PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 18197403-3 2008 METHODS: The effect of celecoxib on CYP1A2 activity (phenacetin O-deethylation) was first studied in vitro using human liver microsomes. Phenacetin 53-63 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 36-42 17618427-2 2007 METHODS: The effect of tolfenamic acid on CYP1A2 (phenacetin O-deethylation) was studied using human liver microsomes, with and without albumin (0-10 mg/ml). Phenacetin 50-60 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 42-48 18307373-3 2008 The potential of duloxetine to inhibit CYP1A2 activity was determined using incubations with human liver microsomes and phenacetin, the CYP1A2 substrate. Phenacetin 120-130 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 39-45 17542019-2 2007 Probe substrates were phenacetin, diclofenac, S-mephenytoin, and dextromethorphan for CYP1A2, CYP2C9, CYP2C19, and CYP2D6, respectively. Phenacetin 22-32 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 86-92 15742976-5 2004 Males had higher metabolism than corresponding females for phenacetin O-deethylation (human marker for CYP1A2 activity), and a high correlation was found between phenacetin activity and immunoreactivity in Western blots produced with rat CYP1A2 antibodies. Phenacetin 162-172 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 238-244 16857327-7 2006 Correlation analysis between the known CYP enzyme activities and the rates of the formation of 5-hydroxy- and 7-hydroxy-KR-33028 in the 16 human liver microsomes has showed significant correlations with CYP3A4-mediated midazolam 1"-hydroxylation and CYP1A2-mediated phenacetin O-deethylation, respectively. Phenacetin 266-276 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 250-256 23045133-3 2006 Phenacetin represents a convenient probe for the assessment of human CYP1A2 activity in vitro (hepatic microsomes and recombinant enzyme). Phenacetin 0-10 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 69-75 23045133-5 2006 Acetaminophen formation in incubations of phenacetin with a CYP1A2 source is readily measured by HPLC with UV detection. Phenacetin 42-52 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 60-66 16049126-4 2005 Phenacetin, diclofenac, S-mephenytoin, bufuralol, and midazolam are used as substrates for CYP1A2, 2C9, 2C19, 2D6, and 3A4, and the assay differentiates between reversible and irreversible inhibition. Phenacetin 0-10 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 91-97 15766918-2 2005 The CYP1A2 protein was expressed in yeast cells and its enzymatic properties were compared with those of marmoset CYP1A2 using ethoxyresorufin (ER) and phenacetin (PN) as substrates. Phenacetin 152-162 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 4-10 15766918-2 2005 The CYP1A2 protein was expressed in yeast cells and its enzymatic properties were compared with those of marmoset CYP1A2 using ethoxyresorufin (ER) and phenacetin (PN) as substrates. Phenacetin 164-166 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 4-10 15801540-1 2004 A cocktail of the following probe substrates for human drug-metabolizing enzymes was used to characterize hepatocyte preparations: phenacetin (for CYP1A2), diclofenac (CYP2C9), diazepam (CYP2C19), bufuralol (CYP2D6), midazolam (CYP3A4/5) and 7-hydroxycoumarin (for glucuronidation and sulphation). Phenacetin 131-141 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 147-153 15231049-6 2004 Also, the relative specificity of the index substrates phenacetin (for CYP1A2) and chlorzoxazone (for CYP2E1) in man appears not to be applicable in rats. Phenacetin 55-65 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 71-77 12814974-7 2003 However, the ratio of the various P450s was modified in the final assay such that metabolism of phenacetin by other enzymes was approximately 20% of the metabolism by CYP1A2. Phenacetin 96-106 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 167-173 15043991-2 2004 OA competitively inhibited CYP1A2-catalyzed phenacetin O-deethylation and CYP3A4-catalyzed midazolam 1-hydroxylation, the major human drug metabolizing CYPs, with IC50 (Ki) values of 143.5 (74.2) microM and 78.9 (41.0) microM, respectively. Phenacetin 44-54 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 27-33 9712458-0 1998 Effect of active and passive cigarette smoking on CYP1A2-mediated phenacetin disposition in Chinese subjects. Phenacetin 66-76 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 50-56 11948533-7 2002 As marker activities, ethoxyresorufin O-deethylation and phenacetin O-deethylation for CYP1A2, bufuralol 1"-hydroxylation and debrisoquin 4-hydroxylation for CYP2D6, testosterone 6beta-hydroxylation and midazolam 1"-hydroxylation for CYP3A4 were compared. Phenacetin 57-67 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 87-93 15618695-7 2002 In contrast, the inhibitory effects of phenacetin, diclofenac, S-mephenytoin, dextromethorphan, bufuralol and terfenadine, typical substrates for CYP1A2, CYP2C9, CYP2C19, CYP2D6 and CYP3A4, respectively, on each recombinant CYP activity decreased after preincubation. Phenacetin 39-49 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 146-152 10460810-6 1999 No remarkable inhibition of other CYP isoforms was observed except for moderate inhibition of CYP1A2-catalyzed phenacetin O-deethylation by fluphenazine (K(i) = 40.2 microM) and perphenazine (K(i) = 65.1). Phenacetin 111-121 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 94-100 10189256-1 1998 Phenacetin O-deethylation, widely used as an index reaction for cytochrome P450 1A2 (CYP1A2) activity, displays biphasic kinetics in human liver microsomes. Phenacetin 0-10 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 64-83 10189256-1 1998 Phenacetin O-deethylation, widely used as an index reaction for cytochrome P450 1A2 (CYP1A2) activity, displays biphasic kinetics in human liver microsomes. Phenacetin 0-10 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 85-91 11765139-2 2001 The inhibition of recombinant CYP1A1 and CYP1A2 activity by quinidine and quinine was evluated using ethoxyresorutin O-deethylation, phenacetin O-deethylation and propranolol desisopropylation as probe catalytic pathways. Phenacetin 133-143 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 41-47 11599655-3 2001 CYP1A2-specific activity was also measured by phenacetin O-deethylation and caffeine 3-demethylation. Phenacetin 46-56 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 0-6 11303964-9 2000 CONCLUSIONS: The population approach characterized the EK parameters and identified the low KM enzyme responsible for phenacetin O-deethylation as CYP1A2. Phenacetin 118-128 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 147-153 10985777-0 2000 Rate-determining steps in phenacetin oxidations by human cytochrome P450 1A2 and selected mutants. Phenacetin 26-36 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 57-76 10421611-7 1999 Fluvoxamine (10 microM) and anti-CYP1A2 antibodies potently inhibited POD activity at 500 microM phenacetin in pooled human liver microsomes to 22.8 and 34.2% of controls, respectively. Phenacetin 97-107 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 33-39 9825829-0 1998 Inhibitory monoclonal antibodies to human cytochrome P450 1A2: analysis of phenacetin O-deethylation in human liver. Phenacetin 75-85 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 42-61 9712458-1 1998 The effect of active and passive cigarette smoking on CYP1A2-mediated phenacetin disposition was evaluated in a controlled study of 36 healthy Chinese subjects. Phenacetin 70-80 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 54-60 9491822-5 1998 RESULTS: Furafylline was a potent, selective inhibitor of phenacetin O-deethylation (CYP1A2-mediated) in human liver microsomes (IC50 = 0.48 microM), but inhibited both phenacetin O-deethylation and tolbutamide 4-hydroxylation (CYP2C9-mediated) at equimolar concentrations in rat liver microsomes (IC50 = 20.8 and 24.0 microM respectively). Phenacetin 58-68 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 85-91 9578183-0 1998 Inhibitory effects of antiarrhythmic drugs on phenacetin O-deethylation catalysed by human CYP1A2. Phenacetin 46-56 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 91-97 9578183-2 1998 METHODS: The inhibitory effects of mexiletine and 10 antiarrhythmic drugs on phenacetin O-deethylation, a marker reaction of CYP1A2, were studied using human liver microsomes and cDNA-expressed CYP1A2. Phenacetin 77-87 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 125-131 9578183-7 1998 In addition, propafenone and mexiletine inhibited phenacetin O-deethylation catalysed by cDNA-expressed CYP1A2. Phenacetin 50-60 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 104-110 7617560-0 1995 Kinetics and inhibition by fluvoxamine of phenacetin O-deethylation in V79 cells expressing human CYP1A2. Phenacetin 42-52 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 98-104 9351907-6 1997 Other substrates of CYP1A2, such as phenacetin, imipramine, caffeine, and estradiol, are also inhibitors of flutamide metabolism by CYP1A2. Phenacetin 36-46 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 20-26 9351907-6 1997 Other substrates of CYP1A2, such as phenacetin, imipramine, caffeine, and estradiol, are also inhibitors of flutamide metabolism by CYP1A2. Phenacetin 36-46 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 132-138 8986010-1 1996 Biotransformation of phenacetin via O-deethylation to acetaminophen, an index reaction reflecting activity of Cytochrome P450-1A2, was studied in microsomal preparations from a series of human livers. Phenacetin 21-31 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 110-129 8885124-0 1996 The influence of ethnic factors and gender on CYP1A2-mediated drug disposition: a comparative study in Caucasian and Chinese subjects using phenacetin as a marker substrate. Phenacetin 140-150 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 46-52 8885124-1 1996 To assess potential ethnic and gender-related differences in the expression of cytochrome CYP1A2-mediated activity, the pharmacokinetics of phenacetin (a CYP1A2 substrate) and its metabolite paracetamol were compared in 20 Caucasian and 20 Chinese subjects after administration of a single oral 900 mg phenacetin dose. Phenacetin 140-150 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 154-160 7617560-1 1995 The kinetics of phenacetin O-deethylation and its inhibition by fluvoxamine was investigated in a V79 cell line (V79MZh1A2) transfected with human CYP1A2. Phenacetin 16-26 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 147-153 7720520-4 1995 Furafylline was a potent, mechanism-based inhibitor for CYP1A2-mediated phenacetin O-deethylation. Phenacetin 72-82 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 56-62 8474022-2 1993 Expressed CYP1A1 and CYP1A2 both catalyzed the O-deethylation of phenacetin, although the apparent Km was about 4-fold lower for CYP1A2 (25 vs. 108 microM). Phenacetin 65-75 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 21-27 8261468-2 1994 The inhibitory potential of furafylline in vivo was first assessed by determining its effect on clearance of phenacetin to paracetamol by the model CYP1A2-dependent O-deethylation pathway. Phenacetin 109-119 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 148-154 8474022-2 1993 Expressed CYP1A1 and CYP1A2 both catalyzed the O-deethylation of phenacetin, although the apparent Km was about 4-fold lower for CYP1A2 (25 vs. 108 microM). Phenacetin 65-75 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 129-135 8474022-3 1993 Phenacetin O-deethylation exhibited biphasic kinetics in human liver microsomes, and the apparent Km for the high-affinity component (9 +/- 6 microM) was consistent with the involvement of CYP1A2 in this reaction. Phenacetin 0-10 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 189-195 8474022-4 1993 The prototypic CYP1A xenobiotic inhibitor and substrate probes alpha-naphthoflavone, ellipticine, 7-ethoxycoumarin and 7-ethoxyresorufin all inhibited CYP1A1- and CYP1A2-mediated phenacetin O-deethylation as well as the high-affinity component of human liver phenacetin O-deethylase activity. Phenacetin 179-189 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 163-169 8474022-4 1993 The prototypic CYP1A xenobiotic inhibitor and substrate probes alpha-naphthoflavone, ellipticine, 7-ethoxycoumarin and 7-ethoxyresorufin all inhibited CYP1A1- and CYP1A2-mediated phenacetin O-deethylation as well as the high-affinity component of human liver phenacetin O-deethylase activity. Phenacetin 259-269 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 163-169 8474022-7 1993 In contrast, the monoclonal antibody MAb 1-7-1, raised against 3-methylcholanthrene-inducible rat cytochromes 450, almost abolished CYP1A1-mediated phenacetin O-deethylation, but had no effect on human liver microsomal- or CYP1A2-catalyzed phenacetin dealkylation. Phenacetin 148-158 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 223-229 8466541-2 1993 The present study demonstrates that fluvoxamine is a very potent inhibitor of the high-affinity O-deethylation of phenacetin, which is catalysed by cytochrome P4501A2 (CYP1A2), in microsomes from three human livers. Phenacetin 114-124 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 148-166 8466541-2 1993 The present study demonstrates that fluvoxamine is a very potent inhibitor of the high-affinity O-deethylation of phenacetin, which is catalysed by cytochrome P4501A2 (CYP1A2), in microsomes from three human livers. Phenacetin 114-124 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 168-174 8095225-9 1993 Inhibition studies with caffeine, phenacetin, 17 beta-estradiol, and progesterone as inhibitors of the CYP1A1 and CYP1A2 catalyzed O-deethylation of 7-ethoxyresorufin suggest all compounds as possible substrates of CYP1A enzymes. Phenacetin 34-44 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 114-120 34442334-0 2021 Functional Characterization of 21 Rare Allelic CYP1A2 Variants Identified in a Population of 4773 Japanese Individuals by Assessing Phenacetin O-Deethylation. Phenacetin 132-142 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 47-53 1306118-6 1992 Moreover, CA was a competitive inhibitor of expressed CYP1A2 catalysed phenacetin O-deethylation, with the apparent Ki (0.080 mM) closely matching the apparent Km (0.082 mM) for CA 3-demethylation by the expressed enzyme. Phenacetin 71-81 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 54-60 34442334-3 2021 Therefore, we functionally characterized 21 novel CYP1A2 variants identified in 4773 Japanese individuals by determining the kinetic parameters of phenacetin O-deethylation. Phenacetin 147-157 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 50-56 33386627-7 2021 HYIpro-3-1 showed a typical pattern of competitive inhibition for CYP1A2-catalyzed phenacetin O-deethylation, based on the Lineweaver-Burk plot, with a Ki value of 0.05 muM in HLMs; the secondary plot also showed a linear pattern. Phenacetin 83-93 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 66-72 31480528-6 2019 For this purpose, the O-deethylation reaction of phenacetin was used for monitoring CYP1A2 enzyme activity, coumarin 7-hydroxylation for CYP2A6 enzyme activity, 6-alpha-hydroxylation of paclitaxel for CYP2C8 enzyme activity, and dextromethorphan O-demethylation for CYP2D6 enzyme activity. Phenacetin 49-59 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 84-90 33397254-2 2021 CYP1A2 metabolises many clinical drugs, such as phenacetin, caffeine, clozapine, tacrine, propranolol, and mexiletine. Phenacetin 48-58 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 0-6 32941854-11 2020 The presented findings may have clinical implications for the prediction of potential drug-drug interactions involving the asenapine-induced inhibition of metabolism of CYP1A2 substrates (e.g. caffeine, theophylline, melatonin, tricyclic antidepressants, phenacetin, propranolol) and iloperidone-induced inhibition of CYP3A4 substrates (e.g. antidepressants, benzodiazepines, atorvastatin, macrolide antibiotics, calcium channel antagonists). Phenacetin 255-265 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 169-175 31706005-2 2020 We found similar and stable CYP1A2 transcript and protein levels in both cell clones leading to specific enzyme activities of about 370 pmol paracetamol x min-1 x mg-1 protein analyzed by phenacetin conversion. Phenacetin 188-198 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 28-34 31239454-9 2019 However, phenacetin (CYP1A2) and chlorzoxazone (CYP2E1) are less selective for the specific enzyme, despite similarities in selectivity towards the different enzymes involved compared to humans. Phenacetin 9-19 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 21-27 28962866-6 2017 Furthermore, the present work found that DCO uncompetitively inhibited CYP1A2-mediated phenacetin O-deethylation with an IC50 value of 1.7muM and a Ki value of 2.6muM. Phenacetin 87-97 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 71-77 28992765-7 2018 The probes for testing CYP1A2 are phenacetin and caffeine while for CYP2C9 tolbutamide. Phenacetin 34-44 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 23-29 29989011-2 2018 The inhibition of CYP enzymatic activities by TQ was evaluated by incubating typical substrates (phenacetin for CYP1A2, tolbutamide for CYP2C9, dextromethorphan for CYP2D6, and testosterone for CYP3A4) with human liver microsomes and NADPH in the absence or presence of TQ (1, 10 and 100 microM). Phenacetin 97-107 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 112-118 29799514-0 2018 Increased Phenacetin Oxidation upon the L382V Substitution in Cytochrome P450 1A2 is Associated with Altered Substrate Binding Orientation. Phenacetin 10-20 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 62-81 29799514-1 2018 Leucine382 of cytochrome P450 1A2 (CYP1A2) plays an important role in binding and O-dealkylation of phenacetin, with the L382V mutation increasing substrate oxidation (Huang and Szklarz, 2010, Drug Metab. Phenacetin 100-110 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 14-33 29799514-1 2018 Leucine382 of cytochrome P450 1A2 (CYP1A2) plays an important role in binding and O-dealkylation of phenacetin, with the L382V mutation increasing substrate oxidation (Huang and Szklarz, 2010, Drug Metab. Phenacetin 100-110 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 35-41 29799514-5 2018 Therefore, in the current studies, we employed nuclear magnetic resonance (NMR) longitudinal (T1) relaxation measurements to investigate phenacetin binding orientations within the active site of CYP1A2 wild type (WT) and mutants. Phenacetin 137-147 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 195-201 27794450-6 2017 We further showed that hepatospheroids convert phenacetin (by CYP1A2) and testosterone (by CYP3A4) to their human-specific metabolites acetaminophen and 6beta-hydroxytestosterone with a predictive clearance rate of 0.011ml/h/106 cells and 0.021ml/h/106 cells respectively, according to first-order kinetics. Phenacetin 47-57 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 62-68 28468305-4 2017 Fargesin negligibly inhibited CYP1A2-catalyzed phenacetin O-deethylation, CYP2A6-catalyzed coumarin 7-hydroxylation, CYP2B6-catalyzed bupropion hydroxylation, and CYP2D6-catalyzed bufuralol 1"-hydroxylation at 100 muM in human liver microsomes. Phenacetin 47-57 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 30-36 25640685-2 2015 Phenacetin, dextromethorphan and testosterone, respectively, were used as CYP1A2, CYP2D6 and CYP3A4 substrates, and their metabolites were determined by validated HPLC methodologies. Phenacetin 0-10 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 74-80 26750984-8 2016 In addition, glycyrol showed selective inhibition of CYP1A1- and CYP1A2-catalyzed phenacetin O-deethylase activity with a half-maximal inhibitory concentration of (IC50) 1.3 and 16.1 muM in human recombinant cDNA-expressed CYP1A1 and CYP1A2, respectively. Phenacetin 82-92 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 65-71 27318879-5 2016 Then, this estimated CV was validated by predicting the CVs of AUC/Dose of tizanidine and phenacetin, which are mainly metabolized by CYP1A2 and have negligible renal clearance. Phenacetin 90-100 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 134-140 27037683-8 2016 CYP1A2 phenacetin metabolism was found to be higher in biochips after 5, 9 and 13 days of culture. Phenacetin 7-17 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 0-6 26490449-7 2015 (AL) exhibited the most potent inhibitory activities on CYP1A2-mediated phenacetin O-deethylation with mean IC50 of 0.04 and 0.36 microg/mL, respectively. Phenacetin 72-82 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 56-62 27128896-4 2016 Aschantin at 100 microM negligibly inhibited CYP1A2-mediated phenacetin O-de-ethylation, CYP2A6-mediated coumarin 7-hydroxylation, CYP2B6-mediated bupropion hydroxylation, and CYP2D6-mediated bufuralol 1"-hydroxylation. Phenacetin 61-71 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 45-51 26838175-8 2016 Cells co-expressing CYP1A2 and CPR were capable of catalyzing the conversion of the known CYP1A2 substrates 7-ethoxyresorufin, phenacetin and the artificial substrate luciferin-MultiCYP, which would not have been possible without interaction of both enzymes. Phenacetin 127-137 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 20-26 26838175-8 2016 Cells co-expressing CYP1A2 and CPR were capable of catalyzing the conversion of the known CYP1A2 substrates 7-ethoxyresorufin, phenacetin and the artificial substrate luciferin-MultiCYP, which would not have been possible without interaction of both enzymes. Phenacetin 127-137 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 90-96 26614990-3 2015 Phenacetin O-deethylation, omeprazole hydroxylation and nifedipine oxidation were used as selective substrates for CYP1A2, CYP2C19 and CYP3A4 activities, respectively. Phenacetin 0-10 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 115-121 26614990-7 2015 The inhibitory activities on CYP1A2-mediated phenacetin O-deethylation and CYP3A4-mediated nifedipine oxidation were moderate. Phenacetin 45-55 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 29-35 25936586-3 2015 CTXA reversibly inhibited the CYP1A2-catalyzed phenacetin O-deethylation, CYP2C8-catalyzed paclitaxel 6-hydroxylation, and CYP2C9-catalyzed diclofenac 4"-hydroxylation with half-maximal inhibitory concentration (IC50) values of 3.9, 4.7, and 2.9 microM, respectively. Phenacetin 47-57 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 30-36 26055126-8 2015 RESULTS: MA strongly inhibited CYP1A2-mediated phenacetin O-deethylation and CYP2B6-mediated bupropion hydroxylation with IC50 values of 3.0 and 3.9 microM, respectively, while it did not significantly inhibit other CYPs. Phenacetin 47-57 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 31-37 25456436-6 2014 RESULT: BER significantly increased the metabolism of midazolam, phenacetin and tolbutamide by inducing the CYP1A2 and 3A4 enzyme in a dose-dependent manner, the mRNA and protein expression of CYP1A2 and 3A4 were increased by berberine at 1000ng mL(-1). Phenacetin 65-75 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 108-114 25456436-6 2014 RESULT: BER significantly increased the metabolism of midazolam, phenacetin and tolbutamide by inducing the CYP1A2 and 3A4 enzyme in a dose-dependent manner, the mRNA and protein expression of CYP1A2 and 3A4 were increased by berberine at 1000ng mL(-1). Phenacetin 65-75 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 193-199 25456436-8 2014 CONCLUSION: BER increases the metabolism of cocktail drugs such as midazolam, phenacetin and tolbutamide by increasing the mRNA and protein expression of CYP1A2 and 3A4. Phenacetin 78-88 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 154-160 23153057-3 2013 The cocktail strategy (in situ incubation) was used to assess the induction of CYP1A2, CYP2B6, CYP2C9 and CYP3A4 by using the recommended probe substrate, i.e. phenacetin, bupropion, diclofenac and midazolam, respectively. Phenacetin 160-170 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 79-85 24194261-4 2014 PL strongly inhibited CYP1A2-mediated phenacetin O-deethylation with an IC50 value of 8.8 muM, as NADPH-independent inhibition, while other CYPs were not significantly inhibited. Phenacetin 38-48 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 22-28 24119207-7 2014 In this study, uremic serum was found to inhibit the CYP1A2-mediated metabolism of phenacetin to acetaminophen in a concentration-dependent and competitive manner. Phenacetin 83-93 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 53-59 29403890-2 2014 This method employed a cocktail of six probe substrates (i.e., phenacetin, amodiaquine, diclofenac, S-mephenytoin, dextromethorphan and midazolam for CYP1A2, 2C8, 2C9, 2C19, 2D6 and 3A4, respectively) as well as individual prototypical inhibitors of the six CYP enzymes in human liver microsomes under optimized incubation conditions. Phenacetin 63-73 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 150-156 24119207-4 2014 CYP1A2 and CYP2D6 activities were estimated by the phenacetin O-deethylation and methoprolol O-demethylation methods, respectively. Phenacetin 51-61 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 0-6 23263815-3 2012 Luotonin A selectively inhibited CYP1A2-catalyzed phenacetin O-deethylation with an IC(50) of 6.3 muM in HLMs, and strongly decreased CYP1A2-catalyzed phenacetin O-deethylation dose-dependently in HLMs, but did not inhibit it time-dependently. Phenacetin 50-60 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 33-39 23000442-3 2013 Incubation of isoform-specific substrate probes CYPs with mollugin (0-25muM) in HLM resulted in strong inhibition of CYP1A2-catalyzed phenacetin O-deethylation, showing IC(50) values of 1.03 and 3.55muM without and with pre-incubation, respectively. Phenacetin 134-144 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 117-123 23263815-3 2012 Luotonin A selectively inhibited CYP1A2-catalyzed phenacetin O-deethylation with an IC(50) of 6.3 muM in HLMs, and strongly decreased CYP1A2-catalyzed phenacetin O-deethylation dose-dependently in HLMs, but did not inhibit it time-dependently. Phenacetin 151-161 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 134-140 22949628-9 2012 The NMR findings are thus consistent with our kinetic and stoichiometric results, providing a likely molecular basis for more efficient metabolism of phenacetin by CYP1A2. Phenacetin 150-160 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 164-170 22949628-0 2012 Preferred binding orientations of phenacetin in CYP1A1 and CYP1A2 are associated with isoform-selective metabolism. Phenacetin 34-44 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 59-65 22949628-7 2012 The subsequent NMR longitudinal (T1) relaxation studies with the substrate phenacetin and its product acetaminophen showed that both compounds displayed similar binding orientations within the active site of CYP1A1 and CYP1A2. Phenacetin 75-85 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 219-225 22949628-8 2012 However, the distance between the OCH2 protons of the ethoxy group (site of phenacetin O-deethylation) and the heme iron was 1.5 A shorter in CYP1A2 than in CYP1A1. Phenacetin 76-86 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 142-148 22940574-0 2012 Metabolic activation by human arylacetamide deacetylase, CYP2E1, and CYP1A2 causes phenacetin-induced methemoglobinemia. Phenacetin 83-93 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 69-75 22940574-12 2012 In conclusion, we found that the hydrolysis by AADAC and subsequent metabolism by CYP1A2 and CYP2E1 play predominant roles in phenacetin-induced methemoglobinemia. Phenacetin 126-136 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 82-88 20501911-3 2010 The kinetics of metabolite formation from phenacetin, tolbutamide, and alprazolam and midazolam, selected as substrates probes for CYP1A2, CYP2C9, and CYP3A4, respectively, were characterized in this in vitro system. Phenacetin 42-52 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 131-137 23331088-8 2012 Similarly, CYP1A2 activity toward phenacetin correlated with formation of R-6 and 7-hydroxywarfarin such that R-8-hydroxywarfarin seems unique to CYP2C19 and possibly a biomarker. Phenacetin 34-44 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 11-17 22305191-4 2012 PSP (1.25-20muM) dose-dependently decreased CYP1A2-mediated metabolism of phenacetin to paracetamol (IC(50) 19.7muM) and CYP3A4-mediated metabolism of testosterone to 6beta-hydroxytestosterone (IC(20) 7.06muM). Phenacetin 74-84 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 44-50 21091898-10 2010 CONCLUSION: Monitoring cytochrome P450 1A2 (CYP450 1A2)-mediated phenacetin metabolism is a simple and efficient method for evaluating human LRF. Phenacetin 65-75 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 23-42 21091898-10 2010 CONCLUSION: Monitoring cytochrome P450 1A2 (CYP450 1A2)-mediated phenacetin metabolism is a simple and efficient method for evaluating human LRF. Phenacetin 65-75 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 44-54 20877236-4 2010 Eupatilin and jaceosidin potently inhibited CYP1A2-catalyzed phenacetin O-deethylation with 50% inhibitory concentration (IC(50)) values of 9.4 microM and 5.3 microM, respectively, and CYP2C9-catalyzed diclofenac 4-hydroxylation with IC(50) values of 4.1 microM and 10.2 microM, respectively. Phenacetin 61-71 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 44-50 21825116-1 2011 In this study, we report the effect of dimethyl sulfoxide (DMSO), acetonitrile, and methanol on the CYP1A2-mediated metabolism of phenacetin in human liver microsomes. Phenacetin 130-140 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 100-106 21825116-2 2011 Phenacetin O-deethylation is the preferred probe reaction for CYP1A2, in which the metabolite, acetaminophen, is quantified using liquid chromatography-tandem mass spectrometry. Phenacetin 0-10 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 62-68 21825116-3 2011 DMSO was found to inhibit CYP1A2-mediated phenacetin O-deethylation even at low concentrations (0.1%). Phenacetin 42-52 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 26-32 21222608-3 2011 Pooled human liver microsome was used for investigating the effects on cytochrome P450 1A2 (CYP1A2) catalytic activities by using phenacetin as a substrate. Phenacetin 130-140 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 71-90 21222608-3 2011 Pooled human liver microsome was used for investigating the effects on cytochrome P450 1A2 (CYP1A2) catalytic activities by using phenacetin as a substrate. Phenacetin 130-140 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 92-98 20609070-4 2010 A probe substrate, phenacetin, was used to index the activity of CYP1A2. Phenacetin 19-29 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 65-71 20528625-4 2010 Metabolism of phenacetin to paracetamol and dextromethorphan to dextrorphan (metabolic reactions catalyzed by CYP 1A2 and 2D6 in humans respectively) were observed in the zebrafish larvae. Phenacetin 14-24 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 110-125 20335269-0 2010 Significant increase in phenacetin oxidation on L382V substitution in human cytochrome P450 1A2. Phenacetin 24-34 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 76-95 19906068-2 2010 In this study phenacetin, a probe drug (1 g for men and 0.85 g for women orally), was applied for the detection of sulfotransferase 1A1 (SULT1A1) and cytochrome P4501A2 (CYP1A2) activities in 82 healthy participants and 148 HCC, 106 cirrhosis, and 41 chronic hepatitis B patients. Phenacetin 14-24 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 150-168 19906068-2 2010 In this study phenacetin, a probe drug (1 g for men and 0.85 g for women orally), was applied for the detection of sulfotransferase 1A1 (SULT1A1) and cytochrome P4501A2 (CYP1A2) activities in 82 healthy participants and 148 HCC, 106 cirrhosis, and 41 chronic hepatitis B patients. Phenacetin 14-24 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 170-176 18834363-2 2008 Phenacetin O-de-ethylation is a marker for CYP1A2 activity. Phenacetin 0-10 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 43-49 21086794-1 2010 BACKGROUND: The cytochrome P450 1A2 (CYP1A2) gene encodes one of the most important enzymes of the Phase I drug metabolism, which is involved in the metabolism of many lipophilic xenobiotics, such as haloperidol, theophylline, phenacetine, and others. Phenacetin 227-238 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 16-35 21086794-1 2010 BACKGROUND: The cytochrome P450 1A2 (CYP1A2) gene encodes one of the most important enzymes of the Phase I drug metabolism, which is involved in the metabolism of many lipophilic xenobiotics, such as haloperidol, theophylline, phenacetine, and others. Phenacetin 227-238 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 37-43 19904008-8 2009 Hence, taking account of CYP1A2 contribution to the metabolism of endogenous substances (steroids), drugs (xanthine derivatives, phenacetin, propranolol, imipramine, phenothiazine neuroleptics, clozapine) and carcinogenic compounds, the inhibition of CYP1A2 by perazine may be of physiological, pharmacological and toxicological importance. Phenacetin 129-139 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 25-31 19204080-6 2009 6-MNA activity correlated strongly with both CYP1A2-mediated phenacetin O-deethylation activity and CYP1A2 protein content (r = 0.85 and 0.74, respectively; p < 0.0001 for both). Phenacetin 61-71 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 45-51 18819885-3 2008 After 15 min of culture, the substrates (testosterone for CYP3A4 and phenacetin for CYP1A2) were added and incubated for another 20 min. Phenacetin 69-79 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 84-90 18573860-9 2008 In conclusion, tacrine, ethoxyresorufin, and phenacetin are probe substrates for CYP1A2 not only in humans but also in dogs. Phenacetin 45-55 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 81-87