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[PMID]:28578073
[Au] Autor:Baravalle R; Ciaramella A; Baj F; Di Nardo G; Gilardi G
[Ad] Endereço:Department of Life Sciences and Systems Biology, University of Torino, Via Accademia Albertina 13, Torino, Italy.
[Ti] Título:Identification of endocrine disrupting chemicals acting on human aromatase.
[So] Source:Biochim Biophys Acta;1866(1):88-96, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Human aromatase is the cytochrome P450 catalysing the conversion of androgens into estrogens playing a key role in the endocrine system. Due to this role, it is likely to be a target of the so-called endocrine disrupting chemicals, a series of compounds able to interfere with the hormone system with toxic effects. If on one side the toxicity of some compounds such as bisphenol A is well known, on the other side the toxic concentrations of such compounds as well as the effect of the many other molecules that are in contact with us in everyday life still need a deep investigation. The availability of biological assays able to detect the interaction of chemicals with key molecular targets of the endocrine system represents a possible solution to identify potential endocrine disrupting chemicals. Here the so-called alkali assay previously developed in our laboratory is applied to test the effect of different compounds on the activity of human aromatase. The assay is based on the detection of the alkali product that forms upon strong alkali treatment of the NADP released upon enzyme turnover. Here it is applied on human aromatase and validated using anastrozole and sildenafil as known aromatase inhibitors. Out of the small library of compounds tested, resveratrol and ketoconazole resulted to inhibit aromatase activity, while bisphenol A and nicotine were found to exert an inhibitory effect at relatively high concentrations (100µM), and other molecules such as lindane and four plasticizers did not show any significant effect. These data are confirmed by quantification of the product estrone in the same reaction mixtures through ELISA. Overall, the results show that the alkali assay is suitable to screen for molecules that interfere with aromatase activity. As a consequence it can also be applied to other molecular targets of EDCs that use NAD(P)H for catalysis in a high throughput format for the fast screening of many different compounds as endocrine disrupting chemicals. This article is part of a Special Issue entitled: Cytochrome P450 biodiversity and biotechnology, edited by Erika Plettner, Gianfranco Gilardi, Luet Wong, Vlada Urlacher, Jared Goldstone.
[Mh] Termos MeSH primário: Inibidores da Aromatase/química
Aromatase/química
Bioensaio
Disruptores Endócrinos/química
[Mh] Termos MeSH secundário: Aromatase/genética
Inibidores da Aromatase/análise
Compostos Benzidrílicos/análise
Compostos Benzidrílicos/química
Disruptores Endócrinos/análise
Ensaio de Imunoadsorção Enzimática
Estrona/química
Expressão Gênica
Seres Humanos
Cetoconazol/análise
Cetoconazol/química
Ligantes
NADP/química
Nicotina/análise
Nicotina/química
Nitrilos/análise
Nitrilos/química
Fenóis/análise
Fenóis/química
Ligação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Citrato de Sildenafila/análise
Citrato de Sildenafila/química
Bibliotecas de Moléculas Pequenas/análise
Bibliotecas de Moléculas Pequenas/química
Estilbenos/análise
Estilbenos/química
Triazóis/análise
Triazóis/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Aromatase Inhibitors); 0 (Benzhydryl Compounds); 0 (Endocrine Disruptors); 0 (Ligands); 0 (Nitriles); 0 (Phenols); 0 (Recombinant Proteins); 0 (Small Molecule Libraries); 0 (Stilbenes); 0 (Triazoles); 2DI9HA706A (Estrone); 2Z07MYW1AZ (anastrozole); 53-59-8 (NADP); 6M3C89ZY6R (Nicotine); BW9B0ZE037 (Sildenafil Citrate); EC 1.14.14.1 (Aromatase); EC 1.14.14.1 (CYP19A1 protein, human); MLT3645I99 (bisphenol A); Q369O8926L (resveratrol); R9400W927I (Ketoconazole)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170605
[St] Status:MEDLINE


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[PMID]:28905453
[Au] Autor:Neuzillet Y; Raynaud JP; Radulescu C; Fiet J; Giton F; Dreyfus JF; Ghoneim TP; Lebret T; Botto H
[Ad] Endereço:Department of Urology, University of Versailles-Saint-Quentin-en-Yvelines, Foch Hospital, Suresnes, France.
[Ti] Título:Sexual steroids in serum and prostatic tissue of human non-cancerous prostate (STERPROSER trial).
[So] Source:Prostate;77(15):1512-1519, 2017 Nov.
[Is] ISSN:1097-0045
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The specific involvement of the sex steroids in the growth of the prostatic tissue remains unclear. Sex steroid concentrations in plasma and in fresh surgical samples of benign central prostate were correlated to prostate volume. METHODS: Monocentric prospective study performed between September 2014 and January 2017. Age, obesity parameters, and both serum and intraprostatic concentrations of sex steroids were collected complying with the latest Endocrine Society guidelines and the steroids assessed by GC/MS. Statistical calculations were adjusted for age and body mass index (BMI). RESULTS: Thirty-two patients, equally divided between normal- and high-volume prostate groups, were included in the analysis. High-volume prostate patients were older, heavier and had higher BMI. Comparison adjusted for age and BMI showed higher DHT concentrations in high-volume prostate. Both normal- and high-volume prostate tissues concentrate sex steroids in a similar way. Comparison of enzymatic activity surrogate marker ratios within tissue highlighted similar TT/E1 and TT/E2 ratios, and higher DHT/E1 ratio and lower DHT/PSA ratio in the high-volume prostates. CONCLUSIONS: STERPROSER trial provides evidence for higher DHT concentration in highvolume prostates, that could reflect either higher 5-alpha reductase expression or lower expression of downstream metabolizing enzymes such as 3a-hydoxysteroid dehydrogenase.
[Mh] Termos MeSH primário: Hormônios Esteroides Gonadais/sangue
Hormônios Esteroides Gonadais/metabolismo
Próstata/metabolismo
[Mh] Termos MeSH secundário: Idoso
Androstenodiol/sangue
Androstenodiol/metabolismo
Índice de Massa Corporal
Desidroepiandrosterona/sangue
Desidroepiandrosterona/metabolismo
Sulfato de Desidroepiandrosterona/sangue
Sulfato de Desidroepiandrosterona/metabolismo
Di-Hidrotestosterona/sangue
Di-Hidrotestosterona/metabolismo
Estradiol/sangue
Estradiol/metabolismo
Estrona/sangue
Estrona/metabolismo
Cromatografia Gasosa-Espectrometria de Massas
Seres Humanos
Masculino
Meia-Idade
Estudos Prospectivos
Hiperplasia Prostática/sangue
Hiperplasia Prostática/metabolismo
Hiperplasia Prostática/cirurgia
Testosterona/sangue
Testosterona/metabolismo
Neoplasias da Bexiga Urinária/sangue
Neoplasias da Bexiga Urinária/metabolismo
Neoplasias da Bexiga Urinária/cirurgia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gonadal Steroid Hormones); 08J2K08A3Y (Dihydrotestosterone); 2DI9HA706A (Estrone); 3XMK78S47O (Testosterone); 459AG36T1B (Dehydroepiandrosterone); 4TI98Z838E (Estradiol); 57B09Q7FJR (Dehydroepiandrosterone Sulfate); 95PS51EMXY (Androstenediol)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170915
[St] Status:MEDLINE
[do] DOI:10.1002/pros.23429


  3 / 8115 MEDLINE  
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[PMID]:28867356
[Au] Autor:Liu J; Zhao R; Ye Z; Frey AJ; Schriver ER; Snyder NW; Hebbring SJ
[Ad] Endereço:Center for Human Genetics, Marshfield Clinic Research Foundation, Marshfield, WI, USA.
[Ti] Título:Relationship of SULT1A1 copy number variation with estrogen metabolism and human health.
[So] Source:J Steroid Biochem Mol Biol;174:169-175, 2017 Nov.
[Is] ISSN:1879-1220
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Human cytosolic sulfotransferase 1A1 (SULT1A1) is considered to be one of the most important SULT isoforms for metabolism, detoxification, and carcinogenesis. This theory is driven by observations that SULT1A1 is widely expressed in multiple tissues and acts on a wide range of phenolic substrates. SULT1A1 is subject to functional common copy number variation (CNV) including deletions or duplications. However, it is less clear how SULT1A1 CNV impacts health and disease. To better understand the biological role of SULT1A1 in human health, we genotyped CNV in 14,275 Marshfield Clinic patients linked to an extensive electronic health record. Since SULT1A1 is linked to steroid metabolism, select serum steroid hormones were measured in 100 individuals with a wide spectrum of SULT1A1 CNV genotypes. Furthermore, comprehensive phenome-wide association studies (PheWAS) were conducted using diagnostic codes and clinical text data. For the first time, individuals homozygous null for SULT1A1 were identified in a human population. Thirty-six percent of the population carried >2 copies of SULT1A1 whereas 4% had ≤1 copy. Results indicate SULT1A1 CNV was negatively correlated with estrone-sulfate to estrone ratio predominantly in males (E1S/E1; p=0.03, r=-0.21) and may be associated with increased risk for common allergies. The effect of SULT1A1 CNV on circulating estrogen metabolites was opposite to the predicted CNV-metabolite trend based on enzymatic function. This finding, and the potential association with common allergies reported herein, warrants future studies.
[Mh] Termos MeSH primário: Arilsulfotransferase/genética
Estrogênios/sangue
Estrona/análogos & derivados
[Mh] Termos MeSH secundário: Variações do Número de Cópias de DNA
Estrona/sangue
Feminino
Genótipo
Seres Humanos
Masculino
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Estrogens); 2DI9HA706A (Estrone); EC 2.8.2.1 (Arylsulfotransferase); EC 2.8.2.1 (SULT1A1 protein, human); QTL48N278K (estrone sulfate)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170905
[St] Status:MEDLINE


  4 / 8115 MEDLINE  
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[PMID]:28817836
[Au] Autor:Oh H; Arem H; Matthews CE; Wentzensen N; Reding KW; Brinton LA; Anderson GL; Coburn SB; Cauley JA; Chen C; Goodman D; Pfeiffer RM; Falk RT; Xu X; Trabert B
[Ad] Endereço:Division of Cancer Epidemiology and Genetics, National Cancer Institute, Bethesda, MD, USA.
[Ti] Título:Sitting, physical activity, and serum oestrogen metabolism in postmenopausal women: the Women's Health Initiative Observational Study.
[So] Source:Br J Cancer;117(7):1070-1078, 2017 Sep 26.
[Is] ISSN:1532-1827
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Prolonged sitting and lower levels of physical activity have been associated with increased levels of parent oestrogens (oestrone and oestradiol), the key hormones in female cancers, in postmenopausal women. However, it is unknown whether sitting and physical activity are associated with circulating oestrogen metabolite levels. METHODS: Among 1804 postmenopausal women enrolled in the Women's Health Initiative Observational Study, 15 serum oestrogens/oestrogen metabolites were quantified using liquid chromatography-tandem mass spectrometry. Physical activity and sitting were self-reported via questionnaire. Using baseline, cross-sectional data, geometric means (GM) of oestrogens/oestrogen metabolites (pmol l ) were estimated using inverse probability weighted linear regression, adjusting for potential confounders and stratified on menopausal hormone therapy (MHT) use. RESULTS: Longer time spent sitting (⩾10 vs ⩽5h per day) was associated with higher levels of unconjugated oestrone, independent of moderate- to vigorous-intensity physical activity and body mass index, among both never/former (GM=70.6 vs 57.7) and current MHT users (GM=242 vs 179) (P-trend ⩽0.03). Among never/former MHT users, sitting (⩾10 vs ⩽5h per day) was positively associated with 2-methoxyestradiol (GM=16.4 vs 14.4) and 4-methoxyestradiol (GM=2.36 vs 1.98) (P-trend ⩽0.04), independent of parent oestrogens. Inverse associations between moderate- to vigorous-intensity physical activity (⩾15 vs 0 metabolic equivalent task-hours per week) and parent oestrogens were found as expected. After adjustment for parent oestrogens, physical activity was not associated with oestrogen metabolites. CONCLUSIONS: Our data suggest that prolonged sitting and lower moderate- to vigorous-intensity physical activity are associated with higher levels of postmenopausal oestrogens/oestrogen metabolites, the oestrogen metabolism patterns that have previously been associated with higher endometrial and breast cancer risk.
[Mh] Termos MeSH primário: Estradiol/análogos & derivados
Estrogênios/sangue
Estrona/sangue
Exercício/fisiologia
Estilo de Vida Sedentário
[Mh] Termos MeSH secundário: Idoso
Estradiol/sangue
Feminino
Terapia de Reposição Hormonal
Seres Humanos
Meia-Idade
Pós-Menopausa/sangue
Postura/fisiologia
Inquéritos e Questionários
[Pt] Tipo de publicação:JOURNAL ARTICLE; OBSERVATIONAL STUDY
[Nm] Nome de substância:
0 (Estrogens); 26788-23-8 (4-methoxyestradiol); 2DI9HA706A (Estrone); 4TI98Z838E (Estradiol); 6I2QW73SR5 (2-methoxyestradiol)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170818
[St] Status:MEDLINE
[do] DOI:10.1038/bjc.2017.268


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[PMID]:28750898
[Au] Autor:Caron-Beaudoin E; Viau R; Hudon-Thibeault AA; Vaillancourt C; Sanderson JT
[Ad] Endereço:INRS - Institut Armand-Frappier, Laval, QC H7V 1B7, Canada; Center for Interdisciplinary Research on Well-Being, Health, Society and Environment (CINBIOSE), Université du Québec à Montréal, Montreal, QC H3C 3P8, Canada. Electronic address: elyse.caron-beaudoin@iaf.inrs.ca.
[Ti] Título:The use of a unique co-culture model of fetoplacental steroidogenesis as a screening tool for endocrine disruptors: The effects of neonicotinoids on aromatase activity and hormone production.
[So] Source:Toxicol Appl Pharmacol;332:15-24, 2017 Oct 01.
[Is] ISSN:1096-0333
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Estrogen biosynthesis during pregnancy is dependent on the collaboration between the fetus producing the androgen precursors, and the placenta expressing the enzyme aromatase (CYP19). Disruption of estrogen production by contaminants may result in serious pregnancy outcomes. We used our recently developed in vitro co-culture model of fetoplacental steroidogenesis to screen the effects of three neonicotinoid insecticides on the catalytic activity of aromatase and the production of steroid hormones. A co-culture of H295R human adrenocortical carcinoma cells with fetal characteristics and BeWo human choriocarcinoma cells which display characteristics of the villous cytotrophoblast was exposed for 24h to various concentrations of three neonicotinoids: thiacloprid, thiamethoxam and imidacloprid. Aromatase catalytic activity was determined in both cell lines using the tritiated water-release assay. Hormone production was measured by ELISA. The three neonicotinoids induced aromatase activity in our fetoplacental co-culture and concordingly, estradiol and estrone production were increased. In contrast, estriol production was strongly inhibited by the neonicotinoids. All three pesticides induced the expression of CYP3A7 in H295R cells, and this induction was reversed by co-treatment of H295R cells with exogenous estriol. CYP3A7 is normally expressed in fetal liver and is a key enzyme involved in estriol synthesis. We suggest that neonicotinoids are metabolized by CYP3A7, thus impeding the 16α-hydroxylation of fetal DHEA(-sulfate), which is normally converted to estriol by placental aromatase. We successfully used the fetoplacental co-culture as a physiologically relevant tool to highlight the potential effects of neonicotinoids on estrogen production, aromatase activity and CYP3A7 expression during pregnancy.
[Mh] Termos MeSH primário: Aromatase/metabolismo
Técnicas de Cocultura/métodos
Disruptores Endócrinos/toxicidade
Inseticidas/toxicidade
Placenta/efeitos dos fármacos
[Mh] Termos MeSH secundário: Carcinoma Adrenocortical
Linhagem Celular Tumoral
Coriocarcinoma/induzido quimicamente
Coriocarcinoma/diagnóstico
Citocromo P-450 CYP3A/genética
Citocromo P-450 CYP3A/metabolismo
Estradiol/metabolismo
Estrogênios/metabolismo
Estrona/metabolismo
Feminino
Regulação da Expressão Gênica
Seres Humanos
Imidazóis/toxicidade
Neonicotinoides
Nitrocompostos/toxicidade
Oxazinas/toxicidade
Placenta/metabolismo
Gravidez
Piridinas/toxicidade
Tiazinas/toxicidade
Tiazóis/toxicidade
Neoplasias Uterinas/induzido quimicamente
Neoplasias Uterinas/diagnóstico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Endocrine Disruptors); 0 (Estrogens); 0 (Imidazoles); 0 (Insecticides); 0 (Neonicotinoids); 0 (Nitro Compounds); 0 (Oxazines); 0 (Pyridines); 0 (Thiazines); 0 (Thiazoles); 2DI9HA706A (Estrone); 3BN7M937V8 (imidacloprid); 4TI98Z838E (Estradiol); 747IC8B487 (thiamethoxam); DSV3A944A4 (thiacloprid); EC 1.14.14.1 (Aromatase); EC 1.14.14.1 (CYP19A1 protein, human); EC 1.14.14.1 (CYP3A7 protein, human); EC 1.14.14.1 (Cytochrome P-450 CYP3A)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170729
[St] Status:MEDLINE


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[PMID]:28728122
[Au] Autor:Xiao S; Lv X; Zeng Y; Jin T; Luo L; Zhang B; Zhang G; Wang Y; Feng L; Zhu Y; Tang F
[Ad] Endereço:Institute of Environmental Medicine, MOE Key Lab of Environment and Health, School of Public Health, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China.
[Ti] Título:Mutagenicity and estrogenicity of raw water and drinking water in an industrialized city in the Yangtze River Delta.
[So] Source:Chemosphere;185:647-655, 2017 Oct.
[Is] ISSN:1879-1298
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Public concern was aroused by frequently reported water pollution incidents in Taihu Lake and the Yangtze River. The pollution also caught and sustained the attention of the scientific community. From 2010 to 2016, raw water and drinking water samples were continually collected at Waterworks A and B (Taihu Lake) and Waterworks C (Yangtze River). The non-volatile organic pollutants in the water samples were extracted by solid phase extraction. Ames tests and yeast estrogen screen (YES) assays were conducted to evaluate the respective mutagenic and estrogenic effects. Water samples from the Yangtze River-based Waterworks C possessed higher mutagenicity than those from Taihu Lake-based Waterworks A (P<0.001) and Waterworks B (P = 0.026). Water treatment enhanced the direct mutagenicity (P = 0.022), and weakened the estrogenicity of the raw water (P<0.001) with a median removal rate of 100%. In fact, very few of the finished samples showed estrogenic activity. Raw water samples from Waterworks A showed weaker estrogenicity than those from Waterworks B (P = 0.034) and Waterworks C (P = 0.006). In summary, mutagenic effects in drinking water and estrogenic effects in raw water merited sustained attention. The Yangtze River was more seriously polluted by mutagenic and estrogenic chemicals than Taihu Lake was.
[Mh] Termos MeSH primário: Água Potável/química
Estrogênios/análise
Mutagênicos/análise
Poluentes Químicos da Água/análise
Abastecimento de Água/estatística & dados numéricos
[Mh] Termos MeSH secundário: Cidades
Estrogênios/toxicidade
Estrona
Indústrias
Lagos
Mutagênese
Mutagênicos/toxicidade
Rios
Poluentes Químicos da Água/toxicidade
Purificação da Água
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drinking Water); 0 (Estrogens); 0 (Mutagens); 0 (Water Pollutants, Chemical); 2DI9HA706A (Estrone)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170721
[St] Status:MEDLINE


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[PMID]:28688342
[Au] Autor:Siewiera P; Rózalska S; Bernat P
[Ad] Endereço:Department of Industrial Microbiology and Biotechnology, Faculty of Biology and Environmental Protection, University of Lodz, Banacha 12/16, 90-237 Lodz, Poland.
[Ti] Título:Estrogen-mediated protection of the organotin-degrading strain Metarhizium robertsii against oxidative stress promoted by monobutyltin.
[So] Source:Chemosphere;185:96-104, 2017 Oct.
[Is] ISSN:1879-1298
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Dibutyltin (DBT) is a global pollutant characterized by pro-oxidative properties. The fungal strain Metarhizium robertsii can eliminate high levels of DBT efficiently. In this study, induction of oxidative stress as well as its alleviation through the application of natural estrogens during the elimination of DBT by M. robertsii were evaluated. During the first 24 h of incubation, the initial concentration of DBT (20 mg l ) was reduced to 3.1 mg l , with simultaneous formation of a major byproduct - monobutyltin (MBT). In the presence of estrone (E1) or 17ß-estradiol (E2), the amounts of dibutyltin residues in the fungal cultures were found to be approximately 2-fold higher compared to cultures without estrogens, which was associated with the simultaneous utilization of the compounds by cytochrome P450 enzymes. On the other hand, MBT levels were approximately 2.5 times lower in the fungal cultures with the addition of one of the estrogens. MBT (not DBT) promotes the generation of O , H O , and NO at levels 65.89 ± 18.08, 4.04 ± 3.62, and 27.92 ± 1.95, respectively. Superoxide dismutase and catalase activities did not show any response of the M. robertsii strain against the overproduction of superoxide anion and hydrogen peroxide. Application of E1 as well as E2 ensured non-enzymatic defense against nitrosative and oxidative stress through scavenging of nitrogen and oxygen reactive species, and limited their levels from 1.5-fold to 21-fold, depending on the used estrogen.
[Mh] Termos MeSH primário: Estrogênios/metabolismo
Metarhizium/fisiologia
Compostos Orgânicos de Estanho/toxicidade
[Mh] Termos MeSH secundário: Estradiol
Estrona
Peróxido de Hidrogênio
Metarhizium/metabolismo
Oxirredução
Estresse Oxidativo
Espécies Reativas de Oxigênio
Superóxido Dismutase
Superóxidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Estrogens); 0 (Organotin Compounds); 0 (Reactive Oxygen Species); 0 (mono-n-butyltin); 1002-53-5 (di-n-butyltin); 11062-77-4 (Superoxides); 2DI9HA706A (Estrone); 4TI98Z838E (Estradiol); BBX060AN9V (Hydrogen Peroxide); EC 1.15.1.1 (Superoxide Dismutase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170709
[St] Status:MEDLINE


  8 / 8115 MEDLINE  
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[PMID]:28686938
[Au] Autor:Du Z; Chen Y; Li X
[Ad] Endereço:Department of Civil Engineering, University of Nebraska-Lincoln, USA.
[Ti] Título:Quantitative proteomic analyses of the microbial degradation of estrone under various background nitrogen and carbon conditions.
[So] Source:Water Res;123:361-368, 2017 Oct 15.
[Is] ISSN:1879-2448
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Microbial degradation of estrogenic compounds can be affected by the nitrogen source and background carbon in the environment. However, the underlying mechanisms are not well understood. The objective of this study was to elucidate the molecular mechanisms of estrone (E1) biodegradation at the protein level under various background nitrogen (nitrate or ammonium) and carbon conditions (no background carbon, acetic acid, or humic acid as background carbon) by a newly isolated bacterial strain. The E1 degrading bacterial strain, Hydrogenophaga atypica ZD1, was isolated from river sediments and its proteome was characterized under various experimental conditions using quantitative proteomics. Results show that the E1 degradation rate was faster when ammonium was used as the nitrogen source than with nitrate. The degradation rate was also faster when either acetic acid or humic acid was present in the background. Proteomics analyses suggested that the E1 biodegradation products enter the tyrosine metabolism pathway. Compared to nitrate, ammonium likely promoted E1 degradation by increasing the activities of the branched-chain-amino-acid aminotransferase (IlvE) and enzymes involved in the glutamine synthetase-glutamine oxoglutarate aminotransferase (GS-GOGAT) pathway. The increased E1 degradation rate with acetic acid or humic acid in the background can also be attributed to the up-regulation of IlvE. Results from this study can help predict and explain E1 biodegradation kinetics under various environmental conditions.
[Mh] Termos MeSH primário: Estrona/genética
Proteômica
[Mh] Termos MeSH secundário: Biodegradação Ambiental
Carbono
Monitoramento Ambiental
Estrona/análise
Nitrogênio/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
2DI9HA706A (Estrone); 7440-44-0 (Carbon); N762921K75 (Nitrogen)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170708
[St] Status:MEDLINE


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[PMID]:28669870
[Au] Autor:Chen J; Feng W; Zhao Y
[Ad] Endereço:Department of Forensic Biology, Henan University of Science and Technology, Luoyang 471023, China. Electronic address: cj11091@haust.edu.cn.
[Ti] Título:Secretory expression, purification and functional characterization of 17ß-hydroxysteroid dehydrogenase type 1 from mammalian HEK293T cells.
[So] Source:Protein Expr Purif;137:52-57, 2017 Sep.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:17ß-hydroxysteroid dehydrogenase type 1 (17ß-HSD1) mainly catalyzes the reduction of estrone into estradiol. The enzymatic conversion is a critical step in estradiol accumulation in breast tissue, which is a valuable prognosis index of breast cancer disease. However, the source of 17ß-HSD1 for inhibitor design is limited. In this study, the fragment encoding human 17ß-HSD1 was successfully cloned and expressed in human embryonic kidney (HEK) 293T mammalian cells. The recombinant protein was purified by immobilized metal ion affinity chromatography yielding above 17 mg of purified 17ß-HSD1 protein per liter of cell culture, with a specific activity of 8.54 µmoL/min/mg of protein for conversion of estradiol into estrone, with NAD as cofactor at pH 9.2. Enzyme characterization studies revealed that the protein has estrogenic activity and the K value for estrone is about 20 nM. The recombinant protein purified from transfected HEK293T cells had higher specific activity compared to that of the enzyme purified directly from placenta. The present data show that the mammalian cell expression system can provide active 17ß-HSD1 which is functionally identical to its natural counterpart and easy to purify in qualities suitable for its structure-function study.
[Mh] Termos MeSH primário: 17-Hidroxiesteroide Desidrogenases
Estrona/química
Expressão Gênica
[Mh] Termos MeSH secundário: 17-Hidroxiesteroide Desidrogenases/biossíntese
17-Hidroxiesteroide Desidrogenases/química
17-Hidroxiesteroide Desidrogenases/genética
17-Hidroxiesteroide Desidrogenases/isolamento & purificação
Cromatografia de Afinidade/métodos
Células HEK293
Seres Humanos
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Proteins); 2DI9HA706A (Estrone); EC 1.1.- (17-Hydroxysteroid Dehydrogenases); EC 1.1.1.51 (3 (or 17)-beta-hydroxysteroid dehydrogenase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170704
[St] Status:MEDLINE


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[PMID]:28630284
[Au] Autor:Burckhardt BC; Henjakovic M; Hagos Y; Burckhardt G
[Ad] Endereço:Center of Physiology and Pathophysiology, University Medical Center Goettingen, Goettingen, Germany (B.C.B, M.H., Y.H., G.B.); Department I of Internal Medicine, University Medical Center Cologne, Cologne, Germany (M.H.); and PortaCellTec Biosciences GmbH, Goettingen, Germany (Y.H.) birgitta.burckha
[Ti] Título:Differential Interaction of Dantrolene, Glafenine, Nalidixic Acid, and Prazosin with Human Organic Anion Transporters 1 and 3.
[So] Source:J Pharmacol Exp Ther;362(3):450-458, 2017 Sep.
[Is] ISSN:1521-0103
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In renal proximal tubule cells, the organic anion transporters 1 and 3 (OAT1 and OAT3) in the basolateral membrane and the multidrug resistance-associated protein 4 (MRP4) in the apical membrane share substrates and co-operate in renal drug secretion. We hypothesized that recently identified MRP4 inhibitors dantrolene, glafenine, nalidixic acid, and prazosin also interact with human OAT1 and/or OAT3 stably transfected in human embryonic kidney 293 cells. These four drugs were tested as possible inhibitors of -[ H]aminohippurate (PAH) and [ C]glutarate uptake by OAT1, and of [ H]estrone-3-sulfate (ES) uptake by OAT3. In addition, we explored whether these drugs decrease the equilibrium distribution of radiolabeled PAH, glutarate, or ES, an approach intended to indirectly suggest drug/substrate exchange through OAT1 and OAT3. With OAT3, a dose-dependent inhibition of [ H]ES uptake and a downward shift in [ H]ES equilibrium were observed, indicating that all four drugs bind to OAT3 and may possibly be translocated. In contrast, the interaction with OAT1 was more complex. With [ C]glutarate as substrate, all four drugs inhibited uptake but only glafenine and nalidixic acid shifted glutarate equilibrium. Using [ H]PAH as a substrate of OAT1, nalidixic acid inhibited but dantrolene, glafenine, and prazosin stimulated uptake. Nalidixic acid decreased equilibrium content of [ H]PAH, suggesting that it may possibly be exchanged by OAT1. Taken together, OAT1 and OAT3 interact with the MRP4 inhibitors dantrolene, glafenine, nalidixic acid, and prazosin, indicating overlapping specificities. At OAT1, more than one binding site must be assumed to explain substrate and drug-dependent stimulation and inhibition of transport activity.
[Mh] Termos MeSH primário: Dantroleno/metabolismo
Glafenina/metabolismo
Ácido Nalidíxico/metabolismo
Proteína 1 Transportadora de Ânions Orgânicos/metabolismo
Transportadores de Ânions Orgânicos Sódio-Independentes/metabolismo
Prazosina/metabolismo
[Mh] Termos MeSH secundário: Ligação Competitiva
Técnicas de Cultura de Células
Estrona/análogos & derivados
Estrona/metabolismo
Células HEK293
Seres Humanos
Taxa de Depuração Metabólica
Proteína 1 Transportadora de Ânions Orgânicos/genética
Transportadores de Ânions Orgânicos Sódio-Independentes/genética
Ligação Proteica
Ensaio Radioligante
Eliminação Renal
Especificidade por Substrato
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Organic Anion Transport Protein 1); 0 (Organic Anion Transporters, Sodium-Independent); 0 (organic anion transport protein 3); 2DI9HA706A (Estrone); 3B91HWA56M (Nalidixic Acid); 46HL4I09AH (Glafenine); F64QU97QCR (Dantrolene); QTL48N278K (estrone sulfate); XM03YJ541D (Prazosin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170621
[St] Status:MEDLINE
[do] DOI:10.1124/jpet.117.241406



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