Base de dados : MEDLINE
Pesquisa : D08.811.074.750 [Categoria DeCS]
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  1 / 1951 MEDLINE  
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[PMID]:29064327
[Au] Autor:Chen T; Liu C; Lu H; Yin M; Shao C; Hu X; Wu J; Wang Y
[Ad] Endereço:1 Department of Oncology, Changhai Hospital, The Second Military Medical University, Shanghai, China.
[Ti] Título:The expression of APE1 in triple-negative breast cancer and its effect on drug sensitivity of olaparib.
[So] Source:Tumour Biol;39(10):1010428317713390, 2017 Oct.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Triple-negative breast cancer is a kind of breast cancer with poor prognosis and special biological behavior, which lacked endocrine therapy and targeted therapy. We investigate the effect of human APE1 (apurinic/apyrimidyl endonuclease 1), a rate-limiting enzyme of base excision repair, on the prognosis in triple-negative breast cancer and drug sensitivity of olaparib. The expression of APE1 was detected by immunohistochemistry in the triple-negative breast cancer tissues and its effect on survival of triple-negative breast cancer patients was followed. To find whether APE1 effect the drug sensitivity in triple-negative breast cancer cells, the APE1-knockout HCC1937 cell line (triple-negative breast cancer cell line) was established by CRISPR/Cas9 system. Then, we use the wild-type and knockout one to test the drug sensitivity of olaparib. The expression of APE1 in triple-negative breast cancer tissues was significantly higher than that in the adjacent tissues (85.6% vs 14.4%) and its expression was related to tumor size (p < 0.05). We also found that it is an independent prognostic factor in patients with triple-negative breast cancer (overall survival, p = 0.01). In vitro assay, the half maximal inhibitory concentration of olaparib in HCC1937-APE1-KO was significantly increased (17.22 vs 91.85 µM) compared to the wild type. The growth curve showed that olaparib had a stronger lethality on HCC1937 compared to HCC1937- APE1-KO (p < 0.05 on day 3). HCC1937 resulted in more mitotic G2/M arrest and increased apoptosis rate after treatment with 40 µM of olaparib, while HCC1937-APE1-KO did not change significantly. When HCC1937 was treated with different concentrations of olaparib, it was found that APE1 expression decreased more significantly at 15 µM of olaparib was. In HCC1937-APE1-KO, the expression of endogenous poly (ADP-ribose) polymerase 1 was also less than that of HCC1937. These results suggested that the expression of APE1 was an important basis for the maintenance of poly (ADP-ribose) polymerase 1, and the deletion of APE1 may be related to the resistance of olaparib.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
DNA Liase (Sítios Apurínicos ou Apirimidínicos)/metabolismo
Resistência a Medicamentos Antineoplásicos/fisiologia
Ftalazinas/farmacologia
Piperazinas/farmacologia
Neoplasias de Mama Triplo Negativas/metabolismo
[Mh] Termos MeSH secundário: Adulto
Idoso
Apoptose/efeitos dos fármacos
Apoptose/fisiologia
Linhagem Celular Tumoral
Feminino
Citometria de Fluxo
Técnicas de Inativação de Genes
Seres Humanos
Imuno-Histoquímica
Concentração Inibidora 50
Estimativa de Kaplan-Meier
Meia-Idade
Inibidores de Poli(ADP-Ribose) Polimerases/farmacologia
Poli(ADP-Ribose) Polimerases/metabolismo
Prognóstico
Modelos de Riscos Proporcionais
Análise Serial de Tecidos
Neoplasias de Mama Triplo Negativas/tratamento farmacológico
Neoplasias de Mama Triplo Negativas/mortalidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Phthalazines); 0 (Piperazines); 0 (Poly(ADP-ribose) Polymerase Inhibitors); EC 2.4.2.30 (Poly(ADP-ribose) Polymerases); EC 4.2.99.18 (APEX1 protein, human); EC 4.2.99.18 (DNA-(Apurinic or Apyrimidinic Site) Lyase); WOH1JD9AR8 (olaparib)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171025
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317713390


  2 / 1951 MEDLINE  
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[PMID]:28926604
[Au] Autor:Wei S; Perera MLW; Sakhtemani R; Bhagwat AS
[Ad] Endereço:Department of Chemistry, Wayne State University, Detroit, Michigan, United States of America.
[Ti] Título:A novel class of chemicals that react with abasic sites in DNA and specifically kill B cell cancers.
[So] Source:PLoS One;12(9):e0185010, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Most B cell cancers overexpress the enzyme activation-induced deaminase at high levels and this enzyme converts cytosines in DNA to uracil. The constitutive expression of this enzyme in these cells greatly increases the uracil content of their genomes. We show here that these genomes also contain high levels of abasic sites presumably created during the repair of uracils through base-excision repair. We further show that three alkoxyamines with an alkyne functional group covalently link to abasic sites in DNA and kill immortalized cell lines created from B cell lymphomas, but not other cancers. They also do not kill normal B cells. Treatment of cancer cells with one of these chemicals causes strand breaks, and the sensitivity of the cells to this chemical depends on the ability of the cells to go through the S phase. However, other alkoxyamines that also link to abasic sites- but lack the alkyne functionality- do not kill cells from B cell lymphomas. This shows that the ability of alkoxyamines to covalently link to abasic sites is insufficient for their cytotoxicity and that the alkyne functionality may play a role in it. These chemicals violate the commonly accepted bioorthogonality of alkynes and are attractive prototypes for anti-B cell cancer agents.
[Mh] Termos MeSH primário: Aminas/farmacologia
Linfócitos B/efeitos dos fármacos
DNA/metabolismo
[Mh] Termos MeSH secundário: Aminas/química
Antineoplásicos/farmacologia
Linfócitos B/citologia
Linfócitos B/metabolismo
Pontos de Checagem do Ciclo Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Células Cultivadas
DNA/química
Quebras de DNA de Cadeia Dupla/efeitos dos fármacos
Reparo do DNA/efeitos dos fármacos
DNA Liase (Sítios Apurínicos ou Apirimidínicos)/antagonistas & inibidores
DNA Liase (Sítios Apurínicos ou Apirimidínicos)/metabolismo
Células HEK293
Células HeLa
Seres Humanos
Linfoma de Células B/metabolismo
Linfoma de Células B/patologia
Células MCF-7
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amines); 0 (Antineoplastic Agents); 9007-49-2 (DNA); EC 4.2.99.18 (APEX1 protein, human); EC 4.2.99.18 (DNA-(Apurinic or Apyrimidinic Site) Lyase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170920
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185010


  3 / 1951 MEDLINE  
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[PMID]:28844667
[Au] Autor:Mahmoudian E; Khalilnezhad A; Gharagozli K; Amani D
[Ad] Endereço:Department of Immunology, School of Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
[Ti] Título:Thioredoxin-1, redox factor-1 and thioredoxin-interacting protein, mRNAs are differentially expressed in Multiple Sclerosis patients exposed and non-exposed to interferon and immunosuppressive treatments.
[So] Source:Gene;634:29-36, 2017 Nov 15.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Oxidative stress is closely linked to inflammation in neurodegenerative diseases. We aimed to investigate the expression of redox system genes in Multiple Sclerosis (MS) patients either exposed or not exposed to conventional treatments. METHODS: Forty-four MS patients were divided into three groups: newly diagnosed (Group 1), receiving interferon (Group 2) and receiving immunosuppressive drugs (Group 3). Also, 15 healthy controls were enrolled. The mRNA expression of TRX1, TXNRD1, TRX2, TXNRD2, TXNIP, and APEX1 genes in peripheral blood mononuclear cells (PBMCs) was assessed by relative quantitative real-time PCR. Also, serum level of Trx1 was measured by ELISA. RESULTS: Serum level of Trx1 in the newly diagnosed MS patients was significantly higher compared to the healthy controls (P=0.013). Likewise, TRX1 and APEX1 expressions were significantly higher in the newly diagnosed patients compared to controls (P=0.003 and P=0.042), patients under interferon treatment (P=0.003 and P=0.013), and patients received immunosuppressants (P=0.001 and P=0.025). Furthermore, TXNIP expression in MS patients (either group 1, group 2, or group 3) was significantly lower than that in the control group (P=0.017, P=0.002, and P=0.022 respectively). The expression of TXNRD1, TRX2, and TXNRD2 did not show any significant difference between the control and the MS patient (P>0.05). CONCLUSIONS: Our data showed that redox system elements are differentially expressed in newly diagnosed MS patients, or patients receiving either interferon or immunosuppressive treatments. However, much more studies are required to confirm our findings and clarify the underlying mechanisms.
[Mh] Termos MeSH primário: Proteínas de Transporte/genética
DNA Liase (Sítios Apurínicos ou Apirimidínicos)/genética
Esclerose Múltipla/genética
Tiorredoxinas/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Feminino
Regulação da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Imunossupressores/farmacologia
Imunossupressores/uso terapêutico
Interferons/farmacologia
Interferons/uso terapêutico
Masculino
Meia-Idade
Esclerose Múltipla/tratamento farmacológico
Esclerose Múltipla/metabolismo
Tiorredoxinas/sangue
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Immunosuppressive Agents); 0 (TXN protein, human); 0 (TXNIP protein, human); 52500-60-4 (Thioredoxins); 9008-11-1 (Interferons); EC 4.2.99.18 (APEX1 protein, human); EC 4.2.99.18 (DNA-(Apurinic or Apyrimidinic Site) Lyase)
[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:170829
[St] Status:MEDLINE


  4 / 1951 MEDLINE  
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[PMID]:28766835
[Au] Autor:Fan X; Wen L; Li Y; Lou L; Liu W; Zhang J
[Ad] Endereço:Department of Gynecologic Oncology, The Fourth Hospital of Hebei Medical University, Shijiazhuang, China.
[Ti] Título:The expression profile and prognostic value of APE/Ref-1 and NPM1 in high-grade serous ovarian adenocarcinoma.
[So] Source:APMIS;125(10):857-862, 2017 Oct.
[Is] ISSN:1600-0463
[Cp] País de publicação:Denmark
[La] Idioma:eng
[Ab] Resumo:To analyze the expression trends and clinical significance of Apurinic/Apyrimidinic Endodeoxyribonuclease 1 (APE1/Ref-1) and Nucleophosmin (NPM1) proteins in high-grade serous ovarian adenocarcinoma (HGSC). The expressions of APE1/Ref-1 and NPM1 proteins in 94 patients with HGSC were determined using the immunohistochemical (IHC) method, and their relationships with clinicopathological features were analyzed by the χ test or Fisher's exact test. The follow-up data, Cox proportional hazards univariate and multivariate survival analyses were integrated to evaluate the prognostic factors affecting patients with HGSC. In the normal fallopian tubes, APE1/Ref-1 and NPM1 protein were mainly distributed in the nuclear. The HGSC experienced changes in the cellular localization of APE1/Ref-1 and NPM1 protein expressions, which were abnormally expressed in the cytoplasm. The rates of abnormal cytoplasmic expression of APE1/Ref-1 and NPM1 proteins in 94 patients with HGSC were 69.1% and 73.4%, respectively, which were significantly higher than the normal fallopian tube tissues (p < 0.05). The abnormal cytoplasmic APE1/Ref-1 and NPM1 are significantly correlated with the lymph node metastasis, chemosensitivity, FIGO staging, and prognosis. The COX multivariate survival analysis showed that the abnormal expression of APE1/Ref-1 protein, FIGO staging, and lymph node metastasis are independent prognostic factors. Collectively, the abnormal cytoplasmic APE1/Ref-1 and NPM1 proteins are associated with the oncogenic progression and chemoresistance of HGSC, and predict a poor prognosis.
[Mh] Termos MeSH primário: Adenocarcinoma/diagnóstico
Adenocarcinoma/patologia
DNA Liase (Sítios Apurínicos ou Apirimidínicos)/análise
Proteínas Nucleares/análise
Neoplasias Ovarianas/diagnóstico
Neoplasias Ovarianas/patologia
[Mh] Termos MeSH secundário: Adulto
Idoso
DNA Liase (Sítios Apurínicos ou Apirimidínicos)/genética
Feminino
Perfilação da Expressão Gênica
Seres Humanos
Imuno-Histoquímica
Meia-Idade
Proteínas Nucleares/genética
Prognóstico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nuclear Proteins); 117896-08-9 (nucleophosmin); EC 4.2.99.18 (APEX1 protein, human); EC 4.2.99.18 (DNA-(Apurinic or Apyrimidinic Site) Lyase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE
[do] DOI:10.1111/apm.12733


  5 / 1951 MEDLINE  
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[PMID]:28647366
[Au] Autor:Yan Z; Yuan Z; Ni J; Gu L; Shen Y
[Ad] Endereço:State Key Laboratory of Microbial Technology, Shandong University, 27 Shanda Nan Rd., Jinan, 250100, PR China.
[Ti] Título:Crystal structure of the crenarchaeal ExoIII AP endonuclease SisExoIII reveals a conserved disulfide bond endowing the protein with thermostability.
[So] Source:Biochem Biophys Res Commun;490(3):774-779, 2017 Aug 26.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:AP endonuclease recognizes and cleaves apurinic/apyrimidinic (AP) sites and plays a critical role in base excision repair. Many ExoIII and EndoIV family AP endonucleases have been characterized both biochemically and structurally in Eukaryote and Bacteria. However, relatively fewer have been studied in Euryarchaeota and there is no such report on an AP endonuclease from Crenarchaeota. Here we report, for the first time, the crystal structure of a crenarchaeal ExoIII AP endonuclease, SisExoIII, from Sulfolobus islandicus REY15A. SisExoIII comprises a two-layer core formed by 10 ß-sheets and a shell formed by 9 surrounding α-helices. A disulfide bond connecting ß8 and ß9 is formed by Cys142 and Cys215. This intra-molecular linkage is conserved among crenarchaeal ExoIII homologs and site-directed mutagenesis revealed that it endows the protein with thermostability, however, disruption of the disulfide bond only has a slight effect on the AP endonuclease activity. We also observed that several key residues within the catalytic center including conserved Glu35 and Asn9 show different conformation compared with known ExoIII proteins and form various intra-molecular salt bridges. The protein possesses three putative DNA binding loops with higher flexibility and hydrophobicity than those of ExoIIIs from other organisms. These features may result in low AP endonuclease activity and defect of exonuclease activity of SisExoIII. The study has deepened our understanding in the structural basis of crenarchaeal ExoIII catalysis and clarified a role of the disulfide bond in maintaining protein thermostability.
[Mh] Termos MeSH primário: DNA Liase (Sítios Apurínicos ou Apirimidínicos)/química
Exodesoxirribonucleases/química
Sulfolobus/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Cristalografia por Raios X
Estabilidade Enzimática
Modelos Moleculares
Conformação Proteica
Alinhamento de Sequência
Sulfolobus/química
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.1.- (Exodeoxyribonucleases); EC 3.1.11.2 (exodeoxyribonuclease III); EC 4.2.99.18 (DNA-(Apurinic or Apyrimidinic Site) Lyase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170626
[St] Status:MEDLINE


  6 / 1951 MEDLINE  
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[PMID]:28628658
[Au] Autor:Bethea CL; Mueller K; Reddy AP; Kohama SG; Urbanski HF
[Ad] Endereço:Division of Reproductive and Developmental Science, Oregon National Primate Research Center, Beaverton, OR, United States of America.
[Ti] Título:Effects of obesogenic diet and estradiol on dorsal raphe gene expression in old female macaques.
[So] Source:PLoS One;12(6):e0178788, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The beneficial effects of bioidentical ovarian steroid hormone therapy (HT) during the perimenopause are gaining recognition. However, the positive effects of estrogen (E) plus or minus progesterone (P) administration to ovariectomized (Ovx) lab animals were recognized in multiple systems for years before clinical trials could adequately duplicate the results. Moreover, very large numbers of women are often needed to find statistically significant results in clinical trials of HT; and there are still opposing results being published, especially in neural and cardiovascular systems. One of the obvious differences between human and animal studies is diet. Laboratory animals are fed a diet that is low in fat and refined sugar, but high in micronutrients. In the US, a large portion of the population eats what is known as a "western style diet" or WSD that provides calories from 36% fat, 44% carbohydrates (includes 18.5% sugars) and 18% protein. Unfortunately, obesity and diabetes have reached epidemic proportions and the percentage of obese women in clinical trials may be overlooked. We questioned whether WSD and obesity could decrease the positive neural effects of estradiol (E) in the serotonin system of old macaques that were surgically menopausal. Old ovo-hysterectomized female monkeys were fed WSD for 2.5 years, and treated with placebo, Immediate E (ImE) or Delayed E (DE). Compared to old Ovx macaques on primate chow and treated with placebo or E, the WSD-fed monkeys exhibited greater individual variance and blunted responses to E-treatment in the expression of genes related to serotonin neurotransmission, CRH components in the midbrain, synapse assembly, DNA repair, protein folding, ubiquitylation, transport and neurodegeneration. For many of the genes examined, transcript abundance was lower in WSD-fed than chow-fed monkeys. In summary, an obesogenic diet for 2.5 years in old surgically menopausal macaques blunted or increased variability in E-induced gene expression in the dorsal raphe. These results suggest that with regard to function and viability in the dorsal raphe, HT may not be as beneficial for obese women as normal weight women.
[Mh] Termos MeSH primário: Dieta Ocidental
Núcleo Dorsal da Rafe/efeitos dos fármacos
Estradiol/farmacologia
Macaca mulatta/metabolismo
[Mh] Termos MeSH secundário: Animais
Moléculas de Adesão Celular Neuronais/genética
Moléculas de Adesão Celular Neuronais/metabolismo
DNA Liase (Sítios Apurínicos ou Apirimidínicos)/genética
DNA Liase (Sítios Apurínicos ou Apirimidínicos)/metabolismo
Núcleo Dorsal da Rafe/metabolismo
Feminino
Histerectomia
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Mesencéfalo/metabolismo
Chaperonas Moleculares/genética
Chaperonas Moleculares/metabolismo
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
Ovariectomia
Receptores de Hormônio Liberador da Corticotropina/genética
Receptores de Hormônio Liberador da Corticotropina/metabolismo
Serotonina/genética
Serotonina/metabolismo
Sinapses/metabolismo
Ubiquitina/genética
Ubiquitina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Adhesion Molecules, Neuronal); 0 (Membrane Proteins); 0 (Molecular Chaperones); 0 (Nerve Tissue Proteins); 0 (Receptors, Corticotropin-Releasing Hormone); 0 (Ubiquitin); 0 (neuroligin 3); 333DO1RDJY (Serotonin); 4TI98Z838E (Estradiol); EC 4.2.99.18 (DNA-(Apurinic or Apyrimidinic Site) Lyase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170620
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0178788


  7 / 1951 MEDLINE  
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[PMID]:28575236
[Au] Autor:Bj Rås KØ; Sousa MML; Sharma A; Fonseca DM; S Gaard CK; Bj Rås M; Otterlei M
[Ad] Endereço:Department of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology (NTNU), N-7491 Trondheim, Norway.
[Ti] Título:Monitoring of the spatial and temporal dynamics of BER/SSBR pathway proteins, including MYH, UNG2, MPG, NTH1 and NEIL1-3, during DNA replication.
[So] Source:Nucleic Acids Res;45(14):8291-8301, 2017 Aug 21.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Base lesions in DNA can stall the replication machinery or induce mutations if bypassed. Consequently, lesions must be repaired before replication or in a post-replicative process to maintain genomic stability. Base excision repair (BER) is the main pathway for repair of base lesions and is known to be associated with DNA replication, but how BER is organized during replication is unclear. Here we coupled the iPOND (isolation of proteins on nascent DNA) technique with targeted mass-spectrometry analysis, which enabled us to detect all proteins required for BER on nascent DNA and to monitor their spatiotemporal orchestration at replication forks. We demonstrate that XRCC1 and other BER/single-strand break repair (SSBR) proteins are enriched in replisomes in unstressed cells, supporting a cellular capacity of post-replicative BER/SSBR. Importantly, we identify for the first time the DNA glycosylases MYH, UNG2, MPG, NTH1, NEIL1, 2 and 3 on nascent DNA. Our findings suggest that a broad spectrum of DNA base lesions are recognized and repaired by BER in a post-replicative process.
[Mh] Termos MeSH primário: Quebras de DNA de Cadeia Simples
Enzimas Reparadoras do DNA/metabolismo
Reparo do DNA
Replicação do DNA
DNA/genética
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
DNA/metabolismo
DNA Glicosilases/metabolismo
DNA Liase (Sítios Apurínicos ou Apirimidínicos)/metabolismo
Proteínas de Ligação a DNA/metabolismo
Desoxirribonuclease (Dímero de Pirimidina)/metabolismo
Células HEK293
Células HeLa
Seres Humanos
Immunoblotting
Espectrometria de Massas/métodos
N-Glicosil Hidrolases/metabolismo
Transdução de Sinais/genética
Fatores de Tempo
Proteína 1 Complementadora Cruzada de Reparo de Raio-X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (X-ray Repair Cross Complementing Protein 1); 0 (XRCC1 protein, human); 9007-49-2 (DNA); EC 3.1.25.1 (Deoxyribonuclease (Pyrimidine Dimer)); EC 3.1.25.1 (NTHL1 protein, human); EC 3.2.2.- (CCNO protein, human); EC 3.2.2.- (DNA Glycosylases); EC 3.2.2.- (FLJ10858 protein, human); EC 3.2.2.- (N-Glycosyl Hydrolases); EC 3.2.2.- (NEIL1 protein, human); EC 3.2.2.- (mutY adenine glycosylase); EC 3.2.2.21 (DNA-3-methyladenine glycosidase II); EC 4.2.99.18 (DNA-(Apurinic or Apyrimidinic Site) Lyase); EC 4.2.99.18 (NEIL2 protein, human); EC 6.5.1.- (DNA Repair Enzymes)
[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:170603
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx476


  8 / 1951 MEDLINE  
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[PMID]:28570836
[Au] Autor:Czarny P; Merecz-Sadowska A; Majchrzak K; Jablkowski M; Szemraj J; Sliwinski T; Karwowski B
[Ad] Endereço:1 Department of Medical Biochemistry, Medical University of Lodz , Lodz, Poland .
[Ti] Título:The Influence of Hepatitis C Virus Therapy on the DNA Base Excision Repair System of Peripheral Blood Mononuclear Cells.
[So] Source:DNA Cell Biol;36(7):535-540, 2017 Jul.
[Is] ISSN:1557-7430
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hepatitis C virus (HCV) can infect extrahepatic tissues, including lymphocytes, creating reservoir of the virus. Moreover, HCV proteins can interact with DNA damage response proteins of infected cells. In this article we investigated the influence of the virus infection and a new ombitasvir/paritaprevir/ritonavir ± dasabuvir ± ribavirin (OBV/PTV/r ± DSV ± RBV) anti-HCV therapy on the PBMCs (peripheral blood mononuclear cells, mainly lymphocytes) DNA base excision repair (BER) system. BER protein activity was analyzed in the nuclear and mitochondrial extracts (NE and ME) of PBMC isolated from patients before and after therapy, and from subjects without HCV, using modeled double-strand DNA, with 2'-deoxyuridine substitution as the DNA damage. The NE and ME obtained from patients before therapy demonstrated lower efficacy of 2'-deoxyuridine removal and DNA repair polymerization than those of the control group or patients after therapy. Moreover, the extracts from the patients after therapy had similar activity to those from the control group. However, the efficacy of apurinic/apyrimidinic site excision in NE did not differ between the studied groups. We postulate that infection of lymphocytes by the HCV can lead to a decrease in the activity of BER enzymes. However, the use of novel therapy results in the improvement of glycosylase activity as well as the regeneration of endonuclease and other crucial repair enzymes.
[Mh] Termos MeSH primário: Antivirais/farmacologia
Núcleo Celular/efeitos dos fármacos
Reparo do DNA
DNA/genética
Leucócitos Mononucleares/efeitos dos fármacos
Mitocôndrias/efeitos dos fármacos
[Mh] Termos MeSH secundário: Anilidas/farmacologia
Carbamatos/farmacologia
Núcleo Celular/metabolismo
Núcleo Celular/virologia
DNA/metabolismo
Quebras de DNA de Cadeia Dupla
DNA Glicosilases/genética
DNA Glicosilases/metabolismo
DNA Liase (Sítios Apurínicos ou Apirimidínicos)/genética
DNA Liase (Sítios Apurínicos ou Apirimidínicos)/metabolismo
Desoxiuridina/metabolismo
Quimioterapia Combinada
Endonucleases/genética
Endonucleases/metabolismo
Expressão Gênica
Hepacivirus/efeitos dos fármacos
Hepacivirus/crescimento & desenvolvimento
Hepatite C Crônica/tratamento farmacológico
Hepatite C Crônica/virologia
Interações Hospedeiro-Patógeno
Seres Humanos
Leucócitos Mononucleares/metabolismo
Leucócitos Mononucleares/virologia
Compostos Macrocíclicos/farmacologia
Mitocôndrias/metabolismo
Mitocôndrias/virologia
Mimetismo Molecular
Cultura Primária de Células
Ribavirina/farmacologia
Ritonavir/farmacologia
Sulfonamidas/farmacologia
Uracila/análogos & derivados
Uracila/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABT-267); 0 (ABT-333); 0 (ABT-450); 0 (Anilides); 0 (Antiviral Agents); 0 (Carbamates); 0 (Macrocyclic Compounds); 0 (Sulfonamides); 49717AWG6K (Ribavirin); 56HH86ZVCT (Uracil); 9007-49-2 (DNA); EC 3.1.- (Endonucleases); EC 3.2.2.- (DNA Glycosylases); EC 3.2.2.- (oxoguanine glycosylase 1, human); EC 4.2.99.18 (APEX1 protein, human); EC 4.2.99.18 (DNA-(Apurinic or Apyrimidinic Site) Lyase); O3J8G9O825 (Ritonavir); W78I7AY22C (Deoxyuridine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170602
[St] Status:MEDLINE
[do] DOI:10.1089/dna.2017.3653


  9 / 1951 MEDLINE  
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[PMID]:28549155
[Au] Autor:Prasai K; Robinson LC; Scott RS; Tatchell K; Harrison L
[Ad] Endereço:Department of Molecular and Cellular Physiology, Louisiana State University Health Sciences Center, Shreveport, LA 71130, USA.
[Ti] Título:Evidence for double-strand break mediated mitochondrial DNA replication in Saccharomyces cerevisiae.
[So] Source:Nucleic Acids Res;45(13):7760-7773, 2017 Jul 27.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The mechanism of mitochondrial DNA (mtDNA) replication in Saccharomyces cerevisiae is controversial. Evidence exists for double-strand break (DSB) mediated recombination-dependent replication at mitochondrial replication origin ori5 in hypersuppressive ρ- cells. However, it is not clear if this replication mode operates in ρ+ cells. To understand this, we targeted bacterial Ku (bKu), a DSB binding protein, to the mitochondria of ρ+ cells with the hypothesis that bKu would bind persistently to mtDNA DSBs, thereby preventing mtDNA replication or repair. Here, we show that mitochondrial-targeted bKu binds to ori5 and that inducible expression of bKu triggers petite formation preferentially in daughter cells. bKu expression also induces mtDNA depletion that eventually results in the formation of ρ0 cells. This data supports the idea that yeast mtDNA replication is initiated by a DSB and bKu inhibits mtDNA replication by binding to a DSB at ori5, preventing mtDNA segregation to daughter cells. Interestingly, we find that mitochondrial-targeted bKu does not decrease mtDNA content in human MCF7 cells. This finding is in agreement with the fact that human mtDNA replication, typically, is not initiated by a DSB. Therefore, this study provides evidence that DSB-mediated replication is the predominant form of mtDNA replication in ρ+ yeast cells.
[Mh] Termos MeSH primário: Quebras de DNA de Cadeia Dupla
Replicação do DNA
DNA Fúngico/metabolismo
DNA Mitocondrial/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Replicação do DNA/genética
DNA Fúngico/genética
DNA Mitocondrial/genética
DNA Liase (Sítios Apurínicos ou Apirimidínicos)/genética
DNA Liase (Sítios Apurínicos ou Apirimidínicos)/metabolismo
Proteínas de Ligação a DNA/genética
Proteínas de Ligação a DNA/metabolismo
Genes Fúngicos
Seres Humanos
Células MCF-7
Modelos Biológicos
Mutação
Mycobacterium marinum/genética
Mycobacterium marinum/metabolismo
Origem de Replicação
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (DNA, Fungal); 0 (DNA, Mitochondrial); 0 (DNA-Binding Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 4.2.99.18 (DNA-(Apurinic or Apyrimidinic Site) Lyase); EC 4.2.99.18 (NTG1 protein, S cerevisiae)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170527
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx443


  10 / 1951 MEDLINE  
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[PMID]:28404743
[Au] Autor:Hou X; Snarski P; Higashi Y; Yoshida T; Jurkevich A; Delafontaine P; Sukhanov S
[Ad] Endereço:Department of Medicine, School of Medicine, University of Missouri at Columbia, Columbia, Missouri, USA.
[Ti] Título:Nuclear complex of glyceraldehyde-3-phosphate dehydrogenase and DNA repair enzyme apurinic/apyrimidinic endonuclease I protect smooth muscle cells against oxidant-induced cell death.
[So] Source:FASEB J;31(7):3179-3192, 2017 Jul.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Atherosclerotic plaque destabilization is the major determinant of most acute coronary events. Smooth muscle cell (SMC) death contributes to plaque destabilization. Here, we describe a novel antiapoptotic mechanism in vascular SMCs that involves interaction of nuclear glyceraldehyde-3-phosphate dehydrogenase (GAPDH) with apurinic/apyrimidinic endonuclease 1 (Ape1), the major oxidized DNA repair enzyme. GAPDH down-regulation potentiated H O -induced DNA damage and SMC apoptosis. Conversely, GAPDH overexpression decreased DNA damage and protected SMCs against apoptosis. Ape1 down-regulation reversed the resistance of GAPDH-overexpressing cells to DNA damage and apoptosis, which indicated that Ape1 is indispensable for GAPDH-dependent protective effects. GAPDH bound Ape1 in the SMC nucleus, and blocking (or oxidation) of GAPDH active site cysteines suppressed GAPDH/Ape1 interaction and potentiated apoptosis. GAPDH up-regulated Ape1 a transcription factor homeobox protein Hox-A5-dependent mechanism. GAPDH levels were reduced in atherosclerotic plaque SMCs, and this effect correlated with oxidative stress and SMC apoptosis. Thus, we demonstrated that nuclear GAPDH/Ape1 interaction preserved Ape1 activity, reduced DNA damage, and prevented SMC apoptosis. Suppression of SMC apoptosis by maintenance of nuclear GAPDH/Ape1 interactions may be a novel therapy to increase atherosclerotic plaque stability.-Hou, X., Snarski, P., Higashi, Y., Yoshida, T., Jurkevich, A., Delafontaine, P., Sukhanov, S. Nuclear complex of glyceraldehyde-3-phosphate dehydrogenase and DNA repair enzyme apurinic/apyrimidinic endonuclease I protect smooth muscle cells against oxidant-induced cell death.
[Mh] Termos MeSH primário: Morte Celular/efeitos dos fármacos
DNA Liase (Sítios Apurínicos ou Apirimidínicos)/metabolismo
Gliceraldeído-3-Fosfato Desidrogenase (Fosforiladora)/metabolismo
Miócitos de Músculo Liso/efeitos dos fármacos
Miócitos de Músculo Liso/enzimologia
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular
Animais
Apolipoproteínas E/genética
Apolipoproteínas E/metabolismo
Núcleo Celular/enzimologia
DNA Liase (Sítios Apurínicos ou Apirimidínicos)/genética
Regulação Enzimológica da Expressão Gênica
Peróxido de Hidrogênio
Camundongos
Camundongos Knockout
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apolipoproteins E); BBX060AN9V (Hydrogen Peroxide); EC 1.2.1.12 (Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)); EC 4.2.99.18 (Apex1 protein, mouse); EC 4.2.99.18 (Apex1 protein, rat); EC 4.2.99.18 (DNA-(Apurinic or Apyrimidinic Site) Lyase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170414
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201601082R



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