A1/2 in rats, and amlodipine significantly inhibited the CYP3A2 in rats. udenafil 39-46 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 188-194 16400709-3 2006 It was reported that the metabolism of DA-8159 and the formation of DA-8164 (a metabolite of DA-8159) were mainly mediated via CYP3A1/2 in rats, and amlodipine significantly inhibited the CYP3A2 in rats. DA-8164 68-75 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 188-194 16400709-3 2006 It was reported that the metabolism of DA-8159 and the formation of DA-8164 (a metabolite of DA-8159) were mainly mediated via CYP3A1/2 in rats, and amlodipine significantly inhibited the CYP3A2 in rats. udenafil 93-100 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 188-194 16400709-3 2006 It was reported that the metabolism of DA-8159 and the formation of DA-8164 (a metabolite of DA-8159) were mainly mediated via CYP3A1/2 in rats, and amlodipine significantly inhibited the CYP3A2 in rats. Amlodipine 149-159 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 188-194 16536909-7 2006 Moreover, we suggest that CYP2C11 and CYP3A2 are key players in the metabolism to cotinine of nicotine in rat LMECs using the respective enzyme inhibitors (tranylcypromine and troleandomycine). Cotinine 82-90 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 38-44 16536909-7 2006 Moreover, we suggest that CYP2C11 and CYP3A2 are key players in the metabolism to cotinine of nicotine in rat LMECs using the respective enzyme inhibitors (tranylcypromine and troleandomycine). Nicotine 94-102 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 38-44 16536909-7 2006 Moreover, we suggest that CYP2C11 and CYP3A2 are key players in the metabolism to cotinine of nicotine in rat LMECs using the respective enzyme inhibitors (tranylcypromine and troleandomycine). Tranylcypromine 156-171 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 38-44 16536909-7 2006 Moreover, we suggest that CYP2C11 and CYP3A2 are key players in the metabolism to cotinine of nicotine in rat LMECs using the respective enzyme inhibitors (tranylcypromine and troleandomycine). Troleandomycin 176-191 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 38-44 16125735-3 2005 The substrates used in this study were tolbutamide (CYP2C6), dextromethorphan (CYP2D2) and midazolam (CYP3A2). Midazolam 91-100 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 102-108 16316929-8 2005 In incubations with pooled rat liver microsomes and recombinant rat CYP3A1 and CYP3A2, troleandomycin (TAO) reduced the formation of GSH conjugates M2-4 by 80-90%, but it had no effect on the formation of M1. Troleandomycin 87-101 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 79-85 16316929-8 2005 In incubations with pooled rat liver microsomes and recombinant rat CYP3A1 and CYP3A2, troleandomycin (TAO) reduced the formation of GSH conjugates M2-4 by 80-90%, but it had no effect on the formation of M1. Glutathione 133-136 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 79-85 15988118-0 2005 Prediction of theophylline clearance in CCl4-treated rats using in vivo CYP1A2 and CYP3A2 contents assessed with the PKCYP test. Theophylline 14-26 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 83-89 15988118-2 2005 Here we show that the amount of CYP3A2 in CCl(4)-treated rats can be estimated appropriately by applying the PKCYP test using midazolam (MDZ) as a probe, assuming that the qg value in control rats does not change. Carbon Tetrachloride 42-48 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 32-38 15988118-2 2005 Here we show that the amount of CYP3A2 in CCl(4)-treated rats can be estimated appropriately by applying the PKCYP test using midazolam (MDZ) as a probe, assuming that the qg value in control rats does not change. Midazolam 126-135 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 32-38 15988118-2 2005 Here we show that the amount of CYP3A2 in CCl(4)-treated rats can be estimated appropriately by applying the PKCYP test using midazolam (MDZ) as a probe, assuming that the qg value in control rats does not change. Midazolam 137-140 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 32-38 15988118-5 2005 The qg value of MDZ was determined in control rats and used to estimate the amounts of CYP3A2 in CCl4-treated rats; the result agreed well with the observed values. Midazolam 16-19 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 87-93 15988118-6 2005 The qg value of CYP3A2 estimated with MDZ as a probe was used together with our previously reported value for CYP1A2 (theophylline metabolism in the liver is known to be almost entirely mediated by CYP3A2 and CYP1A2) to predict the total body clearance (CL(tot)) of theophylline in CCl4-treated rats. Midazolam 38-41 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 16-22 15988118-6 2005 The qg value of CYP3A2 estimated with MDZ as a probe was used together with our previously reported value for CYP1A2 (theophylline metabolism in the liver is known to be almost entirely mediated by CYP3A2 and CYP1A2) to predict the total body clearance (CL(tot)) of theophylline in CCl4-treated rats. Theophylline 118-130 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 16-22 15988118-6 2005 The qg value of CYP3A2 estimated with MDZ as a probe was used together with our previously reported value for CYP1A2 (theophylline metabolism in the liver is known to be almost entirely mediated by CYP3A2 and CYP1A2) to predict the total body clearance (CL(tot)) of theophylline in CCl4-treated rats. Theophylline 118-130 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 198-204 15988118-6 2005 The qg value of CYP3A2 estimated with MDZ as a probe was used together with our previously reported value for CYP1A2 (theophylline metabolism in the liver is known to be almost entirely mediated by CYP3A2 and CYP1A2) to predict the total body clearance (CL(tot)) of theophylline in CCl4-treated rats. Theophylline 266-278 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 16-22 15988118-6 2005 The qg value of CYP3A2 estimated with MDZ as a probe was used together with our previously reported value for CYP1A2 (theophylline metabolism in the liver is known to be almost entirely mediated by CYP3A2 and CYP1A2) to predict the total body clearance (CL(tot)) of theophylline in CCl4-treated rats. Theophylline 266-278 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 198-204 15988118-9 2005 Thus, the PKCYP test using MDZ as a probe can be used to predict the amount of CYP3A2 and the CL(tot) of theophylline in CCl4-treated rats. Midazolam 27-30 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 79-85 16329150-0 2006 Reduction in tamoxifen-induced CYP3A2 expression and DNA adducts using antisense technology. Tamoxifen 13-22 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 31-37 16329150-5 2006 The specific activity of CYP3A2 was increased after TAM administration, and decreased significantly (approximately 70%) in the presence of 12.5 mg AVI-4472. Tamoxifen 52-55 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 25-31 15946133-8 2005 CYP1A1/2, CYP2B1, CYP3A2, CYP4A1, and CYP2E1 were induced by the addition of 3-methylcholanthrene, phenobarbital, pregnenolone-16alpha-carbonitrile, clofibric acid, and ethanol, respectively. Phenobarbital 99-112 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 18-24 15946133-8 2005 CYP1A1/2, CYP2B1, CYP3A2, CYP4A1, and CYP2E1 were induced by the addition of 3-methylcholanthrene, phenobarbital, pregnenolone-16alpha-carbonitrile, clofibric acid, and ethanol, respectively. Pregnenolone Carbonitrile 114-147 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 18-24 15946133-8 2005 CYP1A1/2, CYP2B1, CYP3A2, CYP4A1, and CYP2E1 were induced by the addition of 3-methylcholanthrene, phenobarbital, pregnenolone-16alpha-carbonitrile, clofibric acid, and ethanol, respectively. Clofibric Acid 149-163 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 18-24 15946133-8 2005 CYP1A1/2, CYP2B1, CYP3A2, CYP4A1, and CYP2E1 were induced by the addition of 3-methylcholanthrene, phenobarbital, pregnenolone-16alpha-carbonitrile, clofibric acid, and ethanol, respectively. Ethanol 169-176 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 18-24 15788368-4 2005 Treatment of male Wistar rats with a PPARalpha ligand clofibric acid (CA) induced CYP2B1/2 and CYP3A proteins, activities, and the mRNA expression of CYP2B1, CYP2B2, CYP3A1 and CYP3A2, and suppressed CYP2C11 protein, activities and mRNA expression. Clofibric Acid 54-68 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 177-183 15799453-8 2005 The amounts of MB2, MB4, and MC formed by male and female rat liver microsome preparations were related to the testosterone 6beta-hydroxylase activity and CYP3A1/2 protein content of the preparation. Methylcholanthrene 29-31 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 111-141 15799453-10 2005 These results suggest that the formation of MB2, MB4, and MC in liver microsomes from 14-wk-old rats of either gender is mediated by CYP3A1 and CYP3A2. Methylcholanthrene 58-60 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 144-150 15588932-9 2005 PB enhanced CYP2B1 and 3A2 expression, and DEX and PCN increased CYP3A2 immunostaining. Dexamethasone 43-46 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 65-71 15588932-9 2005 PB enhanced CYP2B1 and 3A2 expression, and DEX and PCN increased CYP3A2 immunostaining. Pregnenolone Carbonitrile 51-54 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 65-71 15783070-4 2005 Testosterone 6beta-hydroxylase activity, which is a marker of CYP3A activity, was measured in rat liver microsomes from CCl4-treated or 5/6 Nx rats. Carbon Tetrachloride 120-124 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 0-30 15783070-6 2005 Testosterone 6beta-hydroxylase activity was reduced by 92% and 59% relative to each control value in rat liver microsomes from CCl4-treated and 5/6 Nx rats, respectively. Carbon Tetrachloride 127-131 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 0-30 16421897-8 2005 Notably, phenobarbital resulted in significant induction of CYP2B1, CYP2B2, CYP2C6, CYP2C13, CYP2E1, CYP3A1, and CYP3A2. Phenobarbital 9-22 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 113-119 15349958-3 2004 The present study investigated the effect of dexamethasone (Dex) on gene expression on both message and protein levels of mdr1a, mdr1b, CYP3A1, and CYP3A2 in small intestine, colon, liver, kidney, and brain microvessels of the rats treated orally with Dex at 1 or 20 mg/kg/day for 3 days. Dexamethasone 45-58 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 148-154 15570024-5 2004 DEX induced CYP3A1, CYP3A2, and CYP3A9 (P < 0.05), but not CYP3A18 mRNA expression in rats fed both diets. Dexamethasone 0-3 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 20-26 15349958-3 2004 The present study investigated the effect of dexamethasone (Dex) on gene expression on both message and protein levels of mdr1a, mdr1b, CYP3A1, and CYP3A2 in small intestine, colon, liver, kidney, and brain microvessels of the rats treated orally with Dex at 1 or 20 mg/kg/day for 3 days. Dexamethasone 60-63 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 148-154 15364003-0 2004 Effect of pioglitazone on endotoxin-induced decreases in hepatic drug-metabolizing enzyme activity and expression of CYP3A2 and CYP2C11. Pioglitazone 10-22 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 117-123 15364003-2 2004 In the present study, we investigated the effect of pioglitazone, a potent PPAR-gamma ligand, on the endotoxin-induced reduction of hepatic drug-metabolizing enzyme activity and on the down-regulation of the expression of hepatic cytochrome P450 (CYP) 3A2 and CYP2C11 proteins in rats. Pioglitazone 52-64 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 230-255 15364003-7 2004 It is unlikely that the protective effect of pioglitazone against endotoxin-induced decreases in the hepatic drug-metabolizing enzyme activity and protein levels of CYP3A2 in the liver is due to the inhibition of the overproduction of NO. Pioglitazone 45-57 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 165-171 15364003-4 2004 Pretreatment with pioglitazone (10 mg/kg, 4 times at 10-min intervals) significantly protected the endotoxin-induced decreases in the systemic clearance of antipyrine and protein levels of CYP3A2, but not CYP2C11, with no biochemical and histopathological changes in the liver. Pioglitazone 18-30 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 189-195 14757125-3 2004 CYP isoenzyme dependences were studied using specific chemical inhibitors for CYP1A2, CYP2D1, and CYP3A2 (alpha-naphthoflavone, quinine, and ketoconazole, respectively). alpha-naphthoflavone 106-126 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 98-104 15319337-7 2004 In agreement with this, DA rat liver microsomes had a higher expression of CYP3A2, which is responsible for diazepam 3-hydroxylation and partly responsible for N-desmethylation. Diazepam 108-116 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 75-81 15288127-3 2004 PB significantly increased P450 levels (200% of control levels) and the activities (300-400% of control) of the specific isoforms (CYP), CYP3A2 and CYP2B1, in male rats. Phenobarbital 0-2 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 137-143 15050404-7 2004 Thus, changes in levels of the mRNA or protein of CYP2B and CYP3A enzymes, especially CYP2B1 and CYP3A2, were closely correlated with those in hepatic PROD and nifedipine oxidation activities, respectively. Nifedipine 160-170 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 97-103 14757125-5 2004 Californine N-demethylation was mainly catalyzed by CYP3A2 and to a minor extent by CYP1A2 and CYP2D1, but not by CYP2C11. californine n 0-13 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 52-58 14757125-6 2004 CYP2D1 and CYP2C11 were shown to be mainly involved in demethylenation of both, californine and protopine, while CYP1A2 and CYP3A2 showed only minor contribution. californine 80-91 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 124-130 14757125-6 2004 CYP2D1 and CYP2C11 were shown to be mainly involved in demethylenation of both, californine and protopine, while CYP1A2 and CYP3A2 showed only minor contribution. protopine 96-105 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 124-130 14706259-3 2004 Good correlations were observed between mRNA expression and enzyme activity of CYP2C11, CYP2E1, CYP3A2 and CYP1A2 in livers of rats given various doses of CCl(4). Cefaclor 155-158 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 96-102 12920173-2 2003 In primary cultures of hepatocytes, DPC 681 significantly induced the testosterone 6beta-hydroxylase activity of rat CYP3A, but not human CYP3A4. dpc 36-39 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 70-100 14557382-4 2003 Injection of curcumin significantly inhibited the rapid transcriptional suppression of CYP2E1, and blocked that of CYP3A2. Curcumin 13-21 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 115-121 12623755-7 2003 We have demonstrated for the first time that nicardipine activated not only the genes of CYP2B1, CYP2B2, CYP3A1 and CYP3A2, but also those of CYP1A1 and CYP1A2 in the rat liver and have further suggested that calcium channel antagonists may show a common capacity for activating the genes of CYP2B1, CYP2B2, CYP3A1 and CYP3A2. Nicardipine 45-56 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 319-325 12807726-11 2003 On the contrary, when PB was applied at a high dose, GST-P positive foci numbers and areas, tumor multiplicity, hydroxyl radicals and 8-OHdG levels were greatly elevated with the increase in CYP2B1/2 and CYP3A2 mRNA, protein, activity and gene expression of GST, nuclear tyrosine phosphatase, NADPH- cytochrome P-450 reductase and guanine nucleotide binding protein G(O) alpha subunit. Phenobarbital 22-24 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 204-210 12867494-7 2003 In the rat, recombinant CYP2C11, CYP2B1, and CYP3A2 catalyzed (-)-verbenone 10-hydroxylation with Vmax and Km ratios (ml/min/nmol p450) of 0.73, 0.20, and 0.03, respectively. verbenone 62-75 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 45-51 12837975-5 2003 The expression of the other isoforms was significantly elevated by both doses of phenobarbital (10 mg >1 mg), though CYP2C6, CYP3A1, and CYP3A2 levels were increased an additional 30-50% when the animals were neonatally exposed to the barbiturate, demonstrating for the first time that mechanisms regulating induction of constitutive CYPs in adults are imprintable at birth. Phenobarbital 81-94 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 140-146 12746107-7 2003 Treatment with ARO produced 22 600-, 5480-, 648-, 52-, 47- and 9-fold increases in levels of CYP1A1, CYP2B1, CYP2B1/2, CYP1A2, CYP3A1 and CYP3A2 mRNA, respectively. Chlorodiphenyl (54% Chlorine) 15-18 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 138-144 12746107-8 2003 DEX treatment produced 97-, 24-, 8- and 4-fold increases, respectively, in CYP3A1, CYP2B1, CYP2B1/2 and CYP3A2 mRNA levels, and MCP produced 339-, 126- and 25-fold increases, respectively, in CYP4A1, CYP2B1 and CYP2B1/2 mRNA levels. Dexamethasone 0-3 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 104-110 12746107-21 2003 PCN also produced 56- and 4-fold increases, respectively, in CYP3A1 and CYP3A2 mRNA levels. Pregnenolone Carbonitrile 0-3 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 72-78 12623755-5 2003 Other calcium channel antagonists, nifedipine, diltiazem and verapamil, also enhanced the gene expression of CYP2B1, CYP2B2, CYP3A1 and CYP3A2, although these showed no capacity for activating CYP1A1 and CYP1A2 genes. Nifedipine 35-45 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 136-142 12623755-5 2003 Other calcium channel antagonists, nifedipine, diltiazem and verapamil, also enhanced the gene expression of CYP2B1, CYP2B2, CYP3A1 and CYP3A2, although these showed no capacity for activating CYP1A1 and CYP1A2 genes. Diltiazem 47-56 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 136-142 12623755-5 2003 Other calcium channel antagonists, nifedipine, diltiazem and verapamil, also enhanced the gene expression of CYP2B1, CYP2B2, CYP3A1 and CYP3A2, although these showed no capacity for activating CYP1A1 and CYP1A2 genes. Verapamil 61-70 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 136-142 12623755-7 2003 We have demonstrated for the first time that nicardipine activated not only the genes of CYP2B1, CYP2B2, CYP3A1 and CYP3A2, but also those of CYP1A1 and CYP1A2 in the rat liver and have further suggested that calcium channel antagonists may show a common capacity for activating the genes of CYP2B1, CYP2B2, CYP3A1 and CYP3A2. Nicardipine 45-56 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 116-122 12906334-0 2003 Effect of sodium alterations on hepatic cytochrome P450 3A2 and 2C11 and renal function in rats. Sodium 10-16 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 40-68 12756212-8 2003 Based on results from supporting experiments with DDT and 2,2-bis(4-chlorophenyl)1,1-dichloroethylene treatment of rats, the contribution of CYP3A23 and CYP3A2 to the enhanced formation of OH-CZX in rats with U-ARF is likely to be negligible. oh-czx 189-195 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 141-147 12712632-5 2003 An immunoinhibition study showed that anti-CYP3A2 antibody reduced MA1 formation to nondetectable levels in liver microsomes from PB-treated female rats. Phenobarbital 130-132 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 43-49 12926555-8 2003 The observed changes indicate an impairment of N-deethylation, i.e. a possible decrease in enzymatic activity of CYP3A2 and CYP1A2, which are the major enzymes catalyzing this reaction. Nitrogen 47-48 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 113-119 12487727-11 2002 CYP3A1 and CYP3A2 protein levels in liver microsomes were significantly increased following oral (3.7- and 3.2-fold, respectively) or intravenous (2.6- and 2.1-fold, respectively) pretreatment with dexamethasone. Dexamethasone 198-211 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 11-17 12515593-6 2002 SKF 525A, which inhibits CYP2B, CYP2C11, and CYP3A2, and orphenadrine, which inhibits CYP2B, also decreased MA(2) formation in liver microsomes from 7-wk-old phenobarbital-pretreated rats. Proadifen 0-8 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 45-51 12515593-8 2002 Furthermore, an immunoinhibition study demonstrated that anti-CYP3A2 antibody reduced MA(1), MAX, and MA(2) formation to nondetectable levels in liver microsomes from 2- and 7-wk-old rats, whereas anti-CYP2C11 or anti-CYP2B antibody, respectively, had no marked effect on MA(1), MAX, and MA(2) formation in liver microsomes from 7-wk-old untreated or PB-treated rats. Phenobarbital 351-353 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 62-68 12423659-9 2002 Phenobarbital caused an enhanced CYP2B1 and 3A2 and dexamethasone and pregnenolone 16 alpha-carbonitrile an increased CYP3A2 immunostaining. Phenobarbital 0-13 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 118-124 12487727-12 2002 On the contrary, only oral dexamethasone pretreatment resulted in a significant change in intestinal CYP3A2-like protein (7.3-fold). Dexamethasone 27-40 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 101-107 11948501-9 2002 Furthermore, since CYP3A2 protein expression appears to be important for the effects of phenobarbital and the alpha-isomer of benzene hexachloride, mRNAs for IL-1 receptor type 1 (IL-1R1) and TNF-alpha receptor type 1 (TNFR1) whose ligands have roles not only in downregulating CYP3A2 expression but also in inducing antiproliferative effect or apoptosis in hepatocyte were examined. Phenobarbital 88-101 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 19-25 12425463-0 2002 Transdermal use of phosphorodiamidate morpholino oligomer AVI-4472 inhibits cytochrome P450 3A2 activity in male rats. phosphorodiamidate morpholino 19-48 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 76-95 12231541-5 2002 Rat and human microsomal metabolism of ET743 was reduced in the presence of chemical CYP3A inhibitors or antirat CYP3A2 antiserum and to a much lesser extent by CYP2E, CYP2C, and CYP2A inhibitors. Trabectedin 39-44 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 113-119 12231541-7 2002 ET743 was metabolized by a number of cDNA-expressed rat P-450 isoforms, including male-predominant CYP2A2 and CYP3A2. Trabectedin 0-5 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 110-116 12167482-9 2002 These results suggest that: (1) CYP3A1 protein is constitutive and largely expressed in rat liver slices; (2) regioselective midazolam oxidation appears to be mainly CYP3A2 dependent; and (3) since CYP3A isoforms have similar half-lives (about 10-14hr), the loss of CYP3A2 protein at 37 degrees might be due to a selective targeting (phosphorylation ?) Midazolam 125-134 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 166-172 12167482-6 2002 By blocking transcription with actinomycin D, the decay of both CYP3A mRNAs followed the same profile at either 20 or 37 degrees, indicating that temperature affected the CYP3A2 protein stability. Dactinomycin 31-44 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 171-177 12167482-8 2002 The use of rat supersomes expressing either CYP3A1 or CYP3A2, strongly supported the hypothesis that 4-hydroxymidazolam was mainly formed by CYP3A2. 4-hydroxymidazolam 101-119 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 54-60 12167482-8 2002 The use of rat supersomes expressing either CYP3A1 or CYP3A2, strongly supported the hypothesis that 4-hydroxymidazolam was mainly formed by CYP3A2. 4-hydroxymidazolam 101-119 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 141-147 12130706-0 2002 Prevention of latently expressed CYP2C11, CYP3A2, and growth hormone defects in neonatally monosodium glutamate-treated male rats by the N-methyl-D-aspartate receptor antagonist dizocilpine maleate. Dizocilpine Maleate 178-197 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 42-48 11948501-9 2002 Furthermore, since CYP3A2 protein expression appears to be important for the effects of phenobarbital and the alpha-isomer of benzene hexachloride, mRNAs for IL-1 receptor type 1 (IL-1R1) and TNF-alpha receptor type 1 (TNFR1) whose ligands have roles not only in downregulating CYP3A2 expression but also in inducing antiproliferative effect or apoptosis in hepatocyte were examined. Phenobarbital 88-101 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 278-284 11948501-9 2002 Furthermore, since CYP3A2 protein expression appears to be important for the effects of phenobarbital and the alpha-isomer of benzene hexachloride, mRNAs for IL-1 receptor type 1 (IL-1R1) and TNF-alpha receptor type 1 (TNFR1) whose ligands have roles not only in downregulating CYP3A2 expression but also in inducing antiproliferative effect or apoptosis in hepatocyte were examined. Hexachlorocyclohexane 126-146 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 19-25 12269382-9 2002 The feeding of GBE for 4 weeks significantly reduced the hypotensive effect of nicardipine that was reported to be metabolized by CYP3A2 in rats. Nicardipine 79-90 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 130-136 11948540-6 2002 The CYP3A2 antisense 22-mer AVI-4472 (5"-GAGCTGAAAGCAGGTCCATCCC-3") caused a sequence-dependent reduction of approximately five-fold in the rat liver CYP3A2 protein levels and erythromycin demethylation activity in 24 h following oral administration at a dose of 2 mg/kg. Erythromycin 176-188 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 4-10 11948540-7 2002 It is concluded that oral administration of PMOs can inhibit c-myc and CYP3A2 gene expression in rat liver by an antisense-based mechanism of action. pmos 44-48 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 71-77 12028663-7 2002 The major phenobarbital (PB)-inducible forms of P450, CYP2B1, CYP2B2, CYP3A2 and CYP2C6, were substantially induced by 3-MeSO(2)-TetraBrB, but CYP1A1 and CYP1A2 were not. Phenobarbital 10-23 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 70-76 12028663-7 2002 The major phenobarbital (PB)-inducible forms of P450, CYP2B1, CYP2B2, CYP3A2 and CYP2C6, were substantially induced by 3-MeSO(2)-TetraBrB, but CYP1A1 and CYP1A2 were not. Phenobarbital 25-27 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 70-76 12028663-7 2002 The major phenobarbital (PB)-inducible forms of P450, CYP2B1, CYP2B2, CYP3A2 and CYP2C6, were substantially induced by 3-MeSO(2)-TetraBrB, but CYP1A1 and CYP1A2 were not. 3-meso(2)-tetrabrb 119-137 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 70-76 11895865-5 2002 On the other hand, the gene expression of CYP3A2 and flavin-containing monooxygenase 1 (FMO1), responsible for the N-demethylation and N-oxidation, respectively, of tamoxifen was increased in a time-dependent fashion up to the 52 week treatment. Tamoxifen 165-174 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 42-48 11895865-7 2002 The present findings demonstrate that in the early stage of the formation of the liver hyperplastic nodules by tamoxifen, the genes of the enzymes responsible for not only detoxification but also activation of tamoxifen were activated, whereas in the later stage (in the nodules), the genes of the detoxification enzymes, CYP3A2 and FMO1, remained active, but those of the activation enzymes such as CYP3A1 and HSTa were suppressed. Tamoxifen 111-120 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 322-328 11895865-7 2002 The present findings demonstrate that in the early stage of the formation of the liver hyperplastic nodules by tamoxifen, the genes of the enzymes responsible for not only detoxification but also activation of tamoxifen were activated, whereas in the later stage (in the nodules), the genes of the detoxification enzymes, CYP3A2 and FMO1, remained active, but those of the activation enzymes such as CYP3A1 and HSTa were suppressed. Tamoxifen 210-219 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 322-328 11875010-5 2002 RESULTS: The preincubation of microsomes with indomethacin and reduced nicotinamide adenine dinucleotide phosphate decreased CYP3A2 activity but not any other isoforms. Indomethacin 46-58 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 125-131 11875010-5 2002 RESULTS: The preincubation of microsomes with indomethacin and reduced nicotinamide adenine dinucleotide phosphate decreased CYP3A2 activity but not any other isoforms. NADP 71-114 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 125-131 11875010-8 2002 Administration of indomethacin caused impairment of not only CYP3A2 but also other CYP isoforms. Indomethacin 18-30 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 61-67 11875010-10 2002 CONCLUSIONS: Metabolism of indomethacin causes inactivation of CYP3A2, which is the result of the covalent binding of its metabolite, whereas partially selective in vivo impairment of CYP isoforms is suggested to be indirect inhibition by inflammatory mediators probably released from Kupffer cells. Indomethacin 27-39 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 63-69 15618710-8 2002 It was also found in intestinal microsomes that anti-rat CYP3A2 antibody can inhibit nifedipine metabolism completely. Nifedipine 85-95 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 57-63 11992648-15 2002 Our results indicate that the drug interaction between CyA and DEX is a consequence of modulation of P-gp and CYP3A2 gene expression by DEX, with differential dose-dependence. Cyclosporine 55-58 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 110-116 11992648-15 2002 Our results indicate that the drug interaction between CyA and DEX is a consequence of modulation of P-gp and CYP3A2 gene expression by DEX, with differential dose-dependence. Dexamethasone 63-66 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 110-116 11992648-15 2002 Our results indicate that the drug interaction between CyA and DEX is a consequence of modulation of P-gp and CYP3A2 gene expression by DEX, with differential dose-dependence. Dexamethasone 136-139 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 110-116 15618669-0 2002 Simultaneous assessment of the in vivo amount of CYP1A2 and CYP3A2 by the PKCYP-test using theophylline in rats. Theophylline 91-103 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 60-66 11872643-2 2002 Significant increase of hydroxyl radical levels by day 4 of PB exposure accompanied the accumulation of 8-OHdG in the nucleus and P-450 isoenzymes CYP2B1/2 and CYP3A2 in the cytoplasm of hepatocytes. Hydroxyl Radical 24-40 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 160-166 11872643-2 2002 Significant increase of hydroxyl radical levels by day 4 of PB exposure accompanied the accumulation of 8-OHdG in the nucleus and P-450 isoenzymes CYP2B1/2 and CYP3A2 in the cytoplasm of hepatocytes. Phenobarbital 60-62 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 160-166 11824557-5 2002 Immunoblot analyses revealed that climbazole induces CYP2B1 and CYP3A2 at the lower dose examined, but it failed to increase CYP2B1 at the higher dose. climbazole 34-44 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 64-70 15618678-8 2002 Correspondingly, the content of CYP3A2 was significantly altered by single or repeated itraconazole administration. Itraconazole 87-99 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 32-38 15618710-9 2002 Thus, the present study demonstrates that nifedipine undergoes significant extraction during passage through the intestinal mucosa, and provides substantial evidence that CYP3A2 is responsible for that. Nifedipine 42-52 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 171-177 11780761-12 2001 3TFBFC was a relatively specific substrate for cDNA-expressed CYP2B1, whereas 2TFBFC could be metabolized by CYP2B1, CYP3A1 and CYP3A2. 2tfbfc 78-84 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 128-134 11780761-17 2001 7BQ was a substrate for cDNA-expressed CYP3A2 and to a lesser extent for CYP3A1. 7-benzyloxyquinoline 0-3 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 39-45 11985335-9 2001 The isoenzymes CYP1A2 and CYP3A2 were distinctly inhibited by all the investigated neuroleptics, while other CYP isoenzymes (CYP2B and/or 2E1) by perazine and levomepromazine. Perazine 146-154 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 26-32 11760817-9 2001 For the activities of testosterone hydroxylation, testosterone 16beta-hydroxylase (T16BH) activity was markedly increased by 30-fold, and testosterone 6beta-hydroxylase (T6BH) and testosterone 7alpha-hydroxylase (T7AH) activities were slightly elevated. Testosterone 22-34 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 138-168 11985335-9 2001 The isoenzymes CYP1A2 and CYP3A2 were distinctly inhibited by all the investigated neuroleptics, while other CYP isoenzymes (CYP2B and/or 2E1) by perazine and levomepromazine. Methotrimeprazine 159-174 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 26-32 11488450-6 2001 On the other hand, the extract had no effects on the formation of AFBO and AFQ1 in human liver microsomes, and on the activities of CYP2B1, CYP2C11 and CYP3A1/2 which were detected by hydroxylation patterns of testosterone. Testosterone 210-222 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 152-160 11561777-2 2001 The metabolism of docetaxel to its primary metabolite, hydroxydocetaxel, is mediated by cytochrome P450 isozymes CYP3A2 and CYP3A4 in rats and humans, respectively. Docetaxel 18-27 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 113-119 11561777-2 2001 The metabolism of docetaxel to its primary metabolite, hydroxydocetaxel, is mediated by cytochrome P450 isozymes CYP3A2 and CYP3A4 in rats and humans, respectively. hydroxydocetaxel 55-71 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 113-119 11346484-4 2001 In rat primary hepatocytes, C + K reduced the expression of cytochrome P450 CYP 2C11 and CYP 3A2, the key enzymes responsible for AFB1 activation to the genotoxic metabolite aflatoxin B1-8,9 epoxide (AFBO). Aflatoxin B1 130-134 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 89-96 11531004-0 2001 Suppression of CYP3A2 mRNA expression in the warfarin-resistant roof rat, Rattus rattus: possible involvement of cytochrome P450 in the warfarin resistance mechanism. Warfarin 45-53 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 15-21 11531004-5 2001 The constitutive levels of CYP2C11 and CYP3A2 mRNAs in the warfarin-resistant and -susceptible roof rat were extremely low compared with those in the STD rat. Warfarin 59-67 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 39-45 11531004-6 2001 In response to warfarin administration, the CYP3A2 mRNA level in the warfarin-susceptible rat increased to about 3-fold of that before the treatment, whereas in the warfarin-resistant roof rat, CYP3A2 mRNA remained at a low level. Warfarin 15-23 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 44-50 11531004-6 2001 In response to warfarin administration, the CYP3A2 mRNA level in the warfarin-susceptible rat increased to about 3-fold of that before the treatment, whereas in the warfarin-resistant roof rat, CYP3A2 mRNA remained at a low level. Warfarin 15-23 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 194-200 11531004-6 2001 In response to warfarin administration, the CYP3A2 mRNA level in the warfarin-susceptible rat increased to about 3-fold of that before the treatment, whereas in the warfarin-resistant roof rat, CYP3A2 mRNA remained at a low level. Warfarin 69-77 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 44-50 11531004-6 2001 In response to warfarin administration, the CYP3A2 mRNA level in the warfarin-susceptible rat increased to about 3-fold of that before the treatment, whereas in the warfarin-resistant roof rat, CYP3A2 mRNA remained at a low level. Warfarin 69-77 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 44-50 11531004-8 2001 The present results suggest the possibility that reduced synthesis of CYP3A2 mRNA is involved in the warfarin-resistant mechanism in the roof rat. Warfarin 101-109 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 70-76 11435969-9 2001 CsA alone suppressed cytochrome P450 (CYP) 3A2 protein levels by 39% (P=0.012) and catalytic activity by 30% (P=0.042). Cyclosporine 0-3 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 21-46 11346484-4 2001 In rat primary hepatocytes, C + K reduced the expression of cytochrome P450 CYP 2C11 and CYP 3A2, the key enzymes responsible for AFB1 activation to the genotoxic metabolite aflatoxin B1-8,9 epoxide (AFBO). aflatoxin B1-2,3-oxide 174-198 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 89-96 11258617-10 2001 Midozolam-treated animals with antisense to CYP3A2 slept significantly longer than did the controls (p < 0.05). midozolam 0-9 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 44-50 11295255-10 2001 At the same sites, phenobarbital led to an increased CYP 2B1 and 3A2 expression and dexamethasone to an elevated CYP 3A2 immunostaining. Dexamethasone 84-97 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 113-120 10995741-2 2001 In the male, these steroids are primarily metabolized into two oxidized (16alpha-hydroxyl and 6beta-hydroxyl) products mainly by the respective, male-specific cytochrome P450 subforms, CYP2C11 and CYP3A2, while they are primarily metabolized into the 5alpha-reduced products by female-predominant 5alpha-reductase in the female. Steroids 19-27 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 197-203 10995741-2 2001 In the male, these steroids are primarily metabolized into two oxidized (16alpha-hydroxyl and 6beta-hydroxyl) products mainly by the respective, male-specific cytochrome P450 subforms, CYP2C11 and CYP3A2, while they are primarily metabolized into the 5alpha-reduced products by female-predominant 5alpha-reductase in the female. 16alpha-hydroxyl 73-89 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 197-203 10995741-2 2001 In the male, these steroids are primarily metabolized into two oxidized (16alpha-hydroxyl and 6beta-hydroxyl) products mainly by the respective, male-specific cytochrome P450 subforms, CYP2C11 and CYP3A2, while they are primarily metabolized into the 5alpha-reduced products by female-predominant 5alpha-reductase in the female. 6beta-hydroxyl 94-108 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 197-203 11258617-6 2001 A C5 propyne-modified phosphorothioate oligonucleotide (PS-ODN) targeted to the cytochrome p450-3A2 (CYP3A2) mRNA translational start site and the reverse sequence, used as a control, were synthesized. methylacetylene 5-12 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 80-99 11038159-6 2000 In vivo cytochrome P450 activity was evaluated with breath tests using substrates for different isoenzymes: caffeine (CYP1A2), aminopyrine (CYP2C11), and erythromycin (CYP3A2). Erythromycin 154-166 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 168-174 11258617-6 2001 A C5 propyne-modified phosphorothioate oligonucleotide (PS-ODN) targeted to the cytochrome p450-3A2 (CYP3A2) mRNA translational start site and the reverse sequence, used as a control, were synthesized. methylacetylene 5-12 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 101-107 11258617-6 2001 A C5 propyne-modified phosphorothioate oligonucleotide (PS-ODN) targeted to the cytochrome p450-3A2 (CYP3A2) mRNA translational start site and the reverse sequence, used as a control, were synthesized. Phosphorothioate Oligonucleotides 22-54 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 80-99 11258617-6 2001 A C5 propyne-modified phosphorothioate oligonucleotide (PS-ODN) targeted to the cytochrome p450-3A2 (CYP3A2) mRNA translational start site and the reverse sequence, used as a control, were synthesized. Phosphorothioate Oligonucleotides 22-54 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 101-107 11258617-6 2001 A C5 propyne-modified phosphorothioate oligonucleotide (PS-ODN) targeted to the cytochrome p450-3A2 (CYP3A2) mRNA translational start site and the reverse sequence, used as a control, were synthesized. ps-odn 56-62 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 80-99 11258617-6 2001 A C5 propyne-modified phosphorothioate oligonucleotide (PS-ODN) targeted to the cytochrome p450-3A2 (CYP3A2) mRNA translational start site and the reverse sequence, used as a control, were synthesized. ps-odn 56-62 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 101-107 11641615-4 2001 CYP3A2-linked activity was evaluated in vivo with the aminopyrine breath test and in vitro by the measurement of nifedipine oxidase microsomal activity. Aminopyrine 54-65 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 0-6 11020454-9 2000 In contrast, CYP3A2, CYP3A9, and CYP3A18 mRNA levels were not affected by dexamethasone treatment, and were hardly detectable after three days of cultivation. Dexamethasone 74-87 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 13-19 11038159-11 2000 In rats with CRF, there was a 35% reduction in the aminopyrine (CYP2C11) and the erythromycin (CYP3A2) breath tests compared with control animals (P <.001). Erythromycin 81-93 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 95-101 10963059-7 2000 Immunoblot analysis revealed that 2,2"-dipyridyl ketone slightly increased CYP2E1 and CYP3A2 at low doses, but not at high dose levels. 2,2'-dipyridylketone 34-55 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 86-92 11046114-0 2000 Chronic intragastric infusion of ethanol-containing diets induces CYP3A9 while decreasing CYP3A2 in male rats. Ethanol 33-40 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 90-96 11046114-5 2000 The CYP3A2 mRNA levels decreased (P <.05) in the rats fed ethanol-containing diets by 73 to 83% compared with rats fed control diets, regardless of the CHO/fat ratio. Ethanol 61-68 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 4-10 11046114-5 2000 The CYP3A2 mRNA levels decreased (P <.05) in the rats fed ethanol-containing diets by 73 to 83% compared with rats fed control diets, regardless of the CHO/fat ratio. CAV protocol 155-158 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 4-10 11046114-8 2000 These results indicate that 1) ethanol differentially affects the expression of CYP3A gene family and this regulation appears to be modulated by dietary CHO/fat ratio; 2) the decrease in testosterone 6 beta-hydroxylase activity and CYP3A apoprotein levels are most likely due to the ethanol-induced decrease in CYP3A2 mRNA levels; and 3) CYP3A9 is induced by ethanol and is a low-affinity, high-K(m) chlorzoxazone hydroxylase. Ethanol 31-38 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 187-218 11046114-8 2000 These results indicate that 1) ethanol differentially affects the expression of CYP3A gene family and this regulation appears to be modulated by dietary CHO/fat ratio; 2) the decrease in testosterone 6 beta-hydroxylase activity and CYP3A apoprotein levels are most likely due to the ethanol-induced decrease in CYP3A2 mRNA levels; and 3) CYP3A9 is induced by ethanol and is a low-affinity, high-K(m) chlorzoxazone hydroxylase. Ethanol 31-38 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 311-317 11046114-8 2000 These results indicate that 1) ethanol differentially affects the expression of CYP3A gene family and this regulation appears to be modulated by dietary CHO/fat ratio; 2) the decrease in testosterone 6 beta-hydroxylase activity and CYP3A apoprotein levels are most likely due to the ethanol-induced decrease in CYP3A2 mRNA levels; and 3) CYP3A9 is induced by ethanol and is a low-affinity, high-K(m) chlorzoxazone hydroxylase. Ethanol 283-290 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 187-218 11046114-8 2000 These results indicate that 1) ethanol differentially affects the expression of CYP3A gene family and this regulation appears to be modulated by dietary CHO/fat ratio; 2) the decrease in testosterone 6 beta-hydroxylase activity and CYP3A apoprotein levels are most likely due to the ethanol-induced decrease in CYP3A2 mRNA levels; and 3) CYP3A9 is induced by ethanol and is a low-affinity, high-K(m) chlorzoxazone hydroxylase. Ethanol 283-290 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 187-218 10879814-8 2000 These results suggest that BPA interacts with rat hepatic CYP1A2, CYP2A2, CYP2B2, CYP2C11, CYP2D1, CYP2E1 and CYP3A2 in vitro. bisphenol A 27-30 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 110-116 10906725-7 2000 The changes in the in vitro production of 6beta- and 2alpha-hydroxytestosterone, markers of CYP3A2 and 2C11 activities, respectively, were consistent with their protein levels, although not statistically different than controls. 6beta- and 2alpha-hydroxytestosterone 42-79 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 92-107 11035197-6 2000 The combination of the iontophoretic delivery mode with potent oligonucleotides resulted in selective inhibition of the CYP3A2 gene expression in the rat liver. Oligonucleotides 63-79 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 120-126 10799341-13 2000 ROS formation in corn oil-treated rats as well as in ethylbenzene-treated rats was also inhibited with antibodies to anti-CYP2E1 and anti-CYP3A2. Reactive Oxygen Species 0-3 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 138-144 10799341-13 2000 ROS formation in corn oil-treated rats as well as in ethylbenzene-treated rats was also inhibited with antibodies to anti-CYP2E1 and anti-CYP3A2. ethylbenzene 53-65 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 138-144 10799341-14 2000 These results suggest that CYP2C11 does not appear to influence free radical production and that the increase in free radical production in EB treated rats is consistent with the EB-mediated elevation of CYP2B, CYP 2E1, and CYP3A2. ethylbenzene 140-142 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 224-230 10799341-14 2000 These results suggest that CYP2C11 does not appear to influence free radical production and that the increase in free radical production in EB treated rats is consistent with the EB-mediated elevation of CYP2B, CYP 2E1, and CYP3A2. ethylbenzene 179-181 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 224-230 11112093-5 2000 That is, CYP1A, CYP2B and CYP3A2, but not CYP2E, were observed 24 h after CLO or KET or MIC treatment. Clotrimazole 74-77 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 26-32 11112093-5 2000 That is, CYP1A, CYP2B and CYP3A2, but not CYP2E, were observed 24 h after CLO or KET or MIC treatment. Ketoconazole 81-84 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 26-32 10460791-1 1999 Cytochrome P-450 (CYP) 3A2 and CYP2C11 are sources of 70 and 30%, respectively, of N-vinylprotoporphyrin IX (N-vinylPP) formation after administration of 3-[(arylthio)ethyl]sydnone (TTMS) to rats. 21-Vinylprotoporphyrin 83-107 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 0-26 10688605-11 2000 The activity of cytochrome P-450 3A2 (CYP3A2) was evaluated by immunoblot analysis and erythromycin N-demethylation. erythromycin n 87-101 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 16-36 10688605-11 2000 The activity of cytochrome P-450 3A2 (CYP3A2) was evaluated by immunoblot analysis and erythromycin N-demethylation. erythromycin n 87-101 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 38-44 10600171-3 1999 Promoter deletion analyses revealed that the CYP3A2 -57 to -168 region, homologous to the CYP3A23 dexamethasone-responsive region, mediated its low level activation. Dexamethasone 98-111 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 45-51 10539769-5 1999 Dexamethasone significantly induced turnover of erythromycin and testosterone, expression of CYP3A apoprotein, and expression of CYP3A1 and CYP3A2 mRNA (P < 0.05). Dexamethasone 0-13 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 140-146 10704895-0 2000 Effect of dose on cyclosporine-induced suppression of hepatic cytochrome P450 3A2 and 2C11. Cyclosporine 18-30 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 62-90 10565810-6 1999 Microsomal androst-4-ene-3,17-dione hydroxylation activities mediated by CYP2C11 (16alpha-hydroxylation) and CYP3A2 (6beta-hydroxylation) were decreased in liver from OA-fed rats for only 5 days, whereas CYP2A1/2-mediated steroid 7alpha-hydroxylation was decreased after 10 days; these observations were complemented by immunoblot analysis that demonstrated the impaired expression of the corresponding CYP proteins. Androstenedione 11-35 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 109-115 10565810-6 1999 Microsomal androst-4-ene-3,17-dione hydroxylation activities mediated by CYP2C11 (16alpha-hydroxylation) and CYP3A2 (6beta-hydroxylation) were decreased in liver from OA-fed rats for only 5 days, whereas CYP2A1/2-mediated steroid 7alpha-hydroxylation was decreased after 10 days; these observations were complemented by immunoblot analysis that demonstrated the impaired expression of the corresponding CYP proteins. Steroids 222-229 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 109-115 10460791-1 1999 Cytochrome P-450 (CYP) 3A2 and CYP2C11 are sources of 70 and 30%, respectively, of N-vinylprotoporphyrin IX (N-vinylPP) formation after administration of 3-[(arylthio)ethyl]sydnone (TTMS) to rats. n-vinylpp 109-118 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 0-26 10460791-1 1999 Cytochrome P-450 (CYP) 3A2 and CYP2C11 are sources of 70 and 30%, respectively, of N-vinylprotoporphyrin IX (N-vinylPP) formation after administration of 3-[(arylthio)ethyl]sydnone (TTMS) to rats. 3-[(arylthio)ethyl]sydnone 154-180 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 0-26 10460791-1 1999 Cytochrome P-450 (CYP) 3A2 and CYP2C11 are sources of 70 and 30%, respectively, of N-vinylprotoporphyrin IX (N-vinylPP) formation after administration of 3-[(arylthio)ethyl]sydnone (TTMS) to rats. 3-(2-(2,4,6-trimethylphenyl)thioethyl)-4-methylsydnone 182-186 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 0-26 10460791-2 1999 Female rats receiving TTMS were pretreated with dexamethasone, which induces CYP3A1 preferentially to CYP3A2. Dexamethasone 48-61 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 102-108 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Diazinon 29-37 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 53-59 10548448-18 1999 These results suggest that OPEO biodegradation products interact with constitutive P450 isoforms, CYP1A2, CYP2A2, CYP2B2, CYP2C11 and CYP3A2 in rat liver in vitro (OP > OP2EO > OP1EC), and that the mechanism of this interaction differs depending on the compound and P450 isoform. opeo 27-31 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 134-140 10386583-4 1999 Anti-CYP3A2 antibody (which cross-reacts with CYP3A4) or ketoconazole (an inhibitor of the CYP3A superfamily) inhibited nitric oxide formation from isosorbide dinitrate in rat heart microsomes. Nitric Oxide 120-132 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 5-11 10386583-4 1999 Anti-CYP3A2 antibody (which cross-reacts with CYP3A4) or ketoconazole (an inhibitor of the CYP3A superfamily) inhibited nitric oxide formation from isosorbide dinitrate in rat heart microsomes. Isosorbide Dinitrate 148-168 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 5-11 9917326-3 1999 The 6betaB-A site shows a high degree of similarity to a consensus sequence of the binding site of hepatocyte nuclear factor 4 (HNF-4) and also to the 6betaA-A site on the rat CYP3A2 gene promoter region. 6betab-a 4-12 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 176-182 9917326-3 1999 The 6betaB-A site shows a high degree of similarity to a consensus sequence of the binding site of hepatocyte nuclear factor 4 (HNF-4) and also to the 6betaA-A site on the rat CYP3A2 gene promoter region. 6betaa-a 151-159 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 176-182 9917326-4 1999 Our previous study suggested an involvement of the 6betaA-A site in the basal transactivation of CYP3A2 gene using HepG2 cells. 6betaa-a 51-59 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 97-103 9917326-5 1999 In the present study, transactivation through the 6betaB-A and 6betaA-A sites of CYP3A1 and CYP3A2 genes has directly been shown by coexpression of HNF-4 and CYP3A1 or CYP3A2 promoter-reporter fused genes. 6betab-a 50-58 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 92-98 9917326-5 1999 In the present study, transactivation through the 6betaB-A and 6betaA-A sites of CYP3A1 and CYP3A2 genes has directly been shown by coexpression of HNF-4 and CYP3A1 or CYP3A2 promoter-reporter fused genes. 6betab-a 50-58 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 168-174 9917326-5 1999 In the present study, transactivation through the 6betaB-A and 6betaA-A sites of CYP3A1 and CYP3A2 genes has directly been shown by coexpression of HNF-4 and CYP3A1 or CYP3A2 promoter-reporter fused genes. 6betaa-a 63-71 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 92-98 9917326-5 1999 In the present study, transactivation through the 6betaB-A and 6betaA-A sites of CYP3A1 and CYP3A2 genes has directly been shown by coexpression of HNF-4 and CYP3A1 or CYP3A2 promoter-reporter fused genes. 6betaa-a 63-71 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 168-174 10048600-10 1999 The formation of 9-hydroxyrisperidone is highly correlated with testosterone 6beta-hydroxylase activities, suggesting that inducible CYP3A contributes significantly to the metabolism of risperidone in rat. Paliperidone Palmitate 17-37 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 64-94 10048600-10 1999 The formation of 9-hydroxyrisperidone is highly correlated with testosterone 6beta-hydroxylase activities, suggesting that inducible CYP3A contributes significantly to the metabolism of risperidone in rat. Risperidone 26-37 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 64-94 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Testosterone 98-110 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 53-59 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Testosterone 220-232 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 53-59 9890448-6 1999 Results obtained by using chemical inhibitors or antibodies selectively active against specific CYPs provide a direct evidence for the involvement of CYP2C11, CYP3A2, and CYP2B1/2, indicating that each of them contributed about 40-50% of the diazinon metabolism, in hepatic microsomes from untreated, phenobarbital-, and dexamethasone-treated rats, respectively. Diazinon 242-250 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 159-165 9890448-6 1999 Results obtained by using chemical inhibitors or antibodies selectively active against specific CYPs provide a direct evidence for the involvement of CYP2C11, CYP3A2, and CYP2B1/2, indicating that each of them contributed about 40-50% of the diazinon metabolism, in hepatic microsomes from untreated, phenobarbital-, and dexamethasone-treated rats, respectively. Phenobarbital 301-314 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 159-165 9890448-6 1999 Results obtained by using chemical inhibitors or antibodies selectively active against specific CYPs provide a direct evidence for the involvement of CYP2C11, CYP3A2, and CYP2B1/2, indicating that each of them contributed about 40-50% of the diazinon metabolism, in hepatic microsomes from untreated, phenobarbital-, and dexamethasone-treated rats, respectively. Dexamethasone 321-334 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 159-165 9708877-3 1998 Among the P450-dependent monooxygenase activities, testosterone 2alpha-hydroxylase (T2AH) and testosterone 6beta-hydroxylase (T6BH) activities, which are associated with CYP2C11 and CYP3A2 respectively, were remarkably decreased by 40 mg/kg BPA. bisphenol A 241-244 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 94-124 9717516-7 1998 Induction of the dexamethasone-inducible CYP3A23 mRNA to 4.5- and 2.5-fold of control was detected in liver of MET- and 3BP-induced rats; CYP3A2 mRNA levels were unchanged. Dexamethasone 17-30 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 41-47 10030456-4 1998 The specificity of the induction by 4-methylpyrazole and of the inhibition by diallyl sulfide for CYP2E1 was determined using the [14C]caffeine (CYP1A2), [14C]aminopyrine (CYP2C11), and [14C]erythromycin (CYP3A2) breath tests. allyl sulfide 78-93 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 205-211 9708877-3 1998 Among the P450-dependent monooxygenase activities, testosterone 2alpha-hydroxylase (T2AH) and testosterone 6beta-hydroxylase (T6BH) activities, which are associated with CYP2C11 and CYP3A2 respectively, were remarkably decreased by 40 mg/kg BPA. bisphenol A 241-244 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 126-130 9708877-3 1998 Among the P450-dependent monooxygenase activities, testosterone 2alpha-hydroxylase (T2AH) and testosterone 6beta-hydroxylase (T6BH) activities, which are associated with CYP2C11 and CYP3A2 respectively, were remarkably decreased by 40 mg/kg BPA. bisphenol A 241-244 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 182-188 9708877-5 1998 Furthermore, immunoblotting showed that BPA (20 or 40 mg/kg) significantly reduced CYP2C 11/6 and CYP3A2/1 protein levels in rat liver microsomes. bisphenol A 40-43 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 98-106 9708877-7 1998 The Km values for T2AH and T6BH in 20 and 40 mg/kg BPA-treated rats were significantly high compared with that in control rats. bisphenol A 51-54 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 27-31 9708877-8 1998 The Vmax for T2AH was dose-dependently decreased by BPA treatment, whereas that of T6BH was only decreased by BPA at 40 mg/kg. bisphenol A 110-113 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 83-87 9353139-1 1997 Using a CYP3A2-specific oligonucleotide and an antipeptide antibody raised against the C terminus of CYP3A2 (VINGA) it is demonstrated that metyrapone administration to adult (12 weeks old) but not immature (3 weeks old) male Sprague Dawley rats induces the hepatic expression of CYP3A2 mRNA and protein. Metyrapone 140-150 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 8-14 9443857-7 1998 Antibody inhibition experiments demonstrated ethosuximide metabolite levels for PB microsomes were not affected by CYP2B1 antibodies, whereas CYP3A2 antibodies reduced metabolite levels for both PB and CTZ microsomes by over 80%. Phenobarbital 195-197 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 142-148 9443857-7 1998 Antibody inhibition experiments demonstrated ethosuximide metabolite levels for PB microsomes were not affected by CYP2B1 antibodies, whereas CYP3A2 antibodies reduced metabolite levels for both PB and CTZ microsomes by over 80%. Clotrimazole 202-205 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 142-148 9806224-6 1998 The amount of CYP3A2 protein and the activity of erythromycin N-demethylase were significantly increased by dexamethasone and prednisolone pretreatments, but dexamethasone showed a greater effect than prednisolone. Dexamethasone 108-121 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 14-20 9806224-6 1998 The amount of CYP3A2 protein and the activity of erythromycin N-demethylase were significantly increased by dexamethasone and prednisolone pretreatments, but dexamethasone showed a greater effect than prednisolone. Prednisolone 126-138 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 14-20 9806224-6 1998 The amount of CYP3A2 protein and the activity of erythromycin N-demethylase were significantly increased by dexamethasone and prednisolone pretreatments, but dexamethasone showed a greater effect than prednisolone. Dexamethasone 158-171 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 14-20 9806224-6 1998 The amount of CYP3A2 protein and the activity of erythromycin N-demethylase were significantly increased by dexamethasone and prednisolone pretreatments, but dexamethasone showed a greater effect than prednisolone. Prednisolone 201-213 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 14-20 9493318-8 1998 The levels of testosterone 6 beta-hydroxylase (T6BH) activity and CYP3A2/1 protein in the male rat were reduced by cis-1,2-DCE but not trans-1,2-DCE. CIS-1,2-DICHLOROETHYLENE 115-126 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 14-45 9493318-8 1998 The levels of testosterone 6 beta-hydroxylase (T6BH) activity and CYP3A2/1 protein in the male rat were reduced by cis-1,2-DCE but not trans-1,2-DCE. CIS-1,2-DICHLOROETHYLENE 115-126 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 47-51 9493318-8 1998 The levels of testosterone 6 beta-hydroxylase (T6BH) activity and CYP3A2/1 protein in the male rat were reduced by cis-1,2-DCE but not trans-1,2-DCE. CIS-1,2-DICHLOROETHYLENE 115-126 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 66-74 9399990-7 1997 Antisera raised against rat CYP3A2 strongly inhibited quinine 3-hydroxylation by about 96, 84 and 92% with mouse, rat and dog liver microsomes, respectively, but neither anti-rat 2C11 and 2E1 antisera did so with rat liver microsomes. Quinine 54-61 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 28-34 9870717-1 1998 Both hypothyroidism and retinol supplementation in rats induce CYP 3A2 and suppress CYP 2C11. Vitamin A 24-31 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 63-70 9353139-1 1997 Using a CYP3A2-specific oligonucleotide and an antipeptide antibody raised against the C terminus of CYP3A2 (VINGA) it is demonstrated that metyrapone administration to adult (12 weeks old) but not immature (3 weeks old) male Sprague Dawley rats induces the hepatic expression of CYP3A2 mRNA and protein. Metyrapone 140-150 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 101-107 9353139-1 1997 Using a CYP3A2-specific oligonucleotide and an antipeptide antibody raised against the C terminus of CYP3A2 (VINGA) it is demonstrated that metyrapone administration to adult (12 weeks old) but not immature (3 weeks old) male Sprague Dawley rats induces the hepatic expression of CYP3A2 mRNA and protein. Metyrapone 140-150 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 101-107 9193873-8 1997 Anti-CYP3A2 antisera inhibited the activities of the S-oxidases catalyzing the reactions from FS to R-FSO (40%) and to S-FSO (60%) at the high substrate concentration and inhibited the activities of the S-oxidases, thus catalyzing reactions from R-FSO and S-FSO to FSO2 (70%) at both high and low substrate concentrations. phenylalanylserine 94-96 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 5-11 9321518-1 1997 Caffeine and 7,8-benzoflavone activate CYP3A2 in rat liver microsomes. Caffeine 0-8 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 39-45 9321518-1 1997 Caffeine and 7,8-benzoflavone activate CYP3A2 in rat liver microsomes. alpha-naphthoflavone 13-29 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 39-45 9268688-1 1997 Maintenance of rats on a vitamin A-deficient diet resulting in undetectable levels of plasma retinol and significant reductions in relative testes weight compared to age-matched controls leads to the loss of liver membrane-bound low affinity glucocorticoid binding site (LAGS) activity without any effects on the levels of constitutively expressed CYP3A2 protein. Vitamin A 25-34 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 348-354 9268688-4 1997 Retinol acetate administration alone induces CYP3A2 protein to apparent maximal levels since dexamethasone 21-phosphate does not further increase the induction response. retinol acetate 0-15 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 45-51 9268688-5 1997 However, CYP3A2 remains inducible to dexamethasone 21-phosphate in vitamin A-deficient rats. dexamethasone 21-phosphate 37-63 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 9-15 9268688-5 1997 However, CYP3A2 remains inducible to dexamethasone 21-phosphate in vitamin A-deficient rats. Vitamin A 67-76 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 9-15 9268688-6 1997 These data suggest that vitamin A status affects the expression of LAGS and CYP3A2 but that glucocorticoids regulate the induction of CYP3A2 by a mechanism(s) independent of their interaction with the LAGS. Vitamin A 24-33 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 76-82 9193873-8 1997 Anti-CYP3A2 antisera inhibited the activities of the S-oxidases catalyzing the reactions from FS to R-FSO (40%) and to S-FSO (60%) at the high substrate concentration and inhibited the activities of the S-oxidases, thus catalyzing reactions from R-FSO and S-FSO to FSO2 (70%) at both high and low substrate concentrations. r-fso 100-105 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 5-11 9193873-8 1997 Anti-CYP3A2 antisera inhibited the activities of the S-oxidases catalyzing the reactions from FS to R-FSO (40%) and to S-FSO (60%) at the high substrate concentration and inhibited the activities of the S-oxidases, thus catalyzing reactions from R-FSO and S-FSO to FSO2 (70%) at both high and low substrate concentrations. s-fso 119-124 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 5-11 9193873-8 1997 Anti-CYP3A2 antisera inhibited the activities of the S-oxidases catalyzing the reactions from FS to R-FSO (40%) and to S-FSO (60%) at the high substrate concentration and inhibited the activities of the S-oxidases, thus catalyzing reactions from R-FSO and S-FSO to FSO2 (70%) at both high and low substrate concentrations. r-fso 246-251 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 5-11 9193873-8 1997 Anti-CYP3A2 antisera inhibited the activities of the S-oxidases catalyzing the reactions from FS to R-FSO (40%) and to S-FSO (60%) at the high substrate concentration and inhibited the activities of the S-oxidases, thus catalyzing reactions from R-FSO and S-FSO to FSO2 (70%) at both high and low substrate concentrations. s-fso 256-261 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 5-11 9193873-8 1997 Anti-CYP3A2 antisera inhibited the activities of the S-oxidases catalyzing the reactions from FS to R-FSO (40%) and to S-FSO (60%) at the high substrate concentration and inhibited the activities of the S-oxidases, thus catalyzing reactions from R-FSO and S-FSO to FSO2 (70%) at both high and low substrate concentrations. fso2 265-269 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 5-11 9193873-11 1997 Anti-CYP3A2 antisera inhibited the activities of all the S-oxidases in human liver microsomes ranging from 40 to 80%, suggesting that CYP3A is also involved in all of the S-oxidations of flosequinan in humans. flosequinan 187-198 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 5-11 9569940-9 1997 Immunoblotting showed that CYP3A2/1 and CYP4A1 protein levels were significantly induced from 1.3- to 2.2-fold by Irgasan DP300 (> or = 0.4 mmol/kg), whereas those of CYP1A1/2, CYP2C11/6 and CYP2E1 were not affected by any doses of Irgasan DP300. dp300 122-127 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 27-33 21781750-6 1997 Polyclonal antibodies raised against rat liver microsomal CYP3A2 and a CYP3A inhibitor, troleandomycin (TAO), effectively inhibited T-6beta-hydroxylation by liver microsomes from both strains of rats. Troleandomycin 104-107 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 58-64 9569940-9 1997 Immunoblotting showed that CYP3A2/1 and CYP4A1 protein levels were significantly induced from 1.3- to 2.2-fold by Irgasan DP300 (> or = 0.4 mmol/kg), whereas those of CYP1A1/2, CYP2C11/6 and CYP2E1 were not affected by any doses of Irgasan DP300. dp300 243-248 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 27-33 9217276-6 1997 Phenobarbital, a typical inducer of CYP3A2 and 2B1 increased CYP3A2 level as well, but had less potency in the induction of CYP2B1 in HSCs. Phenobarbital 0-13 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 36-50 9458185-8 1997 Immunoblotting showed CYP1A1/2, CYP2B1/2, CYP2E1, and CYP3A2/1 protein levels were significantly decreased by 60-66% by 1,1-DCE (800 mg/kg), whereas that of CYP4A1/2 was not affected by any dose of 1,1-DCE. vinylidene chloride 120-127 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 54-62 9217276-6 1997 Phenobarbital, a typical inducer of CYP3A2 and 2B1 increased CYP3A2 level as well, but had less potency in the induction of CYP2B1 in HSCs. Phenobarbital 0-13 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 36-42 8968370-0 1996 Enhanced inhibition of microsomal cytochrome P450 3A2 in rat liver during diltiazem biotransformation. Diltiazem 74-83 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 34-53 8968370-4 1996 The principal finding to emerge was that the N-demethylated metabolite of DTZ was a more potent competitive inhibitor than DTZ of CYP3A2-dependent testosterone 6 beta-hydroxylation. Nitrogen 45-46 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 130-136 8968370-4 1996 The principal finding to emerge was that the N-demethylated metabolite of DTZ was a more potent competitive inhibitor than DTZ of CYP3A2-dependent testosterone 6 beta-hydroxylation. Diltiazem 74-77 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 130-136 8968370-4 1996 The principal finding to emerge was that the N-demethylated metabolite of DTZ was a more potent competitive inhibitor than DTZ of CYP3A2-dependent testosterone 6 beta-hydroxylation. Diltiazem 123-126 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 130-136 8968370-5 1996 This P450 appeared to be the preferred target for inhibition, because the observed K/K(m) ratio for inhibition of CYP3A2-dependent steroid hydroxylation was approximately 4- and 100-fold lower than those for CYP2C11 and CYP2A1-dependent pathways, respectively. Steroids 131-138 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 114-120 8968370-9 1996 Considered together, the findings of the present study establish that N-desmethyl-DTZ is a preferential inhibitor of CYP3A2 in rat hepatic microsomes, with greater potency than the parent drug. N-monodemethyldiltiazem 70-85 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 117-123 8894516-5 1996 Ciprofloxacin and norfloxacin significantly depressed the N-demethylation of erythromycin by CYP3A4 in human microsomes and by CYP3A2 in rat microsomes. Ciprofloxacin 0-13 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 127-133 8894516-5 1996 Ciprofloxacin and norfloxacin significantly depressed the N-demethylation of erythromycin by CYP3A4 in human microsomes and by CYP3A2 in rat microsomes. Norfloxacin 18-29 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 127-133 8690406-8 1996 In both control and phenobarbital-treated hepatocytes, rat recombinant IFN-gamma (33 U/mL) reduced mRNA for 3A2 and 3A1-like CYPs, as well as 3A protein and testosterone 6 beta-hydroxylase activity. Phenobarbital 20-33 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 157-188 8886602-11 1996 Immunoinhibition studies revealed that polyclonal anti-rat CYP3A2 antibody inhibited MDZ metabolism 80-90% in rat, human, and cDNA-expressed human CYP3A4 microsomes, thus suggesting that members of the CYP3A4 subfamily were involved in the metabolism. Midazolam 85-88 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 59-65 8694846-5 1996 At this time, CYP3A2-mediated testosterone 6 beta-hydroxylation was approximately 7-fold higher in hepatocytes cultured in the presence of metyrapone than in control cells, and CYP2C11-dependent testosterone 2 alpha- and 16 alpha-hydroxylation activities were between 2 and 3-fold greater. Testosterone 30-42 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 14-20 8879146-7 1996 5-OH-NEF formation was inhibited by antibody to rat CYP3A2 by 60%, and antibodies to CYP2B1, CYP2C11 and CYP2E1 also showed 15-25% inhibition of the formation of 5-OH-NEF. 5-oh 0-4 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 52-58 8694846-5 1996 At this time, CYP3A2-mediated testosterone 6 beta-hydroxylation was approximately 7-fold higher in hepatocytes cultured in the presence of metyrapone than in control cells, and CYP2C11-dependent testosterone 2 alpha- and 16 alpha-hydroxylation activities were between 2 and 3-fold greater. Metyrapone 139-149 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 14-20 8694846-5 1996 At this time, CYP3A2-mediated testosterone 6 beta-hydroxylation was approximately 7-fold higher in hepatocytes cultured in the presence of metyrapone than in control cells, and CYP2C11-dependent testosterone 2 alpha- and 16 alpha-hydroxylation activities were between 2 and 3-fold greater. Testosterone 195-207 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 14-20 8694846-9 1996 However, treatment of cells with metyrapone considerably elevated levels of one or more CYP3A subfamily mRNA species, as detected by a riboprobe based on the cDNA for CYP3A1 ("CYP3A1-like mRNA") that were demonstrated, by another riboprobe, not to be CYP3A2 or RNCYP3AM. Metyrapone 33-43 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 251-257 8694846-13 1996 The particular mechanism employed is gene-specific, whereby even the highly homologous genes CYP3A2, RL33/cDEX and, possibly, RNCYP3AM are subject to different types of regulation in the presence of metyrapone. Metyrapone 199-209 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 93-99 8865369-12 1996 These results indicate that the CYP2E1 subfamily is the major enzyme involved in TMO N-demethylation in rat in vitro although the CYP3A2 is also involved in this transformation. Nitrogen 85-86 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 130-136 8696774-5 1996 Irgasan DP300 slightly inhibited testosterone 6 beta-hydroxylase (TS6BH) activities in some microsomes. dp300 8-13 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 33-64 8696774-5 1996 Irgasan DP300 slightly inhibited testosterone 6 beta-hydroxylase (TS6BH) activities in some microsomes. dp300 8-13 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 66-71 8866826-8 1996 Human CYP3A4 and rat CYP3A2 had high testosterone 2 beta- and 6 beta-hydroxylation activities in a modified reconstituted system with a lipid mixture. Testosterone 37-49 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 21-27 8625305-4 1996 Evidence is presented that the male-specific rat CYP 3A2, an orthologue of human CYP 3A4, may be primarily responsible for AFB activation in rat liver at both high and low AFB substrate concentrations. Aflatoxin B1 123-126 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 49-56 8577819-1 1995 The ability of 3,5,3"-triiodothyronine (T3) and cobalt-protoporphyrin LX (CoPP) to alter the levels of the cytochrome P-450 isoforms, CYP3A2, CYP2E1, CYP2B1 and CYP2B2, was examined in vitro in thyroidectomized adult male rats. Triiodothyronine 15-38 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 134-140 8573203-0 1996 Impact of tamoxifen on peripubertal androgen imprinting of rat hepatic cytochrome P450 2C11, cytochrome P450 3A2, and steroid 5 alpha-reductase. Tamoxifen 10-19 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 93-112 8849332-15 1995 However, following treatment of rats with PCN, both CYP3A1 and CYP3A2 were found to be strongly expressed in hepatocytes throughout the lobule, although CYP3A2 showed greater expression in the centrilobular region. Pregnenolone Carbonitrile 42-45 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 63-69 8849332-15 1995 However, following treatment of rats with PCN, both CYP3A1 and CYP3A2 were found to be strongly expressed in hepatocytes throughout the lobule, although CYP3A2 showed greater expression in the centrilobular region. Pregnenolone Carbonitrile 42-45 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 153-159 8531135-0 1995 Inhibition of the rat cytochrome P450 3A2 by an antisense phosphorothioate oligodeoxynucleotide in vivo. phosphorothioate oligodeoxynucleotide 58-95 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 22-41 8531135-4 1995 Midazolam (MZ) sleep times were used as CYP3A2-specific in vivo marker in male Sprague-Dawley rats. Midazolam 0-9 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 40-46 8577819-1 1995 The ability of 3,5,3"-triiodothyronine (T3) and cobalt-protoporphyrin LX (CoPP) to alter the levels of the cytochrome P-450 isoforms, CYP3A2, CYP2E1, CYP2B1 and CYP2B2, was examined in vitro in thyroidectomized adult male rats. Triiodothyronine 40-42 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 134-140 8577819-1 1995 The ability of 3,5,3"-triiodothyronine (T3) and cobalt-protoporphyrin LX (CoPP) to alter the levels of the cytochrome P-450 isoforms, CYP3A2, CYP2E1, CYP2B1 and CYP2B2, was examined in vitro in thyroidectomized adult male rats. cobalt-protoporphyrin lx 48-72 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 134-140 8577819-1 1995 The ability of 3,5,3"-triiodothyronine (T3) and cobalt-protoporphyrin LX (CoPP) to alter the levels of the cytochrome P-450 isoforms, CYP3A2, CYP2E1, CYP2B1 and CYP2B2, was examined in vitro in thyroidectomized adult male rats. copp 74-78 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 134-140 8535396-9 1995 These results suggest that a CYP2D isozyme(s) is the primary enzyme in alprenolol 4-hydroxylation and N-desisopropylation in a lower substrate concentration range, and that the involvement of some male-specific P450 isozyme(s) other than CYP2C11 or CYP3A2 may cause the sex difference in the 4-hydroxylation. Alprenolol 71-81 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 249-255 8535396-9 1995 These results suggest that a CYP2D isozyme(s) is the primary enzyme in alprenolol 4-hydroxylation and N-desisopropylation in a lower substrate concentration range, and that the involvement of some male-specific P450 isozyme(s) other than CYP2C11 or CYP3A2 may cause the sex difference in the 4-hydroxylation. Nitrogen 102-103 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 249-255 7598745-13 1995 We have concluded that CP alters the enzymes NADPH P450 reductase, steroid 5 alpha-reductase and CYP3A2 via perturbation of the regulation of these enzymes by testosterone and/or thyroid hormones. Testosterone 159-171 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 97-103 7728897-4 1995 Major PB-inducible forms, CYP2B1, CYP2B2, CYP3A2 and CYP2C6 were induced with four PCBs (342 mumol/kg) and their 3-MeSO2 metabolites (0.5-10 mumol/kg), indicating that 3-MeSO2 metabolites were strong PB-type inducers of hepatic drug-metabolizing enzymes. Polychlorinated Biphenyls 83-87 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 42-48 7728897-4 1995 Major PB-inducible forms, CYP2B1, CYP2B2, CYP3A2 and CYP2C6 were induced with four PCBs (342 mumol/kg) and their 3-MeSO2 metabolites (0.5-10 mumol/kg), indicating that 3-MeSO2 metabolites were strong PB-type inducers of hepatic drug-metabolizing enzymes. 3-meso2 113-120 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 42-48 7726576-12 1995 These results suggest an essential role of the binding of HNF-4 and/or HNF-4-related nuclear factors to the 6 beta A-A site on the basal transcriptional activation of the CYP3A2 gene in liver cells. beta a-a 110-118 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 171-177 7979376-11 1994 Catalytic properties of 6 beta-A for typical CYP3A substrates were consistent with those of purified rat P450(6 beta-1) and P450(6 beta-3), corresponding, respectively, to CYP3A2 or the variant form (K. Nagata, F. J. Gonzalez, Y. Yamazoe, and R. Kato (1990) J. Biochem. beta- 26-31 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 172-178 7736342-8 1994 Since CYP3A2 is absent or very low in hepatic microsomes from DEX-treated adult female rats, this identifies CYP3A1 as an isoform capable of biotransforming GTN to an activator of guanylyl cyclase. Dexamethasone 62-65 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 6-12 7736342-8 1994 Since CYP3A2 is absent or very low in hepatic microsomes from DEX-treated adult female rats, this identifies CYP3A1 as an isoform capable of biotransforming GTN to an activator of guanylyl cyclase. Nitroglycerin 157-160 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 6-12 7895610-7 1994 Antisera against rat CYP2B1, CYP2E1, and CYP3A2 suppressed dorzolamide N-deethylase activity by 52%, 43% and 46%, respectively, whereas only 18% and 15% of the activity were inhibited by anti-CYP1A1 and anti-CYP4A1 antibodies, respectively. dorzolamide 59-70 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 41-47 8097709-4 1993 Activities of testosterone 2 beta- and 6 beta-hydroxylases were increased by administration of clarithromycin and N-demethyl clarithromycin when these activities were measured in the presence of ferricyanide, but not significant induction was observed when measured in the absence of ferricyanide. Clarithromycin 95-109 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 14-58 8268852-6 1993 In the reconstituted system using the lipids extracted from microsomes, CYP 3A2 more effectively catalyzed the oxidation of 9-AA to 9-ACA, and its catalytic activity (nmol/min/nmol P450) was 3.33 or 6.61 in the absence or presence of cytochrome b5, respectively. 9-anthraldehyde 124-128 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 72-79 8268852-6 1993 In the reconstituted system using the lipids extracted from microsomes, CYP 3A2 more effectively catalyzed the oxidation of 9-AA to 9-ACA, and its catalytic activity (nmol/min/nmol P450) was 3.33 or 6.61 in the absence or presence of cytochrome b5, respectively. 9-anthroic acid 132-137 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 72-79 7918645-9 1994 Injection of IL1, low doses of dexamethasone, or both, in male rats produced decreases in total P450, and in CYP3A2 and CYP2C11 mRNA and protein expression similar to effects previously seen for CYP2C12 expression in females. Dexamethasone 31-44 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 109-115 8097709-4 1993 Activities of testosterone 2 beta- and 6 beta-hydroxylases were increased by administration of clarithromycin and N-demethyl clarithromycin when these activities were measured in the presence of ferricyanide, but not significant induction was observed when measured in the absence of ferricyanide. N-Desmethyl Clarithromycin 114-139 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 14-58 8097709-4 1993 Activities of testosterone 2 beta- and 6 beta-hydroxylases were increased by administration of clarithromycin and N-demethyl clarithromycin when these activities were measured in the presence of ferricyanide, but not significant induction was observed when measured in the absence of ferricyanide. hexacyanoferrate III 195-207 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 14-58 8097709-4 1993 Activities of testosterone 2 beta- and 6 beta-hydroxylases were increased by administration of clarithromycin and N-demethyl clarithromycin when these activities were measured in the presence of ferricyanide, but not significant induction was observed when measured in the absence of ferricyanide. hexacyanoferrate III 284-296 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 14-58 8423554-6 1993 Antibodies raised against CYP3A2 (anti-CYP3A) clearly inhibited microsomal 4"-hydroxylation of R-mephenytoin, but marginally S-mephenytoin, in rats. (R)-(-)-Mephenytoin 95-108 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 26-32 8423554-6 1993 Antibodies raised against CYP3A2 (anti-CYP3A) clearly inhibited microsomal 4"-hydroxylation of R-mephenytoin, but marginally S-mephenytoin, in rats. Mephenytoin 125-138 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 26-32 1417000-1 1992 Modulation of CYP3A1 and CYP3A2 mRNA expression by dexamethasone and by phenobarbital has been studied in immature (21-day-old) and adult (90-day-old) rat liver. Dexamethasone 51-64 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 25-31 1417000-1 1992 Modulation of CYP3A1 and CYP3A2 mRNA expression by dexamethasone and by phenobarbital has been studied in immature (21-day-old) and adult (90-day-old) rat liver. Phenobarbital 72-85 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 25-31 1417000-3 1992 However, CYP3A2 mRNA, although physiologically extinguished in the adult females, still responds to dexamethasone stimulation. Dexamethasone 100-113 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 9-15 1731631-10 1992 Administration of testosterone propionate restores the physiological levels of CYP3A2 mRNA characteristic of the male rat liver. Testosterone Propionate 18-41 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 79-85 1534660-8 1992 As an inducer of P450 3A1/2, loratadine was slightly less effective than phenobarbital, and was considerably less effective than dexamethasone, which caused a 10- to 33-fold increase in testosterone 2 beta-, 6 beta- and 15 beta-hydroxylase activity. Loratadine 29-39 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 186-239 1534660-8 1992 As an inducer of P450 3A1/2, loratadine was slightly less effective than phenobarbital, and was considerably less effective than dexamethasone, which caused a 10- to 33-fold increase in testosterone 2 beta-, 6 beta- and 15 beta-hydroxylase activity. Dexamethasone 129-142 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 186-239 2233686-7 1990 In a similar experiment using two phenobarbital-like inducers, (trans)nonachlor and clotrimazole, the relative inductions of P450b, P450e, P450p, and P450pcn2 mRNAs proved to be similar to those produced by phenobarbital (P450p/P450b potency ratios = 14- and 16-fold, respectively). Phenobarbital 34-47 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 150-158 1715015-5 1991 Kepone also resembled phenobarbital in these experiments, in that there were dose-dependent increases in the amounts of hepatocellular P450p, P450pcn2, P450PB-1, P450f, and NADPH-cytochrome P450 oxidoreductase mRNAs. Chlordecone 0-6 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 142-150 2067545-6 1991 Addition of 1 microM dexamethasone (DEX) to the culture medium increased UDP-glucuronyltransferase activity towards DIG, cytochrome P450 reductase and testosterone-6 beta-hydroxylase activities up to 2.5-, 2.0- and 7-fold, respectively and induced cytochrome P450IIIA immunoreactive protein(s) in the hepatocytes after 24 and 48 h of culture; DEX was less effective at the 72 h time-point. Dexamethasone 21-34 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 151-182 2067545-6 1991 Addition of 1 microM dexamethasone (DEX) to the culture medium increased UDP-glucuronyltransferase activity towards DIG, cytochrome P450 reductase and testosterone-6 beta-hydroxylase activities up to 2.5-, 2.0- and 7-fold, respectively and induced cytochrome P450IIIA immunoreactive protein(s) in the hepatocytes after 24 and 48 h of culture; DEX was less effective at the 72 h time-point. Dexamethasone 36-39 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 151-182 2233686-1 1990 Phenobarbital induces cytochromes P450 (P450s) of not only the class IIB gene subfamily (i.e., P450b and P450e) but also the class IIIA gene subfamily (P450p and P450pcn2). Phenobarbital 0-13 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 162-170 2233686-6 1990 Phenobarbital also produced a weak dose-dependent induction of P450pcn2 mRNA, with a potency (ED50 = 3.4 x 10(-5) M) intermediate between those for P450b/e and P450p. Phenobarbital 0-13 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 63-71 2233686-7 1990 In a similar experiment using two phenobarbital-like inducers, (trans)nonachlor and clotrimazole, the relative inductions of P450b, P450e, P450p, and P450pcn2 mRNAs proved to be similar to those produced by phenobarbital (P450p/P450b potency ratios = 14- and 16-fold, respectively). Clotrimazole 84-96 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 150-158 2233686-7 1990 In a similar experiment using two phenobarbital-like inducers, (trans)nonachlor and clotrimazole, the relative inductions of P450b, P450e, P450p, and P450pcn2 mRNAs proved to be similar to those produced by phenobarbital (P450p/P450b potency ratios = 14- and 16-fold, respectively). Phenobarbital 207-220 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 150-158 2393297-9 1990 Analysis of Northern blots hybridized with oligonucleotides specific for P450PCN1(IIIA1) and P450PCN2(IIIA2), respectively, revealed that untreated male rat liver and cultures of hepatocytes prepared from these animals expressed readily detectable amounts of P450PCN1(IIIA1) mRNA. Oligonucleotides 43-59 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 93-101 2393297-11 1990 We conclude that the pathways for the induction of P450b/e and P450p by phenobarbital, and the pathways for the gender-specific basal expression of P450PCN1(IIIA1) and P450PCN2(IIIA2) are not the same and can be distinguished by their differential response to inhibition of ongoing protein synthesis. Phenobarbital 72-85 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 168-176 34952190-0 2022 Aidi injection altered the activity of CYP2D4, CYP1A2, CYP2C19, CYP3A2, CYP2E1 and CYP2C11 in normal and diethylnitrosamine-induced hepatocellular carcinoma in rats. aidi 0-4 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 64-70 34952190-3 2022 However, the changes of Aidi injection on the activities of CYP2D4, CYP1A2, CYP2C19, CYP3A2, CYP2E1 and CYP2C11 in normal and HCC states are still unknown. aidi 24-28 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 85-91 34155553-12 2022 RESULTS: Experimental DM induced by STZ caused a significant decrement in liver CYP3A2 protein content of rats on days 10 and 20 (P < 0.01), and 30 (P < 0.05) compared to the control animals. Streptozocin 36-39 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 80-86 34384867-5 2021 In particular, along with testicular damage and low testosterone levels, we also observed a decrease in male-specific (CYP3A2) or male-dominant (CYP2B1 and CYP3A1) CYP isoforms in the livers of rats with hepatotoxicity following cisplatin treatment, which may be associated with an imbalance in male hormone regulation caused by renal and testicular injury. Cisplatin 229-238 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 119-125 35408639-5 2022 The CYP3A2 isoenzyme is responsible for dexamethasone metabolism in vitro. Dexamethasone 40-53 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 4-10 35408639-6 2022 The results showed that ibuprofen acts as a non-competitive inhibitor for CYP3A2 activity with Ki = 224.981 +- 1.854 microM and IC50 = 230.552 +- 2.020 microM, although remdesivir showed a mixed inhibition pattern with a Ki = 22.504 +- 0.008 microM and IC50 = 45.007 +- 0.016 microM. remdesivir 169-179 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 74-80 35164195-0 2022 Development and Validation of a Novel HPLC Method to Analyse Metabolic Reaction Products Catalysed by the CYP3A2 Isoform: In Vitro Inhibition of CYP3A2 Enzyme Activity by Aspirin (Drugs Often Used Together in COVID-19 Treatment). Aspirin 171-178 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 106-112 35164195-0 2022 Development and Validation of a Novel HPLC Method to Analyse Metabolic Reaction Products Catalysed by the CYP3A2 Isoform: In Vitro Inhibition of CYP3A2 Enzyme Activity by Aspirin (Drugs Often Used Together in COVID-19 Treatment). Aspirin 171-178 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 145-151 35164195-3 2022 Thus, the purpose of this study was to use High-Performance Liquid Chromatography (HPLC) to evaluate the in vitro inhibition of CYP3A2 enzyme activity using aspirin in rat liver microsomes (RLMs). Aspirin 157-164 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 128-134 35164195-7 2022 The results showed that aspirin competitively inhibits 6beta-hydroxylation (CYP3A2 activity) with an inhibition constant (Ki) = 95.46 microM and the concentration of the inhibitor causing 50% inhibition of original enzyme activity (IC50) = 190.92 microM. Aspirin 24-31 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 76-82