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[PMID]:29277760
[Au] Autor:Glei M; Fischer S; Lamberty J; Ludwig D; Lorkowski S; Schlörmann W
[Ad] Endereço:Friedrich Schiller University Jena, Institute of Nutrition, Department of Nutritional Toxicology, Jena, Germany.
[Ti] Título:Chemopreventive Potential of Fermented Raw and Roasted Hazelnuts in LT97 Colon Adenoma Cells.
[So] Source:Anticancer Res;38(1):83-93, 2018 01.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: Due to their unique composition of health-promoting compounds, the consumption of hazelnuts may contribute to the prevention of colon cancer. MATERIALS AND METHODS: Since hazelnuts are often consumed roasted, the impact of different roasting conditions (RC1=140.6°C/25 min, RC2=155.1°C/20 min and RC3=180.4°C/21 min) on chemopreventive effects of in vitro fermented hazelnuts was analyzed in LT97 colon adenoma cells. RESULTS: FS (2.5%) of raw and roasted hazelnuts reduced H O -induced DNA damage while 5% FS significantly induced gene expression of SOD2 (3.0-fold) and GSTP1 (2.1-fold). GPx1 mRNA levels were significantly decreased (0.6-fold) by FS (2.5%). The growth of LT97 cells was significantly reduced by hazelnut FS in a time- and dose-dependent manner. Hazelnut FS (5%) increased the numbers of early apoptotic cells (9.6% on average) and caspase-3 activities (6.4-fold on average). CONCLUSION: These results indicate a chemopreventive potential of in vitro fermented hazelnuts which is largely unaffected by the roasting process.
[Mh] Termos MeSH primário: Adenoma/tratamento farmacológico
Anticarcinógenos/farmacologia
Antineoplásicos/farmacologia
Neoplasias do Colo/tratamento farmacológico
Corylus
Preparações de Plantas/farmacologia
[Mh] Termos MeSH secundário: Adenoma/genética
Adenoma/prevenção & controle
Apoptose/efeitos dos fármacos
Catalase/genética
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Neoplasias do Colo/genética
Neoplasias do Colo/prevenção & controle
Culinária
Dano ao DNA/efeitos dos fármacos
Glutationa Peroxidase/genética
Glutationa S-Transferase pi/genética
Seres Humanos
Peróxido de Hidrogênio/toxicidade
Nozes
RNA Mensageiro/metabolismo
Superóxido Dismutase-1/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anticarcinogenic Agents); 0 (Antineoplastic Agents); 0 (Plant Preparations); 0 (RNA, Messenger); 0 (SOD1 protein, human); BBX060AN9V (Hydrogen Peroxide); EC 1.11.1.- (glutathione peroxidase GPX1); EC 1.11.1.6 (Catalase); EC 1.11.1.9 (Glutathione Peroxidase); EC 1.15.1.1 (Superoxide Dismutase-1); EC 2.5.1.18 (GSTP1 protein, human); EC 2.5.1.18 (Glutathione S-Transferase pi)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171227
[St] Status:MEDLINE


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[PMID]:28899750
[Au] Autor:Mizukami S; Watanabe Y; Saegusa Y; Nakajima K; Ito Y; Masubuchi Y; Yoshida T; Shibutani M
[Ad] Endereço:Laboratory of Veterinary Pathology, Division of Animal Life Science, Institute of Agriculture, Tokyo University of Agriculture and Technology, 3-5-8 Saiwai-cho, Fuchu-shi, Tokyo 183-8509, Japan; Pathogenetic Veterinary Science, United Graduate School of Veterinary Sciences, Gifu University, 1-1 Yana
[Ti] Título:Downregulation of UBE2E2 in rat liver cells after hepatocarcinogen treatment facilitates cell proliferation and slowing down of DNA damage response in GST-P-expressing preneoplastic lesions.
[So] Source:Toxicol Appl Pharmacol;334:207-216, 2017 Nov 01.
[Is] ISSN:1096-0333
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We previously found downregulation of ubiquitin-conjugating enzyme E2E 2 (UBE2E2) in GST-P-positive proliferative lesions produced by tumor promotion from early hepatocarcinogenesis stages in rats. Here we investigated the role of UBE2E2 downregulation in preneoplastic lesions of the liver and other target organs produced by tumor promotion in rats. Increased number of UBE2E2-related ubiquitination target proteins, phosphorylated c-MYC, KDM4A and KMT5A, was found in the UBE2E2-downregulated GST-P foci, compared with GST-P foci expressing UBE2E2. However, p21 , another UBE2E2 target protein, did not increase in the positive cells. Furthermore, the numbers of PCNA cells and γH2AX cells were increased in UBE2E2-downregulated foci. These results suggest sustained activation of c-MYC and stabilization of KMT5A to result in c-MYC-mediated transcript upregulation and following KMT5A-mediated protein stabilization of PCNA in GST-P foci, as well as KDM4A stabilization resulting in slowing down of DNA damage response in these lesions. Similar results were also observed in GST-P foci produced by repeated treatment of rats with a hepatocarcinogen, thioacetamide, for 90days. Hepatocarcinogen treatment for 28 or 90days also increased the numbers of liver cells expressing UBE2E2-related ubiquitination target proteins, as well as PCNA or γH2AX cells. Conversely, UBE2E2 downregulation was lacking in PPARα agonist-induced hepatocarcinogenesis, as well as in carcinogenic processes targeting other organs, suggestive of the loss of UBE2E2-related ubiquitination limited to hepatocarcinogenesis producing GST-P proliferative lesions. Our results suggest that repeated hepatocarcinogen treatment of rats causes stabilization of UBE2E2-related ubiquitination target proteins in liver cells to promote carcinogenesis.
[Mh] Termos MeSH primário: Carcinógenos/toxicidade
Proliferação Celular/efeitos dos fármacos
Dano ao DNA/efeitos dos fármacos
Glutationa S-Transferase pi/metabolismo
Hepatócitos/efeitos dos fármacos
Ubiquitina-Proteína Ligases/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose
Reparo do DNA
Regulação para Baixo
Regulação da Expressão Gênica
Glutationa S-Transferase pi/genética
Lesões Pré-Cancerosas/induzido quimicamente
Distribuição Aleatória
Ratos
Ubiquitina-Proteína Ligases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carcinogens); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.5.1.18 (Glutathione S-Transferase pi); EC 2.5.1.18 (Gstp1 protein, rat); EC 6.3.2.19 (UBE2E2 protein, rat)
[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:170914
[St] Status:MEDLINE


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[PMID]:28882992
[Au] Autor:Lin; Kostov R; Huang JT; Henderson CJ; Wolf CR
[Ad] Endereço:Division of Cancer Research, Jacqui Wood Cancer Centre (D.L., C.J.H., C.R.W.), Molecular & Cellular Medicine (R.K.), and Biomarker & Drug Analysis Core (J.T.-J.H.), School of Medicine, Ninewells Hospital, University of Dundee, Dundee, United Kingdom.
[Ti] Título:Novel Pathways of Ponatinib Disposition Catalyzed By CYP1A1 Involving Generation of Potentially Toxic Metabolites.
[So] Source:J Pharmacol Exp Ther;363(1):12-19, 2017 Oct.
[Is] ISSN:1521-0103
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ponatinib, a pan-BCR-ABL tyrosine kinase inhibitor for the treatment of chronic myeloid leukemia (CML), causes severe side effects including vascular occlusions, pancreatitis, and liver toxicity, although the underlying mechanisms remain unclear. Modifications of critical proteins through reactive metabolites are thought to be responsible for a number of adverse drug reactions. In vitro metabolite screening of ponatinib with human liver microsomes and glutathione revealed unambiguous signals of ponatinib-glutathione (P-GSH) adducts. Further profiling of human cytochrome P450 (P450) indicated that CYP1A1 was the predominant P450 enzyme driving this reaction. P-GSH conjugate formation paralleled the disappearance of hydroxylated ponatinib metabolites, suggesting the initial reaction was epoxide generation. Mouse glutathione -transferase p1 (mGstp1) further enhanced P-GSH adduct formation in vitro. Ponatinib pharmacokinetics were determined in vivo in wild-type (WT) mice and mice humanized for CYP1A1/2 and treated with the CYP1A1 inducers 2,3,7,8-tetrachlorodibenzodioxin or 3-methylcholanthrene. Ponatinib exposure was significantly decreased in treated mice compared with controls (7.7- and 2.2-fold for WT and humanized CYP1A1/2, respectively). Interestingly, the P-GSH conjugate was only found in the feces of CYP1A1-induced mice, but not in control animals. Protein adducts were also identified by liquid chromatography-tandem mass spectrometry analysis of mGstp1 tryptic digests. These results indicate that not only could CYP1A1 be involved in ponatinib disposition, which has not been previously reported, but also that electrophilic intermediates resulting from CYP1A1 metabolism in normal tissues may contribute to ponatinib toxicity. These data are consistent with a recent report that CML patients who smoke are at greater risk of disease progression and premature death.
[Mh] Termos MeSH primário: Biocatálise
Citocromo P-450 CYP1A1/metabolismo
Imidazóis/metabolismo
Piridazinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Glutationa/metabolismo
Glutationa S-Transferase pi/metabolismo
Seres Humanos
Imidazóis/toxicidade
Masculino
Camundongos
Piridazinas/toxicidade
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Imidazoles); 0 (Pyridazines); 0 (Recombinant Proteins); 4340891KFS (ponatinib); EC 1.14.14.1 (Cytochrome P-450 CYP1A1); EC 2.5.1.18 (Glutathione S-Transferase pi); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170909
[St] Status:MEDLINE
[do] DOI:10.1124/jpet.117.243246


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[PMID]:28770368
[Au] Autor:Minina VI; Soboleva OA; Glushkov AN; Voronina EN; Sokolova EA; Bakanova ML; Savchenko YA; Ryzhkova AV; Titov RA; Druzhinin VG; Sinitsky MY; Asanov MA
[Ad] Endereço:Federal State Budget Scientific Institution, The Federal Research Center of Coal and Coal Chemistry of Siberian Branch of the Russian Academy of Sciences, Sovetskiy Ave 18, Kemerovo, 650065, Russian Federation. vminina@mail.ru.
[Ti] Título:Polymorphisms of GSTM1, GSTT1, GSTP1 genes and chromosomal aberrations in lung cancer patients.
[So] Source:J Cancer Res Clin Oncol;143(11):2235-2243, 2017 Nov.
[Is] ISSN:1432-1335
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:PURPOSE: To study the potential links between genetic polymorphisms in the GSTT1, GSTM1, GSTP1 genes and the frequency of chromosomal aberrations (CAs) in lung cancer patients and healthy residents in Russian Federation. METHODS: 200 cells in well-spread metaphase with 46 chromosomes were examined for 353 newly diagnosed lung cancer patients (males) who received medical treatment in the Kemerovo Regional Oncology Center (Kemerovo, Russian Federation), and 300 healthy males from Kemerovo, Russian Federation. The polymorphisms of the GSTM1 del and GSTT1 del genes were analysed by multiplex PCR. Genotyping of the polymorphic variants in the GSTP1 (A313G, T341C) gene was performed using Real-time PCR with competing TaqMan probes complementary to the polymorphic DNA sites. The data analysis was performed using software STATISTICA 8.0 (StatSoft Inc., USA). RESULTS: We discovered that a GSTM1 del polymorphism increases the frequency of chromosomal damage in smoking patients with lung cancer, a general group of lung cancer patients, donors with non-small cell lung cancer and patients in the latest stages of the malignant process. The synergetic effects of occupational exposure and the malignant process can induce some modifications in the cytogenetic status in lung cancer patients harbouring the GSTM1 del polymorphism. CONCLUSIONS: CAs in peripheral blood lymphocytes can be used as biomarkers of the early biological effects of exposure to genotoxic carcinogens and may predict future cancer incidence in several epidemiologic studies. Genetic changes in genes encoding phase II detoxification enzymes are linked to decreases in the metabolic detoxification of environmentally derived genotoxic carcinogens.
[Mh] Termos MeSH primário: Carcinoma Pulmonar de Células não Pequenas/genética
Aberrações Cromossômicas
Glutationa S-Transferase pi/genética
Glutationa Transferase/genética
Polimorfismo Genético/genética
Carcinoma de Pequenas Células do Pulmão/genética
[Mh] Termos MeSH secundário: Biomarcadores Tumorais/genética
Carcinoma Pulmonar de Células não Pequenas/patologia
Feminino
Seguimentos
Seres Humanos
Neoplasias Pulmonares/genética
Neoplasias Pulmonares/patologia
Masculino
Meia-Idade
Estadiamento de Neoplasias
Prognóstico
Carcinoma de Pequenas Células do Pulmão/patologia
Taxa de Sobrevida
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); EC 2.5.1.- (glutathione S-transferase T1); EC 2.5.1.18 (GSTP1 protein, human); EC 2.5.1.18 (Glutathione S-Transferase pi); EC 2.5.1.18 (Glutathione Transferase); EC 2.5.1.18 (glutathione S-transferase M1)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170804
[St] Status:MEDLINE
[do] DOI:10.1007/s00432-017-2486-3


  5 / 2258 MEDLINE  
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[PMID]:28700487
[Au] Autor:Sheng X; Guo Y; Lu Y
[Ad] Endereço:aDepartment of Thyroid and Breast Surgery, Ningbo First Hospital bMedical School of Ningbo University, Ningbo, Zhejiang, China.
[Ti] Título:Prognostic role of methylated GSTP1, p16, ESR1 and PITX2 in patients with breast cancer: A systematic meta-analysis under the guideline of PRISMA.
[So] Source:Medicine (Baltimore);96(28):e7476, 2017 Jul.
[Is] ISSN:1536-5964
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: BRCA1 and RASSF1A promoter methylation has been reported to be correlated with a worse survival in patients with breast cancer. However, the prognostic values of GSTP1, p16, ESR1, and PITX2 promoter methylation in breast cancer remain to be determined. Here, we performed this study to evaluate the prognostic significance of GSTP1, p16, ESR1, and PITX2 promoter methylation in breast cancer. METHODS: A range of online databases was systematically searched to identify available studies based on the Preferred Reporting Items for Systematic reviews and Meta-Analyses (PRISMA) guideline. The pooled hazard ratios (HRs) with their 95% confidence intervals (95% CIs) were applied to estimate the prognostic effect of GSTP1, p16, ESR1, and PITX2 promoter methylation in breast cancer for multivariate regression analysis. RESULTS: 13 eligible articles involving 3915 patients with breast cancer were analyzed in this meta-analysis. In a large patient population, GSTP1 showed a trend toward a worse prognosis in overall survival (OS) (HR = 1.64, 95% CI = 0.93-2.87, P = .085). PITX2 promoter methylation was significantly correlated with a worse prognosis in OS (HR = 1.57, 95% CI = 1.15-2.14, P = .004), but no association between p16 promoter methylation and OS (HR = 0.92, 95% CI = 0.31-2.71, P = .884). PITX2 promoter methylation was significantly correlated with an unfavorable prognosis of patients with breast cancer in metastasis-free survival (MFS) (HR = 1.73, 95% CI = 1.33-2.26, P < .001). The result from 3 studies with 227 cases showed that ESR1 promoter methylation was linked to a worse prognosis in OS (HR = 1.55, 95% CI = 1.06-2.28, P = .025). CONCLUSIONS: Our findings suggest ESR1 and PITX2 promoter methylation may be correlated with a worse survival of patients with breast cancer (ESR1: OS, PITX2: OS and MFS). The clinical utility of aberrantly methylated ESR1 and PITX2 could be a promising factor for the prognosis of breast cancer.
[Mh] Termos MeSH primário: Neoplasias da Mama/genética
Inibidor p16 de Quinase Dependente de Ciclina/genética
Receptor alfa de Estrogênio/genética
Glutationa S-Transferase pi/genética
Proteínas de Homeodomínio/genética
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Biomarcadores Tumorais/genética
Neoplasias da Mama/diagnóstico
Metilação de DNA
Seres Humanos
Prognóstico
Regiões Promotoras Genéticas
[Pt] Tipo de publicação:JOURNAL ARTICLE; META-ANALYSIS
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Cyclin-Dependent Kinase Inhibitor p16); 0 (Estrogen Receptor alpha); 0 (Homeodomain Proteins); 0 (P16 protein, human); 0 (Transcription Factors); 0 (estrogen receptor alpha, human); 184787-43-7 (homeobox protein PITX2); EC 2.5.1.18 (GSTP1 protein, human); EC 2.5.1.18 (Glutathione S-Transferase pi)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170730
[Lr] Data última revisão:
170730
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE
[do] DOI:10.1097/MD.0000000000007476


  6 / 2258 MEDLINE  
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[PMID]:28699644
[Au] Autor:Kormann R; Jannot AS; Narjoz C; Ribeil JA; Manceau S; Delville M; Joste V; Prié D; Pouchot J; Thervet E; Courbebaisse M; Arlet JB
[Ad] Endereço:Physiology Department, Georges Pompidou European Hospital, Assistance Publique-Hôpitaux de Paris, Paris, France.
[Ti] Título:Roles of APOL1 G1 and G2 variants in sickle cell disease patients: kidney is the main target.
[So] Source:Br J Haematol;179(2):323-335, 2017 Oct.
[Is] ISSN:1365-2141
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In African-American patients with sickle cell disease (SCD), APOL1 G1 and G2 variants are associated with increased risk of sickle cell nephropathy (SCN). To determine the role of APOL1 variants in SCD patients living in Europe, we genotyped 152 SCD patients [aged 30·4 (24·3-36·4) years], mainly of Sub-Saharan African ancestry, for APOL1 G1 and G2 and for variants of four genes with kidney tropism (GSTM1, GSTT1, GSTP1, and HMOX1). Homozygous or double-heterozygous APOL G1 and G2 genotypes were strongly associated with end stage renal disease (P = 0·003) and worse Kidney Disease: Improving Global Outcomes stages (P = 0·001). Further, these genotypes were associated in an age-dependent manner with lower estimated glomerular filtration rate (eGFR, P = 0·008), proteinuria (P = 0·009) and albuminuria (P < 0·001) but not with other SCD complications. Compared to APOL1 G1/wild type (WT), the APOL1 G2/WT genotype was associated with a lower eGFR (P = 0·04) in an age-dependent manner, suggesting that the G2/WT patients are likely to have worse kidney prognosis. Other genes variants analysed were not associated with SCN or other SCD complications. Our data indicate that APOL1 screening should be considered for the management of SCD patients, including those of non-African-American origin, as those with homozygous or double heterozygous variants are clearly at higher risk of SCN.
[Mh] Termos MeSH primário: Albuminúria
Anemia Falciforme
Apolipoproteínas/genética
Variação Genética
Heterozigoto
Homozigoto
Rim/fisiopatologia
Lipoproteínas HDL/genética
[Mh] Termos MeSH secundário: Adulto
Afroamericanos
Albuminúria/genética
Albuminúria/fisiopatologia
Anemia Falciforme/genética
Anemia Falciforme/fisiopatologia
Apolipoproteína L1
Feminino
Taxa de Filtração Glomerular
Glutationa S-Transferase pi/genética
Glutationa Transferase/genética
Heme Oxigenase-1/genética
Seres Humanos
Masculino
[Pt] Tipo de publicação:CLINICAL TRIAL; JOURNAL ARTICLE; MULTICENTER STUDY
[Nm] Nome de substância:
0 (APOL1 protein, human); 0 (Apolipoprotein L1); 0 (Apolipoproteins); 0 (Lipoproteins, HDL); EC 1.14.14.18 (HMOX1 protein, human); EC 1.14.14.18 (Heme Oxygenase-1); EC 2.5.1.- (glutathione S-transferase T1); EC 2.5.1.18 (GSTP1 protein, human); EC 2.5.1.18 (Glutathione S-Transferase pi); EC 2.5.1.18 (Glutathione Transferase); EC 2.5.1.18 (glutathione S-transferase M1)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE
[do] DOI:10.1111/bjh.14842


  7 / 2258 MEDLINE  
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[PMID]:28692125
[Au] Autor:Dos Santos EVW; Alves LNR; Louro ID
[Ad] Endereço:Núcleo de Genética Humana e Molecular Departamento de Ciências Biológicas, Centro de Ciências Humanas e Naturais, , , Brasil eldamariavw@yahoo.com.br.
[Ti] Título:Steroid metabolism gene polymorphisms and their implications on breast and ovarian cancer prognosis.
[So] Source:Genet Mol Res;16(3), 2017 Jul 06.
[Is] ISSN:1676-5680
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:A role for estrogen in the etiology of breast and ovarian cancers has been suggested; therefore, genetic polymorphisms in steroid metabolism genes could be involved in the carcinogenesis of these tumors. We have aimed to investigate the role of GSTP1 and CYP17 polymorphisms and their correlation with MSI (microsatellite instability) and LOH (loss of heterozygosity) in AR, ERß and CYP19 genes in women from Espírito Santo State, Brazil. The study population consisted of 107 female breast and 24 ovarian tumors. GSTP1 and CYP17 polymorphisms were detected by polymerase chain reaction (PCR) amplification followed by restriction fragment length polymorphism (RFLP) analysis while MSI and LOH were analyzed by PCR. GSTP1 and CYP17 polymorphisms alone were not associated with an increased risk for breast or ovarian tumors. However, when combined with MSI/LOH in AR, ERß and CYP19 genes, we were able to detect significant associations with the GSTP1 wild-type genotype in PR (progesterone receptor) negative breast cancers or the CYP17 wild-type genotype in ER (estrogen receptor) and PR-negative breast tumors. No associations with ovarian tumors were detected. Our results suggest that wild-type GSTP1 or CYP17 genes when combined with LOH/MSI in steroid metabolism genes may play a role in ER and/or PR negative breast cancers. These data support the hypothesis that genes related to steroid metabolism are important in the characterization of breast cancer and that the analysis of single polymorphisms may not be sufficient.
[Mh] Termos MeSH primário: Neoplasias da Mama/genética
Glutationa S-Transferase pi/genética
Neoplasias Ovarianas/genética
Polimorfismo Genético
Esteroide 17-alfa-Hidroxilase/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Idoso de 80 Anos ou mais
Neoplasias da Mama/patologia
Feminino
Seres Humanos
Perda de Heterozigosidade
Repetições de Microssatélites
Meia-Idade
Neoplasias Ovarianas/patologia
Esteroides/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Steroids); EC 1.14.14.19 (Steroid 17-alpha-Hydroxylase); EC 2.5.1.18 (GSTP1 protein, human); EC 2.5.1.18 (Glutathione S-Transferase pi)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170711
[St] Status:MEDLINE
[do] DOI:10.4238/gmr16039691


  8 / 2258 MEDLINE  
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[PMID]:28622826
[Au] Autor:Saad-Hussein A; Noshy M; Taha M; El-Shorbagy H; Shahy E; Abdel-Shafy EA
[Ad] Endereço:National Research Centre, Egypt. Electronic address: amel_h@hotmail.com.
[Ti] Título:GSTP1 and XRCC1 polymorphisms and DNA damage in agricultural workers exposed to pesticides.
[So] Source:Mutat Res;819:20-25, 2017 Jul.
[Is] ISSN:1873-135X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Pesticide exposure may be associated with increased risk of genotoxicity and carcinogenesis. These risks may be affected by polymorphisms of genes for glutathione transferase-dependent metabolism of pesticides and for DNA repair. We studied the prevalence of GSTP1 and XRCC1 polymorphisms and their possible correlation with DNA damage following prolonged pesticide exposure. DNA damage was estimated by the comet assay in peripheral blood samples from 51 pesticide-exposed workers and 50 controls. GSTP1 (105) and XRCC1 (399 and 194) genotypes were identified by restriction fragment length analysis. Individuals carrying theGSTP1 Ile-Ile or XRCC1399 Arg-Arg genotypes showed greater DNA damage than observed for other alleles.
[Mh] Termos MeSH primário: Dano ao DNA
Proteínas de Ligação a DNA/genética
Fazendeiros
Glutationa S-Transferase pi/genética
Exposição Ocupacional/efeitos adversos
Praguicidas/toxicidade
Polimorfismo de Fragmento de Restrição
[Mh] Termos MeSH secundário: Substituição de Aminoácidos/genética
Ensaio Cometa
Dano ao DNA/genética
Genótipo
Seres Humanos
Masculino
Meia-Idade
Proteína 1 Complementadora Cruzada de Reparo de Raio-X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Pesticides); 0 (X-ray Repair Cross Complementing Protein 1); 0 (XRCC1 protein, human); EC 2.5.1.18 (GSTP1 protein, human); EC 2.5.1.18 (Glutathione S-Transferase pi)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170618
[St] Status:MEDLINE


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[PMID]:28622459
[Au] Autor:Pégeot H; Mathiot S; Perrot T; Gense F; Hecker A; Didierjean C; Rouhier N
[Ad] Endereço:UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, Université de Lorraine/INRA, Vandoeuvre-lès-Nancy, France.
[Ti] Título:Structural plasticity among glutathione transferase Phi members: natural combination of catalytic residues confers dual biochemical activities.
[So] Source:FEBS J;284(15):2442-2463, 2017 Aug.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The glutathione transferase (GST) gene family is divided into 14 classes in photosynthetic organisms. Among them, the Phi class (GSTF) is composed of a large number of genes that are often induced in response to environmental constraints due to their ability to detoxify xenobiotics, to their peroxidase activity and to their involvement in the biosynthesis and/or transport of secondary metabolites. However, the exact functions of GSTFs from many plants including Populus trichocarpa are unknown. Here, following GSTF1 characterization, we have performed a comparative analysis of the seven other GSTFs found in poplar by systematically evaluating the biochemical and enzymatic properties of the corresponding recombinant proteins and of variants mutated for active site residues and by determining the three-dimensional structures of several representatives. Owing to the presence of a cysteine with a pK value around 5 in their active site, GSTF3, F7, and F8 displayed a thiol transferase activity in addition to the usual glutathione transferase and peroxidase activities. From structural analyses, it appeared that these dual biochemical properties originate from the existence of a certain variability in the ß1-α1 loop. This allows positioning of several active site residues at proximity of the glutathione molecule, which itself remains unchanged in GSTF three-dimensional structures. These results highlight the promiscuity of some GSTFs and that changes of active site residues in some isoforms during evolution generated functional diversity by modifying their activity profile. DATABASE: Structural data are available in the PDB under the accession numbers 5EY6, 5F05, 5F06, and 5F07.
[Mh] Termos MeSH primário: Glutationa S-Transferase pi/metabolismo
Modelos Moleculares
Proteínas de Plantas/metabolismo
Populus/enzimologia
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Sequência de Aminoácidos
Substituição de Aminoácidos
Biocatálise
Domínio Catalítico
Cisteína/química
Dimerização
Estabilidade Enzimática
Glutationa/química
Glutationa/metabolismo
Glutationa S-Transferase pi/química
Glutationa S-Transferase pi/genética
Isoenzimas/química
Isoenzimas/genética
Isoenzimas/metabolismo
Mutagênese Sítio-Dirigida
Mutação
Filogenia
Proteínas de Plantas/química
Proteínas de Plantas/genética
Conformação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Isoenzymes); 0 (Plant Proteins); 0 (Recombinant Proteins); EC 2.5.1.18 (Glutathione S-Transferase pi); GAN16C9B8O (Glutathione); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170617
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14138


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[PMID]:28562019
[Au] Autor:Yip VLM; Meng X; Maggs JL; Jenkins RE; Marlot PT; Marson AG; Park BK; Pirmohamed M
[Ad] Endereço:MRC Centre for Drug Safety Science, Department of Molecular and Clinical Pharmacology, The University of Liverpool , Liverpool L69 3GE, United Kingdom.
[Ti] Título:Mass Spectrometric Characterization of Circulating Covalent Protein Adducts Derived from Epoxide Metabolites of Carbamazepine in Patients.
[So] Source:Chem Res Toxicol;30(7):1419-1435, 2017 Jul 17.
[Is] ISSN:1520-5010
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Carbamazepine (CBZ) is an effective antiepileptic drug that has been associated with hypersensitivity reactions. The pathogenesis of those reactions is incompletely understood but is postulated to involve a complex interplay between the drug's metabolism, genetic variation in human leukocyte antigens, and adverse activation of the immune system. Multiple T-cell activation mechanisms have been hypothesized including activation by drug-peptide conjugates derived from proteins haptenated by reactive metabolites. However, definitive evidence of the drug-protein adducts in patients has been lacking. In this study, mass spectrometry was used to characterize protein modifications by microsomally-generated metabolites of CBZ and in patients taking CBZ therapy. CBZ 10,11-epoxide (CBZE), a major electrophilic plasma metabolite of CBZ, formed adducts with glutathione-S-transferase pi (GSTP; Cys47) and human serum albumin (HSA; His146 and His338, but not Cys34) in vitro via notably divergent side-chain selectivity. Both proteins were adducted at the same residues by undefined monoxygenated metabolites ([O]CBZ) when they were incubated with human liver microsomes, NADPH and CBZ. There was also evidence for formation of a CBZ adduct at His146 and His338 of HSA derived via dehydration from an intermediate arene oxide adduct. Glutathione trapping of reactive metabolites confirmed microsomal production of CBZE and indicated simultaneous production of arene oxides. In 15 patients prescribed CBZ therapy, [O]CBZ-modified HSA (His146) was detected in all subjects. The relative amount of adduct was moderately positively correlated with plasma concentrations of CBZ (r = 0.44, p = 0.002) and CBZE (r = 0.35, p = 0.006). Our results have provided the first chemical evidence for microsomal production of [O]CBZ species that are able to escape the microsomal domain to react covalently with soluble proteins. This study has also demonstrated the presence of circulating [O]CBZ-modified HSA in patients without hypersensitivity reactions who were receiving standard CBZ therapy. The implications of those circulating adducts for susceptibility to CBZ hypersensitivity merit further immunological investigation in hypersensitive patients.
[Mh] Termos MeSH primário: Carbamazepina/sangue
Compostos de Epóxi/sangue
Glutationa S-Transferase pi/sangue
Albumina Sérica/análise
[Mh] Termos MeSH secundário: Carbamazepina/química
Carbamazepina/metabolismo
Compostos de Epóxi/metabolismo
Glutationa S-Transferase pi/metabolismo
Seres Humanos
Espectrometria de Massas
Estrutura Molecular
Albumina Sérica/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Epoxy Compounds); 0 (Serum Albumin); 33CM23913M (Carbamazepine); EC 2.5.1.18 (Glutathione S-Transferase pi)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170601
[St] Status:MEDLINE
[do] DOI:10.1021/acs.chemrestox.7b00063



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