Relevant bibliographies by topics / CYP2B6

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Academic literature on the topic 'CYP2B6'

Author: Grafiati
Published: 4 June 2021
Last updated: 29 January 2023

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Journal articles on the topic "CYP2B6"

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Ma, Wenjuan, Wei Wang, Xuhua Huang, Guangzhe Yao, Qi Jia, Jiayuan Shen, Huizi Ouyang, Yanxu Chang, and Jun He. "HPLC-MS/MS Analysis of Aconiti Lateralis Radix Praeparata and Its Combination with Red Ginseng Effect on Rat CYP450 Activities Using the Cocktail Approach." Evidence-Based Complementary and Alternative Medicine 2020 (March 9, 2020): 1–12. http://dx.doi.org/10.1155/2020/8603934.

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Red ginseng is often combined with Aconiti Lateralis Radix Praeparata to reduce alkaloids-related toxicity of the latter. Such herb-pairing also results in better therapeutic effect in heart failure, as compared to the singular use of either herb. The purpose of this study was to investigate the effect of Aconiti Lateralis Radix Praeparata and its combination with red ginseng on the activities of CYP450 enzymes in rats. A sensitive and reliable HPLC-MS/MS method was established and validated for the simultaneous determination of eight probe drugs, phenacetin (CYP1A2), tolbutamide (CYP2C9), omeprazole (CYP2C19), dextromethorphan (CYP2D6), dapsone (CYP3A4), 7-hydroxycoumarin (CYP2A6), bupropion (CYP2B6), and amodiaquine (CYP2C8), in rat plasma using diazepam as internal standard (IS). The chromatographic separation was performed on a Waters XBridge™ C18 column (2.1 mm × 100 mm, 3.5 μm) using a gradient elution with the mobile phase consisting of acetonitrile and water (containing 0.1% formic acid) at a flow rate of 0.3 mL/min. The method was successfully applied in evaluating the effect of Aconiti Lateralis Radix Praeparata and red ginseng on the activities of CYP450 enzymes. The pharmacokinetic results of the eight probe drugs suggested that Aconiti Lateralis Radix Praeparata may inhibit the activity of CYP2A6, CYP2C19, CYP2B6, CYP1A2, CYP3A4, and CYP2C9 enzymes in rats. Comparison between the two groups, Aconiti Lateralis Radix Praeparata combined with red ginseng and Aconiti Lateralis Radix Praeparata, indicated that red ginseng may inhibit the activity of CYP2D6 and CYP2B6 enzymes while inducing the activity of CYP1A2, CYP3A4, and CYP2C9 enzymes.
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Lim, Sharoen Yu Ming, Mustafa Ahmed Alshagga, Mohammed Abdullah Alshawsh, Chin Eng Ong, and Yan Pan. "In vitro effects of 95% khat ethanol extract (KEE) on human recombinant cytochrome P450 (CYP)1A2, CYP2A6, CYP2B6, CYP2C8, CYP2C19, CYP2E1, CYP2J2 and CYP3A5." Drug Metabolism and Personalized Therapy 37, no. 1 (August 17, 2021): 55–67. http://dx.doi.org/10.1515/dmpt-2021-1000196.

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Abstract Objectives Khat, a natural amphetamine-like psychostimulant plant, are widely consumed globally. Concurrent intake of khat and xenobiotics may lead to herb-drug interactions and adverse drug reactions (ADRs). This study is a continuation of our previous study, targeted to evaluate the in vitro inhibitory effects of khat ethanol extract (KEE) on human cytochrome (CYP) 1A2, CYP2A6, CYP2B6, CYP2C8, CYP2C19, CYP2E1, CYP2J2, and CYP3A5, major human drug metabolizing enzymes. Methods In vitro fluorescence enzyme assays were employed to assess CYPs inhibition with the presence and absence of various KEE concentrations. Results KEE reversibly inhibited CYP2A6, CYP2B6, CYP2C8, CYP2C19, CYP2E1, CYP2J2 and CYP3A5 but not CYP1A2 with IC50 values of 25.5, 99, 4.5, 21, 27, 17, and 10 μg/mL respectively. No irreversible inhibition of KEE on all the eight CYPs were identified. The Ki values of CYP2A6, CYP2B6, CYP2C8, CYP2C19, CYP2E1, CYP2J2 and CYP3A5 were 20.9, 85, 4.8, 18.3, 59.3, 3, and 21.7 μg/mL, respectively. KEE inhibited CYP2B6 via competitive or mixed inhibition; CYP2E1 via un-competitive or mixed inhibition; while CYP2A6, CYP2C8, CYP2C19, CYP2J2 and CYP3A5 via non-competitive or mixed inhibition. Conclusions Caution should be taken by khat users who are on medications metabolized by CYP2A6, CYP2B6, CYP2C8, CYP2C19, CYP2E1, CYP2J2, and CYP3A5.
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Claw, Katrina G., Julie A. Beans, Seung-Been Lee, Jaedon P. Avey, Patricia A. Stapleton, Steven E. Scherer, Ahmed El-Boraie, et al. "Pharmacogenomics of Nicotine Metabolism: Novel CYP2A6 and CYP2B6 Genetic Variation Patterns in Alaska Native and American Indian Populations." Nicotine & Tobacco Research 22, no. 6 (June 25, 2019): 910–18. http://dx.doi.org/10.1093/ntr/ntz105.

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Abstract Introduction Alaska Native and American Indian (AN/AI) populations have higher tobacco use prevalence than other ethnic/racial groups. Pharmacogenetic testing to tailor tobacco cessation treatment may improve cessation rates. This study characterized polymorphic variations among AN/AI people in genes associated with metabolism of nicotine and drugs used for tobacco cessation. Methods Recruitment of AN/AI individuals represented six subgroups, five geographic subgroups throughout Alaska and a subgroup comprised of AIs from the lower 48 states living in Alaska. We sequenced the CYP2A6 and CYP2B6 genes to identify known and novel gain, reduced, and loss-of-function alleles, including structural variation (eg, gene deletions, duplications, and hybridizations). Results Variant allele frequencies differed substantially between AN/AI subgroups. The gene deletion CYP2A6*4 and reduced function CYP2A6*9 alleles were found at high frequency in Northern/Western subgroups and in Lower 48/Interior subgroups, respectively. The reduced function CYP2B6*6 allele was observed in all subgroups and a novel, predicted reduced function CYP2B6 variant was found at relatively high frequency in the Southeastern subgroup. Conclusions Diverse CYP2A6 and CYP2B6 variation among the subgroups highlight the need for comprehensive pharmacogenetic testing to guide tobacco cessation therapy for AN/AI populations. Implications Nicotine metabolism is largely determined by CYP2A6 genotype, and variation in CYP2A6 activity has altered the treatment success in other populations. These findings suggest pharmacogenetic-guided smoking cessation drug treatment could provide benefit to this unique population seeking tobacco cessation therapy.
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Hashemi-Soteh, Mohammad Bagher, Elaheh Hosseini, Shokoufeh Fazelnia, Faramarz Ghasemian-Sorbeni, Sara Madahian, and Mohammad Reza Shiran. "Frequencies of CYP2B6∗4,∗5, and ∗6 Alleles within an Iranian Population (Mazandaran)." Genetics Research 2021 (December 2, 2021): 1–6. http://dx.doi.org/10.1155/2021/8703812.

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Background. The human CYP2B subfamily consists of one functional gene (CYP2B6) and one pseudogene (CYP2B7P). Cytochrome P450 2B6 (CYP2B6) is a highly polymorphic enzyme that shows marked interindividual and interethnic variations. Currently, 38 alleles have been described, and some of the allelic variants have been associated with low enzyme activity. The aim of this study was to investigate the frequencies of CYP2B6∗4, CYP2B6∗5, and CYP2B6∗6 alleles in the Mazani ethnic group among Iranian Population. Methods. The study was conducted in 289 unrelated healthy volunteers. DNA was extracted from peripheral blood and analyzed by the PCR-RFLP protocol. The PCR product was digested with restriction enzymes and then separated using agarose gel electrophoresis. Results. The frequency of CYP2B6∗4, CYP2B6∗5, and CYP2B6∗6 in this study was 34.60%, 7.26%, and 34.54%, respectively. Conclusion. The frequency of the CYP2B6∗4 allele in the Mazani ethnic group was much higher (34.60%) than other population. The frequency of CYP2B6∗6 (34.54%) also was higher than its frequency in other previously reported population. But the frequency of CYP2B6∗5 in this study was lower than expected. These results will be useful in understanding the ethnic diversity in Iranian population and offer a preliminary basis for more rational use of drugs that are substrates for CYP2B6 in this population.
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Jeong, Seongwook, Phuong D. Nguyen, and Zeruesenay Desta. "Comprehensive In Vitro Analysis of Voriconazole Inhibition of Eight Cytochrome P450 (CYP) Enzymes: Major Effect on CYPs 2B6, 2C9, 2C19, and 3A." Antimicrobial Agents and Chemotherapy 53, no. 2 (November 24, 2008): 541–51. http://dx.doi.org/10.1128/aac.01123-08.

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ABSTRACT Voriconazole is an effective antifungal drug, but adverse drug-drug interactions associated with its use are of major clinical concern. To identify the mechanisms of these interactions, we tested the inhibitory potency of voriconazole with eight human cytochrome P450 (CYP) enzymes. Isoform-specific probes were incubated with human liver microsomes (HLMs) (or expressed CYPs) and cofactors in the absence and the presence of voriconazole. Preincubation experiments were performed to test mechanism-based inactivation. In pilot experiments, voriconazole showed inhibition of CYP2B6, CYP2C9, CYP2C19, and CYP3A (half-maximal [50%] inhibitory concentrations, <6 μM); its effect on CYP1A2, CYP2A6, CYP2C8, and CYP2D6 was marginal (<25% inhibition at 100 μM voriconazole). Further detailed experiments with HLMs showed that voriconazole is a potent competitive inhibitor of CYP2B6 (Ki < 0.5), CYP2C9 (Ki = 2.79 μM), and CYP2C19 (Ki = 5.1 μM). The inhibition of CYP3A by voriconazole was explained by noncompetitive (Ki = 2.97 μM) and competitive (Ki = 0.66 μM) modes of inhibition. Prediction of the in vivo interaction of voriconazole from these in vitro data suggests that voriconazole would substantially increase the exposure of drugs metabolized by CYP2B6, CYP2C9, CYP2C19, and CYP3A. Clinicians should be aware of these interactions and monitor patients for adverse effects or failure of therapy.
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Heintz, Melissa M., Jazmine A. Eccles, Emily M. Olack, Kristal M. Maner-Smith, Eric A. Ortlund, and William S. Baldwin. "Human CYP2B6 produces oxylipins from polyunsaturated fatty acids and reduces diet-induced obesity." PLOS ONE 17, no. 12 (December 15, 2022): e0277053. http://dx.doi.org/10.1371/journal.pone.0277053.

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Multiple factors in addition to over consumption lead to obesity and non-alcoholic fatty liver disease (NAFLD) in the United States and worldwide. CYP2B6 is the only human detoxification CYP whose loss is associated with obesity, and Cyp2b-null mice show greater diet-induced obesity with increased steatosis than wildtype mice. However, a putative mechanism has not been determined. LC-MS/MS revealed that CYP2B6 metabolizes PUFAs, with a preference for metabolism of ALA to 9-HOTrE and to a lesser extent 13-HOTrE with a preference for metabolism of PUFAs at the 9- and 13-positions. To further study the role of CYP2B6 in vivo, humanized-CYP2B6-transgenic (hCYP2B6-Tg) and Cyp2b-null mice were fed a 60% high-fat diet for 16 weeks. Compared to Cyp2b-null mice, hCYP2B6-Tg mice showed reduced weight gain and metabolic disease as measured by glucose tolerance tests, however hCYP2B6-Tg male mice showed increased liver triglycerides. Serum and liver oxylipin metabolite concentrations increased in male hCYP2B6-Tg mice, while only serum oxylipins increased in female hCYP2B6-Tg mice with the greatest increases in LA oxylipins metabolized at the 9 and 13-positions. Several of these oxylipins, specifically 9-HODE, 9-HOTrE, and 13-oxoODE, are PPAR agonists. RNA-seq data also demonstrated sexually dimorphic changes in gene expression related to nuclear receptor signaling, especially CAR > PPAR with qPCR suggesting PPARγ signaling is more likely than PPARα signaling in male mice. Overall, our data indicates that CYP2B6 is an anti-obesity enzyme, but probably to a lesser extent than murine Cyp2b’s. Therefore, the inhibition of CYP2B6 by xenobiotics or dietary fats can exacerbate obesity and metabolic disease potentially through disrupted PUFA metabolism and the production of key lipid metabolites.
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Saiz-Rodríguez, Miriam, Dolores Ochoa, Manuel Román, Pablo Zubiaur, Dora Koller, Gina Mejía, and Francisco Abad-Santos. "Involvement of CYP2D6 and CYP2B6 on tramadol pharmacokinetics." Pharmacogenomics 21, no. 10 (July 2020): 663–75. http://dx.doi.org/10.2217/pgs-2020-0026.

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This study included 24 healthy volunteers who received a single 37.5 mg oral dose of tramadol. We analyzed 18 polymorphisms within CYP2D6, CYP2B6, CYP3A, COMT, ABCB1, SLC22A1 and OPRM1 genes by quantitative PCR, to study whether these polymorphisms affect its pharmacokinetics, pharmacodynamics and safety. CYP2D6 intermediate metabolizers (n = 6) showed higher tramadol plasma concentrations and lower clearance compared with normal and ultrarapid metabolizers. CYP2B6 G516T T/T (n = 2) genotype was also associated to higher tramadol plasma levels. No other polymorphism affected tramadol pharmacokinetics. Three volunteers experienced a prolonged QTc not associated with the genetic variants studied or altered phamacokinetic parameters. The correlation of CYP2B6 genotype with higher tramadol concentrations is remarkable since its influence on its elimination is also relevant and has been less studied to date. However, given our small sample size, it is important to interpret our results with caution.
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Li, Lang, Silvana Borges, Robarge D. Jason, Changyu Shen, Zeruesenay Desta, and David Flockhart. "A Penalized Mixture Model Approach in Genotype/Phenotype Association Analysis for Quantitative Phenotypes." Cancer Informatics 9 (January 2010): CIN.S3493. http://dx.doi.org/10.4137/cin.s3493.

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A mixture normal model has been developed to partition genotypes in predicting quantitative phenotypes. Its estimation and inference are performed through an EM algorithm. This approach can conduct simultaneous genotype clustering and hypothesis testing. It is a valuable method for predicting the distribution of quantitative phenotypes among multi-locus genotypes across genes or within a gene. This mixture model's performance is evaluated in data analyses for two pharmacogenetics studies. In one example, thirty five CYP2D6 genotypes were partitioned into three groups to predict pharmacokinetics of a breast cancer drug, Tamoxifen, a CYP2D6 substrate (p-value = 0.04). In a second example, seventeen CYP2B6 genotypes were categorized into three clusters to predict CYP2B6 protein expression (p-value = 0.002). The biological validities of both partitions are examined using established function of CYP2D6 and CYP2B6 alleles. In both examples, we observed genotypes clustered in the same group to have high functional similarities. The power and recovery rate of the true partition for the mixture model approach are investigated in statistical simulation studies, where it outperforms another published method.
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Veiga, M. I., S. Asimus, P. E. Ferreira, J. P. Martins, I. Cavaco, V. Ribeiro, T. N. Hai, et al. "Pharmacogenomics of CYP2A6, CYP2B6, CYP2C19, CYP2D6, CYP3A4, CYP3A5 and MDR1 in Vietnam." European Journal of Clinical Pharmacology 65, no. 4 (November 1, 2008): 355–63. http://dx.doi.org/10.1007/s00228-008-0573-8.

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Shaheen, Magda, Amira Brown, Deyu Pan, and Katrina Schrode. "3547 Relationship between smoking and alcohol use status: variations in candidate genes associated with addiction and successful quitting smoking." Journal of Clinical and Translational Science 3, s1 (March 2019): 52. http://dx.doi.org/10.1017/cts.2019.125.

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OBJECTIVES/SPECIFIC AIMS: Previous studies showed that 52% of smokers were unsuccessful in quitting smoking. Smoking in alcoholics is 2-3 times that of the general population with 50%-80% of alcoholics smoking regularly. Studies have linked several genetic variants to addiction. We examined the relation between successful quitting smoking, alcohol use, and genetic data for CYP2A6, CYP2B6, DRD2, DRD1 and GABRB1 alleles. METHODS/STUDY POPULATION: We analyzed data from NHANES III 1988-1994 for socioeconomic factors, physical activity, body mass index (BMI), alcohol status, successful quit smoking, and genetic data for CYP2A6, CYP2B6, DRD2, DRD1 and GABRB1 alleles. Multivariate logistic regression was used to examine the association between successful quit smoking and genotypes adjusting for other variables. Data were analyzed using SAS version 9.3 (design & weight). RESULTS/ANTICIPATED RESULTS: Of the 2,269 smokers, 57% were current smokers, 35% were heavy drinkers, 24% were both smokers & heavy drinkers and 41% successfully quitted smoking. Successfully quit smoking was associated with CYP2A6 (rs28399433-TG) (adjusted odds ratio (AOR) = 3.6, 95% confidence interval (CI) = 1.1-11.9, p = 0.03), CYP2B6 (rs2279343-AA and AG) (AOR = 2.3, 95%CI = 1.5-3.5, p = 0.0003 for AA & AOR = 2.3, 95%CI = 1.2-4.2, p = 0.01 for AG) and DRD1 (rs4532-AA) (AOR = 2.2, 95%CI = 1.01-4.6, p = 0.04). Among heavy drinkers, those with CYP2A6 (rs28399433-TG) and CYP2B6 (rs2279343-AA and AG) were more likely to successfully quit smoking and those with CYP2A6 (rs5031017-GG) and GABRB1 (rs1442099-CC) were less likely to successfully quit smoking (p<0.05). DISCUSSION/SIGNIFICANCE OF IMPACT: We concluded that while rs28399433-TG, rs2279343-AA & AG positively impacted the success to quit smoking, rs5031017-GG & rs1442099-CC negatively impacted the success in quitting smoking both overall and specifically in heavy drinker smokers.
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Dissertations / Theses on the topic "CYP2B6"

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Wang, Jue. "Regulation and polymorphism of CYP2A6, CYP2B6 and CYP2E1 : functional and clinical aspects /." Stockholm, 2006. http://diss.kib.ki.se/2006/91-7140-650-6/.

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Wang, Haoyi. "ORGANIZATION AND EVOLUTION OF THE CYP2A-T GENE SUBFAMILY CLUSTER IN RODENTS, AND A COMPARISON TO THE SYNTENIC HUMAN CLUSTER." Miami University / OhioLINK, 2003. http://rave.ohiolink.edu/etdc/view?acc_num=miami1050615100.

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Hofmann, Marco Hans. "Microarray and molecular genetic analysis of aberrant splicing in human drug metabolizing cytochromes P450 CYP2D6 and CYP2B6." [S.l. : s.n.], 2008. http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-36010.

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Uwimana, Eric. "Probing the PCB metabolome: metabolism of chiral and non-chiral polychlorinated biphenyls to chiral hydroxylated metabolites in humans and rats." Diss., University of Iowa, 2018. https://ir.uiowa.edu/etd/6657.

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Polychlorinated biphenyls (PCBs) continue to pose a health concern because of their predominance in the diet and air as well as in environmental samples and humans. PCB congeners with 3 or 4 chlorine substituents in ortho position have been associated with neurodevelopmental disorders. Hydroxylated metabolites (OH-PCBs) of these PCBs are also potentially toxic to the developing brain. Metabolism studies have mainly focused on animal models. However, preliminary data from this dissertation work have revealed PCB metabolism differences between laboratory animal models and humans in terms of metabolite profiles, chiral signatures. More concerning, biotransformation of chiral PCBs is poorly investigated in humans. The objective of this dissertation research was to study the biotransformation of chiral and prochiral PCBs to chiral hydroxylated metabolites in humans and rats and to identify individual human P450 enzymes involved in the metabolism of these PCBs. I chose chiral PCB congeners 2,2',3,4',6-pentachlorobiphenyl (PCB 91); 2,2',3,5',6-pentachlorobiphenyl (PCB 95), 2,2',3,3',4,6'-hexachlorobiphenyl (PCB 132) and 2,2',3,3',6,6'-hexachlorobiphenyl (PCB 136) for this investigation because they are environmentally relevant and their metabolism has been studied in rodents and other laboratory animal species (Kania-Korwel et al., 2016a). Prochiral PCB congeners 2,2′,4,6′-tetrachlorobiphenyl (PCB 51) and 2,2′,4,5,6′-pentachlorobiphenyl (PCB 102) were selected because their considerable presence in technical PCB mixtures. To test the hypothesis that P450 enzyme and species differences mediate the congener-specific enantioselective metabolism of chiral PCBs to hydroxylated metabolites, I sought to establish structure-metabolism relationships by studying the enantioselective metabolism of structurally diverse chiral PCBs by human liver microsomes (HLMs). Racemic PCB 91, PCB 95 and PCB 132 were incubated in vitro with pooled or individual donor HLMs at 37 °C, and levels and chiral signatures of the parent PCB and its hydroxylated metabolites were determined by high-resolution gas chromatography equipped with time-of-flight mass spectrometry (GC/TOF-MS) or electron capture detection (GC-ECD). Hydroxylated metabolites formed were identified and metabolic schemes for these PCBs proposed. I found inter-individual differences in the formation of OH-PCBs by individual donor HLMs. Comparison of the metabolite profiles of PCB 91, PCB 95, PCB 132 and PCB 136 (PCB 136 metabolism by HLMs was investigated by other researchers) revealed congener-specific differences in the oxidation of PCBs by human cytochrome P450 enzymes. PCB 91 and PCB 132 were mainly hydroxylated in meta position, with the 1,2-shift metabolites being the major metabolites formed from both PCB congeners by HLMs. In contrast, PCB 95 and PCB 136 were primarily hydroxylated in the para position. Moreover, we determined human P450 isoforms involved in the metabolism of neurotoxic PCBs using in silico and in vitro approaches. In silico predictions suggested that chiral PCBs are metabolized by CYP1A2, CYP2A6, CYP2B6, CYP2E1, and CYP3A4. Experimentally we found that CYP2A6, CYP2B6 and to a minor extent CYP2E1 were the enzymes involved in the metabolism of these chiral PCBS. We also investigated nonchiral sources of chiral OH-PCBs by studying the P450- and species-dependent biotransformation of prochiral PCB 51 and PCB 102 to chiral OH-PCB metabolites. Prochiral PCB 51 and PCB 102 were incubated with liver microsomes prepared from male Sprague-Dawley rats pretreated with various inducers of P450 enzymes including phenobarbital (PB), dexamethasone (DEX), isoniazid (INH), β-naphthoflavone (BNF), clofibric acid (CFA) or corn oil (CO); and untreated male cynomolgus monkeys, Hartley albino guinea pigs, New Zealand rabbits, golden Syrian hamsters; and untreated female Beagle dogs. PCB 51 and PCB 102 were metabolized to 2,2',4,6'-tetrachlorobiphenyl-3'-ol (OH-PCB 51) and 2,2',4,5,6'-pentachlorobiphenyl-3'-ol (OH-PCB 102), respectively. The formation of both metabolites was P450 isoforms- and species-dependent. Moreover, OH-PCB 51 and OH-PCB 102 were chiral and were formed enantioselectively in all microsomes investigated. Taken together, my findings demonstrate (1) considerable inter-individual variability in the congener-specific metabolism of PCBs to OH-PCBs; (2) the enantioselective formation of OH-PCBs by human CYP2A6, CYP2B6, and CYP2E1; and (3) that chiral PCB metabolites are formed enantioselectively from prochiral PCB congeners. Interestingly, the metabolism of PCBs by CYP2A6 appears to involve arene oxide intermediates, as suggested by the formation of 1,2-shift products as major metabolites of PCB 91 and PCB 132. In contrast, 1,2-shift products are minor PCB metabolites formed in rodents. Therefore extrapolation of hepatic metabolism across species may not be consistent and these differences should be considered in future toxicity and risk assessment studies.
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Blievernicht, Julia. "Massenspektrometrische Diagnostik von CYP2B6 Polymorphismen phänotypische Ausprägung in Lebergewebe und klinische Bedeutung /." [S.l. : s.n.], 2008. http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-36079.

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Almeida, Adriana Ávila de. "Expressão dos genes CYP1A1, CYP1B1, CYP2A6 e CYP2E1 em fumantes com câncer bucal. /." São José dos Campos, 2018. http://hdl.handle.net/11449/153357.

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Orientador: Janete Dias Almeida
Coorientador: Celina Faig Lima Carta
Banca: Emília Ângela Lo Schiavo Arisawa
Banca: Ana Lia Anbinder
Banca: Alberto José de Araújo
Banca: José Benedito Oliveira Amorim
Resumo: Os carcinógenos do tabaco estão relacionados a diversos tipos de câncer incluindo o carcinoma de células escamosas (CCE) bucal. Aliado ao álcool, o tabaco contribui para o desfecho desfavorável destes casos. A susceptibilidade individual ao câncer pode estar relacionada a expressão das enzimas que metabolizam tais carcinógenos. O objetivo deste trabalho é avaliar a expressão dos genes CYP1A1, CYP1B1, CYP2A6 e CYP2E1 no CCE bucal por meio de qPCR. Foram coletadas amostras de 32 indivíduos com CCE e de 15 controles submetidos a cirurgias bucais por lesões benignas. Foram constituídos quatro grupos: Grupo CCE fumante (n=26), Grupo CCE não fumante (n=6), Grupo controle fumante (n=9) e Grupo controle não fumante (n=6). O Teste de Fagerström para Dependência a Cigarros (TFDC) foi usado para avaliar a dependência nicotínica (DN) e AUDIT para avaliação do consumo de etílicos. Houve diminuição da expressão do gene CYP1B1 nos casos de CCE comparados aos controles. Foram encontradas diferenças estaticamente significativas de expressão gênica de CYP1B1 entre os Grupos CCE fumante e controle fumante (p=0,0018), Grupo CCE não fumante e controle não fumante (p=0,0079) e CCE fumante com CCE não fumante (p=0,0385) e entre os quatro grupos (p<0,0001). Houve diminuição da expressão do CYP2A6 no Grupo CCE fumante em relação ao Grupo controle, mas apenas um paciente do Grupo controle expressou este gene. Houve aumento da expressão de CYP2E1 entre os Grupos CCE fumante e controle fumante (p=0,0424... (Resumo completo, clicar acesso eletrônico abaixo)
Abstract: Tobacco carcinogens are related to various types of cancer, including oral squamous cell carcinoma (OSCC). Allied to alcohol, tobacco contributes to the unfavorable outcome of the cases. Individual cancer susceptibility may be related to an expression of the enzymes that metabolize such carcinogens. The aim of this work is to evaluate the expression of the genes CYP1A1, CYP1B1, CYP2A6 and CYP2E1 on OSCC by qPCR. Samples were collected from 32 individuals with OSCC and 15 controls submitted to oral surgeries due to benign lesions. There were four groups: Smoker SCC group (n = 26), nonsmoker SCC group (n = 6), Smoker control group (n = 9) and nonsmoker control group (n = 6). The Fagerström Test for Cigarette Dependence (TFCD) was used to evaluate nicotinic dependence (ND) and AUDIT for the evaluation of alcohol consumption. There was a decrease in CYP1B1 gene expression in cases of SCC compared to controls. (P = 0.0018); smoker CCE and non-smoker control (p = 0.0079); smoker SCC with nonsmoker SCC (p = 0.0385) and between the four groups (p <0.0001). There was a decreased expression in CYP2A6 in the smoker SCC Group compared to the control group, but only one control group patient expressed this gene. There was an increased expression of CYP2E1 between the smoking and nonsmoking SCC groups (p = 0.0424). In conclusion, large interindividual variability was found in the study of the expression of the genes studied. There was greater expression of CYP1A1 and CYP2E1 in samples from... (Complete abstract click electronic access below)
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Almeida, Adriana Ávila de [UNESP]. "Expressão dos genes CYP1A1, CYP1B1, CYP2A6 e CYP2E1 em fumantes com câncer bucal." Universidade Estadual Paulista (UNESP), 2018. http://hdl.handle.net/11449/153357.

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Os carcinógenos do tabaco estão relacionados a diversos tipos de câncer incluindo o carcinoma de células escamosas (CCE) bucal. Aliado ao álcool, o tabaco contribui para o desfecho desfavorável destes casos. A susceptibilidade individual ao câncer pode estar relacionada a expressão das enzimas que metabolizam tais carcinógenos. O objetivo deste trabalho é avaliar a expressão dos genes CYP1A1, CYP1B1, CYP2A6 e CYP2E1 no CCE bucal por meio de qPCR. Foram coletadas amostras de 32 indivíduos com CCE e de 15 controles submetidos a cirurgias bucais por lesões benignas. Foram constituídos quatro grupos: Grupo CCE fumante (n=26), Grupo CCE não fumante (n=6), Grupo controle fumante (n=9) e Grupo controle não fumante (n=6). O Teste de Fagerström para Dependência a Cigarros (TFDC) foi usado para avaliar a dependência nicotínica (DN) e AUDIT para avaliação do consumo de etílicos. Houve diminuição da expressão do gene CYP1B1 nos casos de CCE comparados aos controles. Foram encontradas diferenças estaticamente significativas de expressão gênica de CYP1B1 entre os Grupos CCE fumante e controle fumante (p=0,0018), Grupo CCE não fumante e controle não fumante (p=0,0079) e CCE fumante com CCE não fumante (p=0,0385) e entre os quatro grupos (p<0,0001). Houve diminuição da expressão do CYP2A6 no Grupo CCE fumante em relação ao Grupo controle, mas apenas um paciente do Grupo controle expressou este gene. Houve aumento da expressão de CYP2E1 entre os Grupos CCE fumante e controle fumante (p=0,0424). Concluindo, foi encontrada grande variabilidade interindividual no estudo da expressão dos genes estudados. Houve maior expressão de CYP1A1 e CYP2E1 em amostras de indivíduos fumantes com CCE. Os genes CYP1B1 e CYP2A6 estavam menos expressos no Grupo CCE fumante em relação ao Grupo controle. Para os genes CYP1B1 e CYP2E1 foram encontrados valores significativos na correlação entre a expressão gênica e parâmetros demográficos e de perfil tabágico no Grupo controle fumante, e do AUDIT no Grupo CCE não fumante. O gene CYP2E1, além de estar relacionado ao metabolismo do álcool, também deve ser considerado importante marcador do metabolismo dos carcinógenos derivados do tabaco.
Tobacco carcinogens are related to various types of cancer, including oral squamous cell carcinoma (OSCC). Allied to alcohol, tobacco contributes to the unfavorable outcome of the cases. Individual cancer susceptibility may be related to an expression of the enzymes that metabolize such carcinogens. The aim of this work is to evaluate the expression of the genes CYP1A1, CYP1B1, CYP2A6 and CYP2E1 on OSCC by qPCR. Samples were collected from 32 individuals with OSCC and 15 controls submitted to oral surgeries due to benign lesions. There were four groups: Smoker SCC group (n = 26), nonsmoker SCC group (n = 6), Smoker control group (n = 9) and nonsmoker control group (n = 6). The Fagerström Test for Cigarette Dependence (TFCD) was used to evaluate nicotinic dependence (ND) and AUDIT for the evaluation of alcohol consumption. There was a decrease in CYP1B1 gene expression in cases of SCC compared to controls. (P = 0.0018); smoker CCE and non-smoker control (p = 0.0079); smoker SCC with nonsmoker SCC (p = 0.0385) and between the four groups (p <0.0001). There was a decreased expression in CYP2A6 in the smoker SCC Group compared to the control group, but only one control group patient expressed this gene. There was an increased expression of CYP2E1 between the smoking and nonsmoking SCC groups (p = 0.0424). In conclusion, large interindividual variability was found in the study of the expression of the genes studied. There was greater expression of CYP1A1 and CYP2E1 in samples from smokers with SCC. The CYP1B1 and CYP2A6 genes were less expressed in the smoker SCC Group. Significant values were found for the CYP1B1 and CYP2E1 genes in the correlation between a gene expression and a parameter and a non-smoker control group, non-smoker control group and AUDIT. The CYP2E1 gene, besides being related to alcohol metabolism, should also be considered an important marker of the metabolism of the carcinogens derived from tobacco.
2016/08633-0
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Richter, Tanja. "Untersuchungen zur inter- und intraindividuellen Variabilität der enzymatischen Funktion von Cytochrom P450 CYP2B6." [S.l.] : [s.n.], 2005. http://www.gbv.de/du/services/toc/bs/490264026.

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McCully, S. "Characterisation of the principal human pulmonary drug-oxidising enzymes, CYP3A5, CYP2B6 & FMO." Thesis, University of Aberdeen, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.593066.

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The human lung has been shown to possess a wide range of enzyme systems and the potential to metabolise xenobiotics. Despite this, there is a paucity of well-designed investigations on the expression of pulmonary xenobiotic-metabolising enzymes. This thesis aimed to characterise the principal pulmonary drug-oxidising enzymes (CYP3A5, CPY2B6 & FMO) and to assess the role of this organ in the metabolism of therapeutic agents. CYP3A5 and CYP2B6 mRNAs were detected in 75% and 100% of lungs, respectively, and CYP3A5 and CYP2B6 protein was detected in 33% of lung samples, with 11% samples coexpressing these enzymes. Testosterone 6β-hydroxylation (CYP3A4/5) and 16β-hydroxylation (CYP2B6/7) were approximately 1500- and 700-fold lower in lung than liver, respectively. FMO activity was 29-fold lower in lung microsomes compared with liver. The ability of human lung microsomes to metabolise KC11458, terfenadine, cyclophosphamide and ifosfamide was investigated. KC11458 was metabolised to KC13195 in human lung samples by CYP2B6, whereas KC11458 was primarily metabolised to metabolite 1 by CYO3A4/5 and FMO in human liver. No terfenadine metabolites were detected in human lung incubations, whereas terfenadine alcohol formation was detected in all 8 livers. Human liver samples activated both ifosfamide and cyclophosphamide, whereas only ifosfamide activation was detected in human lung microsomes. This is of interest as lung cancer is the biggest cause of cancer mortality worldwide and ifosfamide is important in cancer therapy. CYP3A expression has been demonstrated in lung tumours, suggesting ifosfamide could be activated in situ. This study has illustrated the functional expression of specific drug-oxidising enzymes within the lung and has demonstrated that his organ can biotransform and bioactivate therapeutic agents with a metabolite profile significantly different from that of the liver. This may have clinical significance and may be important in determining the activation of compounds having local toxic or therapeutic actions within the lung (e.g. ifosfamide).
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Hua, Sally. "GENETIC VARIATIONS OF CYP2B6 ENZYME AND THE RESPONSE TO MEPERIDINE IN ORAL SEDATION." VCU Scholars Compass, 2009. http://scholarscompass.vcu.edu/etd/1709.

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Purpose: The purpose of this study was to determine the relationship of CYP2B6 genotype to the clinical response to meperidine in pediatric dental patients. Methods: Twenty-five patients, ASA I/ II, 45–92 months old, received an oral sedative regimen containing meperidine for dental treatment. The North Carolina Behavior Rating Scale (NCBRS) and Overall Effectiveness of Sedation Scale (OESS) were used to assess their behavior and sedation outcome. Saliva DNA samples were genotyped by PCR-RFLP. Results: We found the following genotype distributions: homozygous wild-type 1*1 (n = 8, 32%), heterozygous 1*6 (n = 13, 52%), and homozygous variant 6*6 (n = 4, 16%). The genotypes were predictive of a significant decrease in the overall effectiveness of sedation. Conclusion: Variation in CYP2B6 appears to be predictive of less successful sedations; wild-type individuals experienced more successful sedations than the homozygous variant 6*6. Future research regarding the enzyme kinetics of meperidine is needed to determine the exact enzymatic function of CYP2B6 and its variants.
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Books on the topic "CYP2B6"

1

Nowak, Maciej P. Comparison of polymorphic CYP2D6, CYP2C19 and CYP2A6 in Canadian Native Indian, Caucasian and Chinese populations. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1999.

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Goodz, Shari D. Investigating aspects of CYP2A6 in Caucasian and African American smokers. Ottawa: National Library of Canada, 2002.

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Zeman, Marilyn Vera. evaluation of coumarin as an in vivo measure of CYP2A6 activity. Ottawa: National Library of Canada, 1998.

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Pianezza, Michael Lawrence. The influence of genetically variable CYP246 on tobacco dependence and smoking behaviour. Ottawa: National Library of Canada, 1998.

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Ramamoorthy, Yamini. In vitro characterization of the catalytic activity of cytochrome P450 2D6 (CYP2D6)*10. Ottawa: National Library of Canada, 2000.

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Dortok, E. Desiree. Analysis of the possible therapeutic use of CYP2A6 inhibition with methoxsalen in smoking cessation. Ottawa: National Library of Canada, 2001.

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Micu, Alina L. An investigation of the induction of hepatic CYP2E1 by low doses of nicotine in the rat. Ottawa: National Library of Canada, 2003.

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Berns, Trevor Aaron. The influence of CYP2D1 in the behavioural pharmacology of amphetamine and hydrocodone in the male wistar rat. Ottawa: National Library of Canada, 1995.

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Lekas, Poli. Analysis of human CYP2E1 mRNA in a HepG2 cell line by reverse transcription-polymerase chain reaction (RT-PCR). Ottawa: National Library of Canada, 1998.

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Kim, Bill Woo Sung. The influence of CYP2A6 and CYP2B6 genotypes on smoking behaviour in adolescents. 2004.

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Book chapters on the topic "CYP2B6"

1

Zhang, Qing-Yu, and Xinxin Ding. "Chapter 10. The CYP2F, CYP2G and CYP2J Subfamilies." In Issues in Toxicology, 309–53. Cambridge: Royal Society of Chemistry, 2008. http://dx.doi.org/10.1039/9781847558428-00309.

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Erratico, Claudio A., Anand K. Deo, and Stelvio M. Bandiera. "Regioselective Versatility of Monooxygenase Reactions Catalyzed by CYP2B6 and CYP3A4: Examples with Single Substrates." In Advances in Experimental Medicine and Biology, 131–49. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16009-2_5.

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Sanders, John C., Rachel Koll, and Randal O. Dull. "CYP2D6: Where It All Began." In A Case Approach to Perioperative Drug-Drug Interactions, 29–32. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4614-7495-1_5.

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Coyle, Dustin, and Randal O. Dull. "CYP2B: 2B or Not 2B?" In A Case Approach to Perioperative Drug-Drug Interactions, 45–47. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4614-7495-1_9.

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Corcos, Laurent, and François Berthou. "Chapter 6. The CYP2B Subfamily." In Issues in Toxicology, 178–99. Cambridge: Royal Society of Chemistry, 2008. http://dx.doi.org/10.1039/9781847558428-00178.

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Yu, Aiming, and Robert L. Haining. "Purification, Biochemical Characterization and Comparative Enzyme Kinetics of Recombinant Human CYP2D6 1 and CYP2D6 2 Variants." In Advances in Experimental Medicine and Biology, 327–30. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-0667-6_51.

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Gmelch, Benjamin S., and Randal O. Dull. "CYP2E1: The Anesthesia Enzyme." In A Case Approach to Perioperative Drug-Drug Interactions, 33–36. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4614-7495-1_6.

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Fergerson, Byron Douglas, Crystal B. Wallentine, and Randal O. Dull. "CYP2C9: The Support Crew I." In A Case Approach to Perioperative Drug-Drug Interactions, 49–51. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4614-7495-1_10.

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Schulz, Thomas G., Peter Ruhnau, and Ernst Hallier. "Lack of Correlation Between CYP2A6 Genotype and Smoking Habits." In Advances in Experimental Medicine and Biology, 213–15. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-0667-6_29.

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Peñas-LLedó, Eva M., Pedro Dorado, and Adrián LLerena. "Pharmacogenomics and Personality: Role of CYP2D6 and Implications for Psychopathology." In Pharmacogenomics in Psychiatry, 30–45. Basel: KARGER, 2010. http://dx.doi.org/10.1159/000317297.

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Conference papers on the topic "CYP2B6"

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Wang, Xiaodong, Zhi-Yi Zhang, Jing Wang, Sharon Lu, Sujata Arora, Lorraine Hughes, Jennifer Christensen, and Vikram Kansra. "Abstract C62: Effects of rolapitant on the pharmacokinetics of dextromethorphan (CYP2D6), tolbutamide (CYP2C9), omeprazole (CYP2C19), efavirenz (CYP2B6), and repaglinide (CYP2C8) in healthy subjects." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics; November 5-9, 2015; Boston, MA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1535-7163.targ-15-c62.

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Evans, William, Jazmine Eccles, and William Baldwin. "Changes in Energy Metabolism Induced by PFOS and Dietary Oxylipins." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/jnpe5541.

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CYP2B6 is a drug metabolizing cytochrome P450 (CYP) that has anti-obesity properties, but also increases non-alcoholic fatty liver disease (NAFLD) in hCYP2B6-transgenic mice compared to Cyp2b-null mice. hCYP2B6-transgenic mice are also more susceptible to perfluorooctane sulfonic acid (PFOS) toxicity, a lipid-like toxicant used in stains, varnishes and firefighting foams that increase NAFLD. Our recent research demonstrates that CYP2B6 metabolizes dietary polyunsaturated fatty acids into the oxylipins, 9-HODE and 9-HOTre, which are strong peroxisome proliferator activated receptor alpha (PPARa) agonists and weak PPARg agonists. The purpose of our studies is to better understand the mechanisms behind PFOS and oxylipin-mediated hepatic steatosis. To test whether PFOS, 9-HODE or 9-HOTrE alter mitochondrial metabolism, Seahorse Mitostress assays were performed using HepG2 cells treated with 0.2, 1 and 5mM PFOS, 9-HODE and 9-HOTrE for 24 hours (n=5). Both PFOS and 9-HOTrE increased spare respiratory capacity in a concentration-dependent manner with lesser effects by 9-HODE. qPCR was performed following exposure of HepG2 cells to 1 and 5 mM of each compound to investigate changes in gene expression that may explain alterations in mitochondrial respiration or hepatic steatosis. PFOS repressed expression of ANGPTL4, a biomarker of PPARgactivation. 9-HODE induced CD36 and FASN expression, genes involved in fatty acid uptake and synthesis. 9-HOTrE induced SREBF1 and Cpt1a expression, genes involved in sterol synthesis and fatty acid transport into the mitochondria and may partially explain the increase in SRC. Thus, based on current results, PFOS is associated with reduced transport of lipids from the liver and 9-HODE increases lipid uptake; both would increase steatosis through different mechanisms. 9-HOTre may increase metabolism and therefore reduce steatosis.
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Jovanović-Šanta, Suzana S., Aleksandar M. Oklješa, Antos B. Sachanka, Yaraslau U. Dzichenka, and Sergei A. Usanov. "17-SUBSTITUTED STEROIDAL TETRAZOLES – NOVEL LIGANDS FOR HUMAN STEROID-CONVERTING CYP ENZYMES." In 1st INTERNATIONAL Conference on Chemo and BioInformatics. Institute for Information Technologies, University of Kragujevac, 2021. http://dx.doi.org/10.46793/iccbi21.336js.

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In animal and human organisms, there are many enzymes, members of the family of heme- containing proteins, cytochromes P450 (CYPs), included in the biosynthesis and metabolism of many biomolecules, as cholesterol, bile acids, sex, and corticosteroid hormones, as well as in metabolism of drugs and xenobiotics. It is also well-known that different imidazole and triazole derivatives are efficient inhibitors of CYPs activity. In this study, we present in vitro screening of binding of novel androstane derivatives with tetrazole- containing substituents in position 17 to human recombinant steroid-converting CYP enzymes: CYP7A1, CYP7B1, CYP17A1, CYP19, and CYP21. Initial screening was performed using a high throughput screening approach, while the affinity of the ligands was analyzed using spectrophotometric titration. For some among tested compounds type I spectral response (substrate-like binding) for CYP7A1 selectively, while for one compound type II spectral response (inhibitor-like binding) for CYP21 were detected, with micromolar values of Kds. Interestingly, one compound with mixed spectral response was found to bind for CYP7B1, which means that there are two optimal positions of the ligand inside the protein active site. Such results could be useful in CYP-inhibiting drug development, during a fast, high-throughput screening of pharmacological potential of novel compounds, as well as in side- effects recognizing.
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Urbschat, Anja E., Patrick Paulus, Quirine Freiin von Quernheim, Patrick Brück, and Elizabeth Ramos-Lopez. "Abstract 4773: Is upregulation of CYP2R1-, CYP27B1- and CYP24 genes in clear cell renal cell carcinoma tissue involved in carcinogenesis." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-4773.

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Rocha, José Claudio Casali da. "THE INFLUENCES OF ADHERENCE TO TAMOXIFEN AND CYP2D6 PHARMACOGENETICS ON PLASMA CONCENTRATIONS OF THE ACTIVE METABOLITE (Z)-ENDOXIFEN IN BREAST CANCER." In Abstracts from the Brazilian Breast Cancer Symposium - BBCS 2021. Mastology, 2021. http://dx.doi.org/10.29289/259453942021v31s2025.

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Tamoxifen efficacy in breast cancer is suspected to depend on adherence and intact drug metabolism. We evaluated the role of adherence behavior and pharmacogenetics on the formation rate of (Z)-endoxifen. In 192 Brazilian patients, we assessed plasma levels of tamoxifen and its metabolites at 3, 6, and 12 months of treatment (LC-MS/MS), adherence behavior (Morisky Medication Adherence Scale), and CYP2D6 and other pharmacogene polymorphisms (MALDI-TOF mass spectrometry and real-time PCR). Adherence explained 47% of the variability of tamoxifen plasma concentrations (p<0.001). While CYP2D6 alone explained 26.4%, the combination with adherence explained 40% of (Z)-endoxifen variability at 12 months (p<0.001). The influence of low adherence not to achieving relevant (Z)-endoxifen levels was the highest in patients with non-compromised CYP2D6 function (RR 3.65, 95%CI 1.48–8.99). As a proof-of-concept, we demonstrated that (Z)-endoxifen levels are influenced by patient adherence to both tamoxifen and CYP2D6, which is particularly relevant for patients with full CYP2D6 function.
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Ciorsac, Alecu, Diana Larisa Vlădoiu, Charline Fagnen, Maxime Louet, Maria A. Miteva, and Adriana Isvoran. "Assessment of some pesticides interactions with human cytochrome P450: CYP2C8, CYP2C9 and CYP2C19 by molecular docking approach." In 9TH INTERNATIONAL PHYSICS CONFERENCE OF THE BALKAN PHYSICAL UNION (BPU-9). AIP Publishing LLC, 2016. http://dx.doi.org/10.1063/1.4944305.

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Valarezo, Gabriela, Victoria Ortega-Hernández, Gonzalo Escobar-Massú, Wanda Fernández, María Paz Marzolo, and Pilar Carvallo. "Abstract 1440: Vitamin D uptake and metabolism in breast cancer tumors: Differential expression of megalin, VDR, CYP27B1 and CYP24A." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-1440.

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Leong, Chee-Onn, Boon Shing Tan, Kai Hung Tiong, Ashwin Muruhadas, Nirmal Randhawa, Heng Lungh Choo, Malcolm FG Stevens, and Tracey D. Bradshaw. "Abstract C75: CYP2S1 and CYP2W1 mediate 2-(3,4-dimethoxyphenyl)-5-fluorobenzothiazole (GW610, NSC 721648) sensitivity in breast and colorectal cancer cells." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 12-16, 2011; San Francisco, CA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1535-7163.targ-11-c75.

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Costa, José Cássio Figueira. "PREDIÇÃO DAS PROPRIEDADES FÍSICO-QUÍMICAS E FARMACOCINÉTICAS DO 7-HIDROXI-5-ACETOXIBISABOLENO: NOVA MOLÉCULA CONGÊNERE DO ALFA-BISABOLOL IDENTIFICADO EM LYCHNOPHORA ERICOIDES MART." In II Congresso Brasileiro de Biotecnologia On-line. Revista Multidisciplinar de Educação e Meio Ambiente, 2022. http://dx.doi.org/10.51189/conbiotec/49.

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Introdução: O metabolismo secundário vegetal é uma das principais responsáveis pela produção de uma grande diversidade de moléculas com potencial bioativo. A elucidação e caracterização molecular de novos compostos bioativos geram bases para estudos químicos e biológicos visando à produção e desenvolvimento de novos fármacos. A quimioinformática torna viável, a partir de algoritmos, a caracterização molecular de substâncias com estruturas elucidadas. O 7-hidroxi-5-acetoxibisaboleno (BoAcet) é um análogo terpenoídico do alfa-bisabolol, possui um agrupamento acetóxi ligado a um carbono secundário na posição 5 do anel heterocíclico, identificado pela primeira vez em extratos etanólicos de Lychnophora ericoides. O composto possui alto potencial antinociceptivo devido à diminuição significativa nos níveis dos mediadores IL-1b e TNF-a, citocinas-chave no processo nociceptivo, entretanto aspectos químicos, farmacocinéticos são desconhecidos. Objetivo: avaliar as propriedades físico-químicas e farmacocinéticas do 7-hidroxi-5-acetoxibisaboleno, composto inédito oriundo da L. ericoides. Metodologia: A molécula foi desenhada (SMILE: CC(C)=CCCC(C)(O)C1CC=C(C)CC1OC(C)=O) e avaliada por meio dos servidores Chemicalize, SwissADME, SwissParam e SwissSimilarity. A análise de similaridade em 32 bancos de dados, não demonstrou correlação estrutural com outros compostos elucidados disponíveis. Resultados: A análise preditiva demonstrou que a molécula possui massa molar de 280,408 g/mol, área de superfície polar topológica de 46,53 Å2, coeficiente de partição Log P o/w de 4,26±0,43, solubilidade intrínseca de 0,249 mg/mL, um doador de H, três aceptores de H, seis ligações rotacionáveis e um anel. As análises das propriedades farmacocinéticas demonstraram através de filtros físico-químicos de Linpiski, Veber, Muegge e Egan, que a molécula apresenta capacidade de atravessar a membrana celular, boa biodisponibilidade oral, não é substrato para a glicoproteína-P e não realiza inibição dos citocromos CYP1A2, CYP2C19, CYP2C9, CYP2D6 e CYP3A4, possui alta absorção, principalmente através do trato gastrointestinal, pode ultrapassar a barreira hematoencefálica, podendo atuar no sistema nervoso central, possui baixa possibilidade de ser absorvido pela pele (Log Kp = -5,60 cm/s. Conclusão: Este estudo evidencia que a BoAcet possui grande potencial para a geração de produtos farmacêuticos, entretanto, avaliações químicas e analises em sistemas biológicos são necessários para melhor compreender os aspectos moleculares, farmacodinâmicos, farmacocinéticos e toxicológicos intrínsecos ao composto.
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Irvin, W., L. Carey, O. Olajide, E. Dees, R. Raab, S. Corso, W. Chiu, et al. "Patients' Understanding of a CYP2D6 Tamoxifen Genotyping Study." In Abstracts: Thirty-Second Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 10‐13, 2009; San Antonio, TX. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-09-6082.

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Reports on the topic "CYP2B6"

1

Casabar, Richard C., Andrew D. Wallace, Ernest Hodgson, and Randy L. Rose. Metabolism of Endosulfan-Alpha by Human Liver Microsomes and its Utility as a Simultaneous In Vitro Probe for CYP2B6 and CYP3A4. Fort Belvoir, VA: Defense Technical Information Center, March 2006. http://dx.doi.org/10.21236/ada445178.

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Dudley, A., M. M. Peden-Adams, J. E. Daly, and D. E. Keil. JP-8 Jet Fuel Induces CYP2B1, CYP2BE1, and GSTPI but not CYP1A1 in Murine Liver. Fort Belvoir, VA: Defense Technical Information Center, March 2001. http://dx.doi.org/10.21236/ada402064.

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Goth-Goldstein, Regine. Oxidative Damage, CYP1B1 and Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, July 2002. http://dx.doi.org/10.21236/ada409396.

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4

Tanaka, Yuichiro. CYP1B1 Polymorphism as a Risk Factor for Race-Related Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, June 2008. http://dx.doi.org/10.21236/ada488824.

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5

Goth-Goldstein, Regine. Role of CYP1B1 in PAH-DNA Adduct Formation and Breast Cancer Risk. Fort Belvoir, VA: Defense Technical Information Center, April 2008. http://dx.doi.org/10.21236/ada484760.

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Goth-Goldstein, Regine, Marion L. Russell, A. P. Muller, M. Caleffi, J. Eschiletti, M. Graudenz, and Michael D. Sohn. Role of CYP1B1 in PAH-DNA adduct formation and breast cancer risk. Office of Scientific and Technical Information (OSTI), April 2010. http://dx.doi.org/10.2172/983194.

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Goth-Goldstein, Regine. Role of CYP1B1 in PAH-DNA Adduct Formation and Breast Cancer Risk. Fort Belvoir, VA: Defense Technical Information Center, March 2006. http://dx.doi.org/10.21236/ada450453.

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Goth-Goldstein, Regine, and Christine A. Erdmann. Role of CYP1B1 in PAH-DNA Adduct Formation and Breast Cancer Risk. Fort Belvoir, VA: Defense Technical Information Center, September 2002. http://dx.doi.org/10.21236/ada411455.

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Tanaka, Yuichiro, and Rajvir Dahiya. CYP1B1 Polymorphism as a Risk Factor for Race-Related Prostate Cancer. Addendum. Fort Belvoir, VA: Defense Technical Information Center, June 2009. http://dx.doi.org/10.21236/ada510133.

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Lamb, Dolores J. Enhancement of Vitamin D Action in Prostate Cancer through Silencing of CYP24. Fort Belvoir, VA: Defense Technical Information Center, February 2009. http://dx.doi.org/10.21236/ada502323.

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