Relevant bibliographies by topics / CYP2E1

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Academic literature on the topic 'CYP2E1'

Author: Grafiati
Published: 4 June 2021
Last updated: 14 March 2023

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Journal articles on the topic "CYP2E1"

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Wang, Guangbao, Yinghui Li, Wei Sun, Zhe Wang, Daoxing Chen, Sheng Shu, Jiayi Jin, et al. "Cytochrome P450-Mediated Metabolic Characterization of a Mono-Carbonyl Curcumin Analog WZ35." Pharmacology 105, no. 1-2 (October 4, 2019): 79–89. http://dx.doi.org/10.1159/000502854.

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WZ35 is a monocarbonyl analog of curcumin, which had been proved advantage over curcumin in chemical stability and antitumor activity. However, its pharmacokinetic profile has not been determined. In the present study, an ultraperformance liquid chromatography-tandem mass spectrometry assay was developed to detect concentration of WZ35 in rat plasma. Subsequently, pharmacokinetic study showed that the oral bioavailability of WZ35 is 10.56%. Cytochrome P450 (CYP450) plays a major role in metabolizing exogenous substance. The concentration of WZ35 was sharply decreased while incubating with microsome. It’s indicated that WZ35 is a substrate of CYP450s. Molecular docking assay showed that WZ35 can combine with CYP2B6 and CYP2C9 to form much more stable complex. The lowest docking energy was generated in complex with CYP2E1. The inhibition of CYP450s by WZ35 was also evaluated. Pan inhibitions of WZ35 on rat CYP3A2, CYP2B1, CYP2C11, CYP2D1, and ­CYP2E1 were observed by detecting probe substrates (midazolam, bupropion, tolbutamide, dextromethorphan, chlorzoxazone) and metabolites accordingly. On an average, 80% activities of enzymes were blocked. Mechanistically, the inhibitions of WZ35 on CYP3A2, CYP2B1, CYP2E1 were in a time-dependent manner according to the results of IC50 shift assay. The collective data demonstrated that the oral bioavailability of monocarbonyl analog of curcumin has significantly improved compared to curcumin. It’s both the substrate and inhibitor of CYP450s through in a time-dependent mechanism.
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TRUONG, Nhu-Traï, Arlette MONCION, Robert BAROUKI, Philippe BEAUNE, and Isabelle de WAZIERS. "Regulatory sequence responsible for insulin destabilization of cytochrome P450 2B1 (CYP2B1) mRNA." Biochemical Journal 388, no. 1 (May 10, 2005): 227–35. http://dx.doi.org/10.1042/bj20041510.

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Diabetes has been reported to increase CYP2E1 (cytochrome P450) and CYP2B1 expression at both the mRNA and protein levels in rat livers. This increase has been attributed to mRNA stabilization and can be reversed by daily insulin treatment. In a previous study, we showed that this hormone directly down-regulates CYP2E1 and 2B1 expression through a post-transcriptional mechanism in rat hepatoma cell lines. We then aimed to identify the molecular mechanisms involved in this regulation. We first identified a 16-mer sequence that we later showed to be the actual functional target of insulin on the rat CYP2E1 mRNA. Similar work was performed with CYP2B1. We first investigated the presence of mRNA–protein interactions. Using cytoplasmic proteins of Fao cells treated or not with insulin (0.1 μM) and the full-length CYP2B1 mRNA as a probe, a major CYP2B1 RNA–protein complex was observed with RNase T1 protection experiments. With the use of different CYP2B1 mRNA probes and by means of competition experiments with antisense oligonucleotides, a protein fixation site was located on a 16-nt sequence in the 5′ part of the coding region. This sequence has a hairpin loop structure, shows 80% sequence identity with a structure previously identified on CYP2E1 and is also responsible for the post-transcriptional effects of insulin on this mRNA. Protein(s) bound to both CYP2B1 and CYP2E1 sequences are cytosolic and have an apparent molecular mass of 60 kDa. The protein(s) that bind(s) to both these sequences and the insulin transduction signal involved in this regulation remain(s) to identified.
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Ferdouse, Afroza, Rishi R. Agrawal, Madeleine A. Gao, Hongfeng Jiang, William S. Blaner, and Robin D. Clugston. "Alcohol induced hepatic retinoid depletion is associated with the induction of multiple retinoid catabolizing cytochrome P450 enzymes." PLOS ONE 17, no. 1 (January 14, 2022): e0261675. http://dx.doi.org/10.1371/journal.pone.0261675.

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Chronic alcohol consumption leads to a spectrum of liver disease that is associated with significant global mortality and morbidity. Alcohol is known to deplete hepatic vitamin A content, which has been linked to the pathogenesis of alcoholic liver disease. It has been suggested that induction of Cytochrome P450 2E1 (CYP2E1) contributes to alcohol-induced hepatic vitamin A depletion, but the possible contributions of other retinoid-catabolizing CYPs have not been well studied. The main objective of this study was to better understand alcohol-induced hepatic vitamin A depletion and test the hypothesis that alcohol-induced depletion of hepatic vitamin A is due to CYP-mediated oxidative catabolism. This hypothesis was tested in a mouse model of chronic alcohol consumption, including wild type and Cyp2e1 -/- mice. Our results show that chronic alcohol consumption is associated with decreased levels of hepatic retinol, retinyl esters, and retinoic acid. Moreover, the depletion of hepatic retinoid is associated with the induction of multiple retinoid catabolizing CYPs, including CYP26A1, and CYP26B1 in alcohol fed wild type mice. In Cyp2e1 -/- mice, alcohol-induced retinol decline is blunted but retinyl esters undergo a change in their acyl composition and decline upon alcohol exposure like WT mice. In conclusion, the alcohol induced decline in hepatic vitamin A content is associated with increased expression of multiple retinoid-catabolizing CYPs, including the retinoic acid specific hydroxylases CYP26A1 and CYP26B1.
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Н.Н., Климкович,, Руденкова, Т.В., Костюк, С.А., Алешкевич, С.Н., Демиденко, А.Н., and Яковлева, Е.А. "Genetic Polymorphisms of Cytochrome P450 in Children with Acute Lymphoblastic Leukemia." Гематология. Трансфузиология. Восточная Европа, no. 4 (December 28, 2022): 418–29. http://dx.doi.org/10.34883/pi.2022.8.4.005.

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Цель. Анализ полиморфизмов генов CYP1A1, CYP2E1, CYP2D6 у детей с токсическими осложнениями на фоне лечения ОЛЛ. Материалы и методы. Материал исследования – периферическая кровь и буккальный эпителий 43 пациентов с ОЛЛ на фоне полихимиотерапии в возрасте от 2 до 17 лет. Использованы клинико-лабораторные, молекулярно-биологические (полимеразная цепная реакция (ПЦР), рестрикция фрагментов ДНК, электрофоретический анализ фрагментов ДНК), статистические методы. Результаты. Профиль токсических осложнений у детей с острыми лимфобластными лейкозами из В-клеток-предшественников на фоне химиотерапии, соответствующих III–IV степени токсичности, представлен гематологическими, гастроинтестинальными, печеночнымии и инфекционными осложнениями. Частота аллелей дикого типа была доминирующей для полиморфизмов: A4889G (rs1048943) в гене CYP1A1; T7632A (rs6413432), G1293C (rs3813867) и C1053T (rs2031920) в гене CYP2Е1; A2549del (rs35742686) в гене CYP2D6, для данных геновариантов частота выявления составила от 90,70 до 100%. Распространенность гетерозиготных геновариантов среди обследованных пациентов была выше для полиморфизма T6235C (rs4646903) в гене CYP1A1 (гетерозиготный аллель ТС – 27,91%), а также для полиморфизма G1846A (rs3892097) в гене CYP2D6 (гетерозиготный аллель GA – 32,56%). Самая высокая частота выявления мутантного аллеля была определена для полиморфизма C100T (rs1065852) в гене CYP2D6 (мутантный аллель ТТ – 27,50%). Заключение. Установлена частота выявления различных вариантов генов CYP1A1, CYP2E1, CYP2D6 у детей на фоне химиотерапии ОЛЛ. Полученные результаты лягут в основу дальнейших исследований определения ассоциации полиморфных вариантов геновCYP с формированием осложнений в ходе лечения детей с ОЛЛ. Purpose. Analysis of CYP1A1, CYP2E1, CYP2D6 gene polymorphisms in children with toxic complications during acute lymphoblastic leukemia (ALL) treatment. Materials and methods. The study material was peripheral blood and buccal epithelium of 43 patients with ALL and polychemotherapy aged from 2 to 17 years. Clinical-laboratory, molecular-biological (polymerase chain reaction (PCR), restriction of DNA fragments, electrophoretic analysis of DNA fragments), statistical methods were used. Results. The profile of toxic complications in children with ALL from B-cell precursors against during of chemotherapy, corresponding to III–IV degrees of toxicity, was represented by hematological, gastrointestinal, hepatic and infectious complications. The frequency of wild-type alleles was dominant for the polymorphisms: A4889G (rs1048943) in the CYP1A1 gene; T7632A (rs6413432), G1293C (rs3813867), and C1053T (rs2031920) in the CYP2E1 gene; A2549del (rs35742686) in the CYP2D6 gene; for these gene variants the detection rate was 90.70 to 100%. The prevalence of heterozygous gene variants among the examined patients was higher for the polymorphism T6235C (rs4646903) in the CYP1A1 gene (heterozygous allele TC – 27.91%), and for the polymorphism G1846A (rs3892097) in the CYP2D6 gene (heterozygous allele GA – 32.56%). The highest frequency of mutant allele detection was determined for the C100T polymorphism (rs1065852) in the CYP2D6 gene (mutant TT allele – 27.50%). Conclusion. The frequency of detection of different variants of CYP1A1, CYP2E1, CYP2D6 genes was established in children during of chemotherapy for ALL. The results obtained will form the basis for further studies to determine the association of CYP polymorphic variants with the formation of complications during the treatment of children with ALL.
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Kochetova, Olga V., Tatyana V. Victorova, and Lilya K. Karimova. "The roles of genes of ksenobiotics biotransformation in the development of predisposition to the toxic heoatitis in workers workers exposed to hepthyle and ethylebenzene-styrene." Ecological genetics 3, no. 1 (March 15, 2005): 3–10. http://dx.doi.org/10.17816/ecogen313-10.

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Introduction: The aim of this study was to estimate the predisposition of influencing possible factors causing chemical induced abnormal liver function on the basis of studying genes encoding xenobiotic metabolizing enzymes. Methods: Genotyping of CYP1A1, CYP2D6, CYP2E1, EPHX1, NAT2 was performed using polymerase chain reaction and restriction fragment length polymorphism on peripheral leucocyte DNA from 73 incident cases of toxic hepatitis, 163 «groups of risk» on development of a toxic hepatitis, 94 healthy workers and 335 controls.Results and conclusions: No significant association was found between a reference group and petrochemical workers when CYP1A1, CYP2D6, CYP2E1, EPHX1 genotypes were included in the analyses. Among workers was observed the increasing of frequency of a combination *4/*4 genes NAT2 compared with control group. Among the patients with a professional toxic hepatitis are established genetic markers of predisposition to development the disease: Ile/Val gene CYP1A1, Tyr/His gene EPHX1; combinations *4/*7 genes NAT2; and as slow phenotype microsomal epoxide hydrolase; combinations of genotypes IleVal/C1C1 of genes CYP1A1 and CYP2E1; combinations of slow phenotypes microsomal epoxide hydrolase and N-acetyltransferase-2. Our results suggest that genotype Ile/Ile of gene CYP1A1; genotype Tyr/Tyr of gene EPHX1; and as a normal phenotype microsomal epoxide hydrolase; a combination of genotypes IleIle/C1C1 of genes CYP1A1 and CYP2E1; a combination of genotypes IleIle/C1C1/CC/N of genes CYP1A1, CYP2E1, CYP2D6 and a normal phenotype microsomal epoxide hydrolase are protective variants. This study demonstrates a significant combined effect of phase I and phase II polymorphisms on the predisposition of professional pathology at workers exposed to hepthyle and ethylebenzene-styrene.
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Li, Xiangyang, Jianxin Yang, Yijie Qiao, Yabin Duan, Yuanyao Xin, Yongqiong Nian, Lin Zhu, and Guiqin Liu. "Effects of Radiation on Drug Metabolism: A Review." Current Drug Metabolism 20, no. 5 (June 20, 2019): 350–60. http://dx.doi.org/10.2174/1389200220666190405171303.

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Background: Radiation is the fourth most prevalent type of pollution following the water, air and noise pollution. It can adversely affect normal bodily functions. Radiation alters the protein and mRNA expression of drugmetabolizing enzymes and drug transporters and the pharmacokinetic characteristics of drugs, thereby affecting drug absorption, distribution, metabolism, and excretion. Therefore, it is important to study the pharmacokinetic changes in drugs under radiation. Methods: To update data on the effects of ionizing radiation and non-ionizing radiation caused by environmental pollution or clinical treatments on the protein and mRNA expression of drug-metabolizing enzymes and drug transporters. Data and information on pharmacokinetic changes in drugs under radiation were analyzed and summarized. Results: The effect of radiation on cytochrome P450 is still a subject of debate. The widespread belief is that higherdose radiation increased the expression of CYP1A1 and CYP1B1 of rat, zebrafish or human, CYP1A2, CYP2B1, and CYP3A1 of rat, and CYP2E1 of mouse or rat, and decreased that of rat’s CYP2C11 and CYP2D1. Radiation increased the expression of multidrug resistance protein, multidrug resistance-associated protein, and breast cancer resistance protein. The metabolism of some drugs, as well as the clearance, increased during concurrent chemoradiation therapy, whereas the half-life, mean residence time, and area under the curve decreased. Changes in the expression of cytochrome P450 and drug transporters were consistent with the changes in the pharmacokinetics of some drugs under radiation. Conclusion: The findings of this review indicated that radiation caused by environmental pollution or clinical treatments can alter the pharmacokinetic characteristics of drugs. Thus, the pharmacokinetics of drugs should be rechecked and the optimal dose should be re-evaluated after radiation.
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Shayakhmetova, G. "COMPARATIVE INVESTIGATION OF ANTI-TUBERCULOSIS DRUGS EFFECTS ON TESTICULAR CYP2Е1 EXPRESSION AND MALE REPRODUCTIVE PARAMETERS UNDER SEPARATE AND COMBINED ADMINISTRATION IN MALE RATS." Bulletin of Taras Shevchenko National University of Kyiv. Series: Biology 72, no. 2 (2016): 80–85. http://dx.doi.org/10.17721/1728_2748.2016.72.80-85.

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Comparative study of anti-tuberculosis drugs anti-androgenic effects and effects on testicular CYP2E1 has been performed. Testicular CYP2E1 mRNA and protein expression, serum total testosterone level, fertility and spermatogenesis parameters in male rats under simultaneous and separate administration of ethambutol, isoniazid, rifampin and pyrazinamide have been investigated. Analysis of the obtained data has proved the prominent role of ethambutol and isoniazid in gonadal toxicity of antituberculosis drugs combination. Activation of CYP2Е1-dependent metabolizing systems in testicular steroidogenic cells could stipulate at least a part of ethambutol, isoniazid and anti-tuberculosis drugs combination negative effects on testosterone level and spermatogenesis processes. Mechanisms of spermatogenesis alteration by rifampin and pyrazinamide need to be explored more extensively, but in the light of our observations they do not depend from testicular CYP2E1.
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ZHUKOV, Andrei, and Magnus INGELMAN-SUNDBERG. "Relationship between cytochrome P450 catalytic cycling and stability: fast degradation of ethanol-inducible cytochrome P450 2E1 (CYP2E1) in hepatoma cells is abolished by inactivation of its electron donor NADPH–cytochrome P450 reductase." Biochemical Journal 340, no. 2 (May 25, 1999): 453–58. http://dx.doi.org/10.1042/bj3400453.

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Ethanol-inducible cytochrome P450 2E1 (CYP2E1) involved in the metabolism of gluconeogenetic precursors and some cytotoxins is distinguished from other cytochrome P450 enzymes by its rapid turnover (in vivo half-life of 4-7 h), with ligands to the haem iron, both substrates and inhibitors, stabilizing the protein. CYP2E1 is also known to have a high oxidase activity in the absence of substrate, resulting in the production of reactive oxygen radicals. We suggested that the rapid intracellular turnover of the enzyme may be partly due to covalent modifications by such radicals or to other changes during catalytic cycling, in which case the inhibition of electron supply from NADPH-cytochrome P450 reductase would be expected to stabilize the protein. Fao hepatoma cells, where CYP2E1 showed a half-life of 4 h upon serum withdrawal, were treated for 1 h with 0.3 μM diphenylene iodonium (DPI), a suicide inhibitor of flavoenzymes, which resulted in ≈ 90% inhibition of the microsomal NADPH-cytochrome P450 reductase and CYP2E1-dependent chlorzoxazone hydroxylase activities. Subsequent cycloheximide chase revealed that the CYP2E1 half-life increased to 26 h. Neither the degradation rates of total protein, CYP2B1 and NADPH-cytochrome P450 reductase nor the cellular ATP level were affected by DPI under the conditions employed. These results demonstrate for the first time that the short half-life of CYP2E1 in vivo may be largely due to the rapid destabilization of the enzyme during catalytic cycling rather than to the intrinsic instability of the protein molecule.
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Shahriary, Ghazaleh Mohammadzadeh, Hamid Galehdari, Amir Jalali, Fatemeh Zanganeh, Seyed Mohammad Reza Alavi, and Mohammad Reza Aghanoori. "CYP2E1*5B, CYP2E1*6, CYP2E1*7B, CYP2E1*2, and CYP2E1*3 Allele Frequencies in Iranian Populations." Asian Pacific Journal of Cancer Prevention 13, no. 12 (December 31, 2012): 6505–10. http://dx.doi.org/10.7314/apjcp.2012.13.12.6505.

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Liu, Lingyu, Janak L. Pathak, Yong-qiang Zhu, and Matthias Bureik. "Comparison of cytochrome P450 expression in four different human osteoblast models." Biological Chemistry 398, no. 12 (November 27, 2017): 1327–34. http://dx.doi.org/10.1515/hsz-2017-0205.

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AbstractCytochromes P450 (CYPs) are important for bone homeostasis, but only limited information is available on their expression in human bone cells. We analyzed the expression levels of eight CYPs in osteoblasts cultured in human bone pieces, in osteoblasts differentiated from human periosteum mesenchymal stem cells, in primary human osteoblasts and in the human osteoblast cell line MG63, respectively. Our results confirm previous reports about the presence of CYP11A1, CYP17A1, CYP24A1 and CYP27B1, while demonstrating expression of CYP2E1, CYP26A1, CYP39A1 and CYP51A1 for the first time. However, expression patterns in the four models were remarkably different from each other.
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Dissertations / Theses on the topic "CYP2E1"

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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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3

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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MEDEIROS, BORBA VIEIRA MARIA ISABEL. "Ontogenese du cyp2e1 hepatique humain : regulation de l'expression du gene cyp2e1 par demethylation des residus cpg." Paris 7, 1997. http://www.theses.fr/1997PA077142.

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Les objectifs de ce travail ont ete l'etude de l'ontogenese du cyp2e1 hepatique humain et la mise en evidence des mecanismes moleculaire impliques dans le controle de l'expression du cyp2e1 au cours du developpement. Le cyp2e1 presente une expression uniquement postnatale : la proteine et les activites enzymatiques correspondantes apparaissent au cours des heures qui suivent la naissance, et augmentent graduellement jusqu'a l'age adulte. Le taux d'arnm cyp2e1 reste faible au cours de la periode perinatale, bien que la concentration de la proteine cyp2e1 augmente immediatement apres la naissance. Ceci suggere l'intervention d'un mecanisme post-transcriptionnel de regulation, probablement par stabilisation de la proteine par les corps cetoniques. A partir de l'age d'un mois, l'augmentation de l'arnm cyp2e1 est parallele a celle du contenu en cyp2e1 microsomal et permet de supposer que le controle de l'expression du cyp2e1 a lieu au niveau transcriptionnel. Les profils de methylation des sites hpall/mspl dans la partie 5', l'exon 1 et l'intron 1 du gene cyp2e1 ont ete compares. Des modifications de l'etat de methylation ont ete observees au niveau d'un site situe a 34 pb en aval de la boite tata et sites localises a l'interieur de l'intron 1. Ces sites sont methyles dans le foie de foetus et de nouveau-nes exprimant des taux faibles d'arnm cyp2e1. Leur demethylation est correlee a l'expression de l'arnm cyp2e1 chez les nouveau-nes et les adultes. Dans le poumon et le rein de foetus, de nouveau-ne et d'adulte, qui expriment des taux faibles d'arnm cyp2e1, les sites hpall/mspl sont egalement methyles, tandis qu'une demethylation partielle existe dans le placenta, exprimant des taux variables de transcrit. En conclusion, deux mecanismes interviennent dans le controle de l'expression du cyp2e1 : la stabilisation de la proteine au cours des jours qui suivent la naissance et l'activation transcriptionnelle du cyp2e1 associee a la demethylation des residus cpg.
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Bulsara, Daksha. "The effects of Poly IC and human interferon #alpha# on rat hepatic CYP4A1 and CYP2E1." Thesis, University of Surrey, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.334347.

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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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Lindgren, Kristjon, and Dana Seng. "The Effects of Cyp2e1 on Hepatic Gene Expression in 129/Sv-Cyp2e1^tm1Gonz/J and 129S1/SvImJ Mice Exposed to Hydrazine." The University of Arizona, 2007. http://hdl.handle.net/10150/624424.

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Class of 2007 Abstract
Objectives: To characterize the difference in hepatic gene expression between Cyp2e1 +/+ and Cyp2e1 -/- mice after exposure to hydrazine in order to elucidate the functional pathway(s) for hydrazine-induced steatosis. Methods: The project was designed by Dr. Charlene McQueen and consisted of the following aims: (1) to characterize the hepatic pathology induced by hydrazine in CYP2E1 +/+ and -/- mice, (2) to evaluate hepatic gene expression profiles following exposure to hydrazine, and (3) to determine the expression of CYP2E1 and CYP4A14. The animal exposure and data collection have been completed and aim #2 is awaiting data analysis. Aim #2 consisted of treating CYP2E1 +/+ and CYP2E1 -/- mice to saline and hydrazine at doses of 100 mg/kg. Livers were collected at six and 24 hours and the mRNA was isolated with an Absolutely RNA RT-PCR Miniprep Kit. The transcriptome was determined using the Affymetrix GeneChip Expression Analysis System using total mouse genome GeneChips. The GeneChips were scanned using an Agilent GeneArray Scanner and the image was quantitated and archived awaiting data analysis. The data was collected by the SWEHSC Microarray Facility on June 20, 2005 was analyzed. The data analysis was completed by both Kristjon Lindgren and Dana Seng with the help and training from Dr. George Watts. The six sets of data from aim #2 was analyzed using Agilent's GeneSpring 7.3.1 software to characterize the two-fold differences in mice (n = 2 per group) hepatic gene expression. Genes of interest were identified as containing the keywords cyp, fatty, glutathione, hepat, lipid, liver, oxid, perox, steroid, and phosphatidylinositol in the Gene Ontology Biological Process, Cellular Component, or Molecular Function descriptions. Lastly, pathway mining of/for genes of interest was performed using Bioresource for array of genes (BioRag) available at www.biorag.org and maintained by the AzCC/SWEHSC Bioinformatics Facility. Results: The amount of information extracted from this research project is too immense to be described or summarized on this form. For more information, please obtain a copy of this research project from the University of Arizona College of Pharmacy or from the project co-authors Kristjon Lindgren (kristjon.lindgren@gmail.com) or Dana Seng (dana.seng@gmail.com). Conclusions: The effects of Cyp2e1 on hepatic gene expression in 129/Sv-Cyp2e1tm1Gonz/J and 129S1/SvImJ mice exposed to hydrazine was analyzed. Data showing that Cyp2e1 was protective against HD-induced hepatotoxicity was consistent with the proposed hypothesis. Hepatic gene expression results show that Cyp2e1 -/- mice have decreased expression of microsomal ω-oxidation genes (Cyp4a10 and Cyp4a14) compared to Cyp2e1 +/+ at 6h (both increased at 24h) and peroxisomal β–oxidation genes (Ehhadh) at 6h like Cyp2e1 +/+ (but increased at 24h only in Cyp2e1 -/-). Conversely, an increased expression of mitochondrial β-oxidation genes (Cpt1a) in both genotypes at 6 and 24h and cholesterol synthesis genes (Fdft1, Hmgcr, Hmgcs1, Idi, Lss, Mvk, Nsdhl, Sc4mol, and Sqle) in Cyp2e1 -/- at 24h was observed. These results support mechanisms by which ω-oxidation or PPARγ is protective or peroxisomal β- oxidation is damaging. Additional studies are needed to further eludidate the mechanisms of HD-induced steatosis.
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Ulusoy, Gulen. "Genetic Polymorphisms Of Alcohol Inducible Cyp2e1 In Turkish Population." Master's thesis, METU, 2005. http://etd.lib.metu.edu.tr/upload/12604747/index.pdf.

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Cytochrome P4502E1 (CYP2E1), the ethanol-inducible isoform of cytochrome P450 superfamily, catalyzes many low molecular weight endogenous and exogenous compounds, including ethanol, acetone, drugs like acetaminophen and chlorzoxazone, and industrial solvents like benzene and styrene, most of which are carcinogenic. Besides, it has a high capacity to produce reactive oxygen species. CYP2E1 is induced by ethanol and isoniazid, as well by some pathophysiological conditions like diabetes and starvation. CYP2E1 gene shows genetic polymorphisms which are thought to play a major role in interindividual variability in drug response and in susceptibility to chemical-induced diseases, like several types of cancers. It is well established that CYP2E1 polymorphisms vary markedly in frequency among different ethnic and racial groups. Therefore, in this study, the frequency of two important CYP2E1 polymorphisms
the single nucleotide polymorphisms C-1019T / G-1259C in 5&rsquo
-flanking region and T7678A poymorphism in intron 6, in Turkish population was investigated. For this purpose, whole blood samples were collected from 132 healthy volunteers representing Turkish population and genomic DNA for each subject was isolated in intact form. The genotypes were determined by PCR amplification of corresponding regions followed by restriction endonuclease RsaI, PstI (for C-1019T / G-1259C SNPs) and DraI (for T7678A SNP) digestions. The genotype frequencies, for C-1019T / G-1259C SNPs, which are in complete linkage disequilibrium, were investigated on 116 DNA samples, and determined as 97.4% for homozygous wild type (c1/c1), 2.6% for heterozygotes (c1/c2) and 0.0% for homozygous mutants (c2c2). The allele frequency of wild type allele (c1) was calculated as 98.7% and that of mutated allele (c2) as 1.3%. The genotype frequencies for T7678A SNP, investigated in 108 DNA samples were determined as 80.6% for homozygous wild type (DD), 19.4% for heterozygotes (CD) and 0.0% for homozygous mutants (CC). The corresponding allele frequencies were 90.3% for wild type allele (D), and 9.7% for mutated allele (C). Genotype frequencies of both polymorphisms fit Hardy-Weinberg equation and showed no significant difference with respect to gender. The genotype distributions of both polymorphisms showed similarity when compared to other Caucasian populations like French, Swedish, German, and Italian populations, while both polymorphisms studied differed significantly from Chilean, Japanese, Taiwanese and Chinese populations, as compared with Chi-Square test.
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Weltman, Martin D. (Martin David). "Pathogenesis of nonalcoholic steatohohepatitis [sic] : the role of CYP2E1." Thesis, The University of Sydney, 1998. https://hdl.handle.net/2123/27739.

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The relevant literature concerning nonalcoholic steatohepatitis (NASH), the morphologically similar condition of alcoholic liver disease (ALD), and the hepatic cytochromes P450 (P450 or CYP) was reviewed with particular emphasis on CYP2E1. CYP2E1 is induced in ALD. It plays an important role in the pathogenesis of this condition by generating reactive oxygen species (ROS). In turn, ROS produce lipid peroxidation, which contributes to the cellular injury in ALD. CYP2E1 is constitutively expressed in acinar zone 3. The early lesions observed in both ALD and NASH are most pronounced in the same acinar region of the liver. Since NASH and ALD have similar histological appearances, the possibility that CYP2E1 may play a significant role in the pathogenesis of NASH was considered. One of the limitations in evaluating the pathogenesis of NASH has been the absence of an appropriate animal model.
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Books on the topic "CYP2E1"

1

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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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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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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Cypher. Brooklyn, N.Y: Powerhouse Books, 2008.

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Cypher. Salt Lake City: Gibbs Smith, 1997.

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The Cronus cypher. Shelton, WA: FML, 2010.

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GmbH, Airtec, ed. Cypres user's guide. Wünnenberg, Germany: AIRTEC, 1991.

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Zero: Cypher of infinity. [Vashon Island, Wash.]: Suzanne Moore, 2014.

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N, Tucker Ezra, ed. Cypher the Mountain Giant. New York: Scholastic, 2007.

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Noble, Ian. Enquire within: A multivalent cypher. Southsea: X Press, 1993.

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Book chapters on the topic "CYP2E1"

1

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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Kiss, I., and I. Ember. "Genetic Polymorphisms of CYP1A1, CYP2E1, and GSTM1 Genes: Susceptibility to Colon Cancer." In Cell Injury and Protection in the Gastrointestinal Tract, 343–47. Dordrecht: Springer Netherlands, 1997. http://dx.doi.org/10.1007/978-94-011-5392-8_34.

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Cederbaum, Arthur I. "Nrf2 and Antioxidant Defense Against CYP2E1 Toxicity." In Subcellular Biochemistry, 105–30. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-5881-0_2.

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Daly, Ann K. "Relevance of CYP2E1 to Non-alcoholic Fatty Liver Disease." In Subcellular Biochemistry, 165–75. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-5881-0_5.

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Lakshman, M. Raj, Mamatha Garige, Maokai A. Gong, Leslie Leckey, Ravi Varatharajalu, Robert S. Redman, Devanshi Seth, et al. "CYP2E1, Oxidative Stress, Post-translational Modifications and Lipid Metabolism." In Subcellular Biochemistry, 199–233. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-5881-0_7.

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Wu, Defeng, and Arthur I. Cederbaum. "Development and Properties of HepG2 Cells That Constitutively Express CYP2E1." In Alcohol, 137–50. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-242-7_11.

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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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Cederbaum, Arthur I. "CYP2E1 – Biochemical and Toxicological Aspects and Role in Alcohol-Induced Liver Injury." In Advances in Bioactivation Research, 1–36. New York, NY: Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-77300-1_6.

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Song, Byoung-Joon. "Gene Structure and Multiple Regulations of the Ethanol-Inducible Cytochrome P45O2E1 (CYP2E1) Subfamily." In Alcohol and Hormones, 177–92. Totowa, NJ: Humana Press, 1995. http://dx.doi.org/10.1007/978-1-4612-0243-1_9.

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Heit, Claire, Hongbin Dong, Ying Chen, David C. Thompson, Richard A. Deitrich, and Vasilis K. Vasiliou. "The Role of CYP2E1 in Alcohol Metabolism and Sensitivity in the Central Nervous System." In Subcellular Biochemistry, 235–47. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-5881-0_8.

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Conference papers on the topic "CYP2E1"

1

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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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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Hammad, S., J. Zhao, Y. Yin, A. Zaza, D. Drasdo, JG Hengstler, and S. Dooley. "CYP2E1 recovery is associated with a pericentral fibrosis pattern after repeated CCl4 insults." In 35. Jahrestagung der Deutschen Arbeitsgemeinschaft zum Studium der Leber. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0038-1677078.

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McCaskill, Michael L., Joseph H. Sisson, and Todd A. Wyatt. "CYP2E1 Mediates Ethanol-Induced DNA Damage And TNF Release In Bronchial Epithelial Cells." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a3252.

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Dehipawala, Sunil, Reginia Sullivan, George Tremberger, David Lieberman, and Tak Cheung. "Bioinformatics of CYP2E1 CpG intron methylation sites and application to HAR1-RELN sequence analysis." In 2016 International conference on Signal Processing, Communication, Power and Embedded System (SCOPES). IEEE, 2016. http://dx.doi.org/10.1109/scopes.2016.7955683.

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Cao, Lei, Jia Lin, Bing He, Hongge Wang, Juan Rao, Yingwen Liu, and Xuemei Zhang. "Abstract 3252: A regulatory variant in CYP2E1 affects the risk of lung squamous cell carcinoma." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-3252.

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Ye, Qinyuan, Pollyanna R. G. Chavez, Fuzhi Lian, Yan Wang, Kang-Quan Hu, Wenhua Ling, Helmut K. Seitz, and Xiang-Dong Wang. "Abstract 964: Chlormethiazole, an inhibitor of CYP2E1, prevented chemical carcinogen-initiated and alcohol-promoted hepatic carcinongenesis in rats." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-964.

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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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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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Dzichenka, Yaraslau, Michail Shapira, Sergei Usanov, Marina Savić, Ljubica Grbović, Jovana Ajduković, and Suzana Jovanović-Šanta. "NOVEL LIGANDS OF HUMAN CYP7 ENZYMES – POSSIBLE MODULATORS OF CHOLESTEROL BLOOD LEVEL: COMPUTER SIMULATION STUDIES." In 1st INTERNATIONAL Conference on Chemo and BioInformatics. Institute for Information Technologies, University of Kragujevac, 2021. http://dx.doi.org/10.46793/iccbi21.435d.

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Abstract:
Our in vitro studies showed that a couple of perspective steroidal derivatives showed previously biomedical potential via enzyme inhibition, receptor binding or antiproliferative effect against the cancer cells of reproductive tissues are able to bind to human CYP7 enzymes – key enzymes taking part in hydroxylation of cholesterol, 25-, 27-hydroxycholesterol and a number of steroidal hormones. In silico screening of binding affinity of the modified steroids toward CYP7 enzymes showed that interaction energy for the new ligands is comparable with consequent values, calculated for the ‘essential’ substrates of the enzymes – cholestenone (CYP7A1) and DHEA (CYP7B1). However, no correlation between binding energy and the affinity of the ligand was found. Novel ligands interact with conserved amino acids taking part in stabilization of natural substrates of CYP7 enzymes. A couple of structural features, governing ligand binding, were identified. Among which are planar structure of A-ring for CYP7A1 ligands, absence of many polar fragments in side-chain and presence of polar group at C3 position. Analysis of the docking results showed that CYP7B1 higher selectivity in comparison with CYP7A1 is connected by the structure of the cavity formed by α-helices I and B`. The data obtained will be used for the explanation of ligand specificity of human sterol- hydroxylases.
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Reports on the topic "CYP2E1"

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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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Ma, Long, Gang Jin, Yi Yang, Yao Pang, Wenhao Wang, Hongyi Zhang, Jiawei Liu, et al. Association Between CYP2A13 Polymorphisms and Lung Cancer. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, September 2020. http://dx.doi.org/10.37766/inplasy2020.9.0102.

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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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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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