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Pesquisa : D08.811.277.040.025.159.155 [Categoria DeCS]
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[PMID]:29277765
[Au] Autor:Yang G; Qiu J; Wang D; Tao Y; Song Y; Wang H; Tang J; Wang X; Sun YU; Yang Z; Hoffman RM
[Ad] Endereço:Hangzhou Third Hospital, Hangzhou, P.R. China.
[Ti] Título:Traditional Chinese Medicine Curcumin Sensitizes Human Colon Cancer to Radiation by Altering the Expression of DNA Repair-related Genes.
[So] Source:Anticancer Res;38(1):131-136, 2018 01.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: The aim of the present study was to investigate the radio-sensitizing efficacy of curcumin, a traditional Chinese medicine (TCM) on colon cancer cells in vitro and in vivo. MATERIALS AND METHODS: Human colon cancer HT-29 cells were treated with curcumin (2.5 µM), irradiation (10 Gy) and the combination of irradiation and curcumin. Cell proliferation was assessed using the MTT assay. Apoptotic cells were detected by Annexin V-PE/7-AAD analysis. PCR was performed to determine differential-expression profiling of 95 DNA-repair genes in irradiated cells and cells treated with both irradiation and curcumin. Differentially-expressed genes were confirmed by Western blotting. In vivo radio-sensitizing efficacy of curcumin was assessed in a xenograft mouse model of HT-29 colon cancer. Curcumin was administrated daily by intraperitoneal injection at 20 mg/kg/dose. Mice received irradiation (10 Gy) twice weekly. Apoptosis of the cancer cells following treatment was determined by TUNEL staining. RESULTS: Irradiation induced proliferation inhibition and apoptosis of HT-29 cells in vitro. Concurrent curcumin treatment sensitized the HT-29 tumor to irradiation (p<0.01). DNA repair-related genes CCNH and XRCC5 were upregulated and LIG4 and PNKP downregulated by the combination of curcumin and irradiation compared with irradiation alone (p<0.05). Combined treatment of curcumin and irradiation resulted in a significantly greater tumor-growth inhibition and apoptosis compared to irradiation treatment alone (p<0.01). CONCLUSION: Curcumin sensitizes human colon cancer in vitro and in vivo to radiation. Downregulation of LIG4 and PNKP and upregulation of XRCC5 and CCNH DNA-repair-related genes were involved in the radio-sensitizing efficacy of curcumin in colon cancer.
[Mh] Termos MeSH primário: Neoplasias do Colo/tratamento farmacológico
Neoplasias do Colo/radioterapia
Curcumina/farmacologia
Curcumina/uso terapêutico
Radiossensibilizantes/farmacologia
Radiossensibilizantes/uso terapêutico
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos dos fármacos
Apoptose/efeitos da radiação
Proliferação Celular/efeitos dos fármacos
Proliferação Celular/efeitos da radiação
Neoplasias do Colo/metabolismo
Neoplasias do Colo/patologia
Ciclina H/genética
Ciclina H/metabolismo
DNA Ligase Dependente de ATP/genética
DNA Ligase Dependente de ATP/metabolismo
Reparo do DNA/genética
Enzimas Reparadoras do DNA/genética
Enzimas Reparadoras do DNA/metabolismo
Feminino
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Regulação Neoplásica da Expressão Gênica/efeitos da radiação
Células HT29
Seres Humanos
Autoantígeno Ku/genética
Autoantígeno Ku/metabolismo
Medicina Tradicional Chinesa
Camundongos Endogâmicos BALB C
Camundongos Nus
Fosfotransferases (Aceptor do Grupo Álcool)/genética
Fosfotransferases (Aceptor do Grupo Álcool)/metabolismo
Carga Tumoral/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CCNH protein, human); 0 (Cyclin H); 0 (LIG4 protein, human); 0 (Radiation-Sensitizing Agents); EC 2.7.1.- (PNKP protein, human); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 3.6.4.12 (XRCC5 protein, human); EC 4.2.99.- (Ku Autoantigen); EC 6.5.1.- (DNA Repair Enzymes); EC 6.5.1.1 (DNA Ligase ATP); IT942ZTH98 (Curcumin)
[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


  2 / 1620 MEDLINE  
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[PMID]:28985363
[Au] Autor:Zhu S; Fisher LA; Bessho T; Peng A
[Ad] Endereço:Department of Oral Biology, College of Dentistry, University of Nebraska Medical Center, Lincoln, NE 68583, USA.
[Ti] Título:Protein phosphatase 1 and phosphatase 1 nuclear targeting subunit-dependent regulation of DNA-dependent protein kinase and non-homologous end joining.
[So] Source:Nucleic Acids Res;45(18):10583-10594, 2017 Oct 13.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:DNA-dependent protein kinase catalytic subunit (DNA-PKcs) plays a key role in mediating non-homologous end joining (NHEJ), a major repair pathway for DNA double-strand breaks (DSBs). The activation, function and dynamics of DNA-PKcs is regulated largely by its reversible phosphorylation at numerous residues, many of which are targeted by DNA-PKcs itself. Interestingly, these DNA-PKcs phosphorylation sites function in a distinct, and sometimes opposing manner, suggesting that they are differentially regulated via complex actions of both kinases and phosphatases. In this study we identified several phosphatase subunits as potential DSB-associated proteins. In particular, protein phosphatase 1 (PP1) is recruited to a DSB-mimicking substrate in Xenopus egg extracts and sites of laser microirradiation in human cells. Depletion of PP1 impairs NHEJ in both Xenopus egg extracts and human cells. PP1 binds multiple motifs of DNA-PKcs, regulates DNA-PKcs phosphorylation, and is required for DNA-PKcs activation after DNA damage. Interestingly, phosphatase 1 nuclear targeting subunit (PNUTS), an inhibitory regulator of PP1, is also recruited to DNA damage sites to promote NHEJ. PNUTS associates with the DNA-PK complex and is required for DNA-PKcs phosphorylation at Ser-2056 and Thr-2609. Thus, PNUTS and PP1 together fine-tune the dynamic phosphorylation of DNA-PKcs after DNA damage to mediate NHEJ.
[Mh] Termos MeSH primário: Quebras de DNA de Cadeia Dupla
Reparo do DNA por Junção de Extremidades
Proteína Quinase Ativada por DNA/metabolismo
Proteínas de Ligação a DNA/metabolismo
Proteínas Nucleares/metabolismo
Proteína Fosfatase 1/metabolismo
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Animais
Células HeLa
Seres Humanos
Autoantígeno Ku/metabolismo
Fosforilação
Xenopus
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Nuclear Proteins); 0 (PPP1R10 protein, human); 0 (RNA-Binding Proteins); EC 2.7.11.1 (DNA-Activated Protein Kinase); EC 3.1.3.16 (Protein Phosphatase 1); EC 4.2.99.- (Ku Autoantigen)
[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:171007
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx686


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[PMID]:28867292
[Au] Autor:Myler LR; Gallardo IF; Soniat MM; Deshpande RA; Gonzalez XB; Kim Y; Paull TT; Finkelstein IJ
[Ad] Endereço:Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA; Howard Hughes Medical Institute, The University of Texas at Austin, Austin, TX 78712, USA; Center for Systems and Synthetic Biology, The University of Texas at Austin, Austin, TX 78712, USA.
[Ti] Título:Single-Molecule Imaging Reveals How Mre11-Rad50-Nbs1 Initiates DNA Break Repair.
[So] Source:Mol Cell;67(5):891-898.e4, 2017 Sep 07.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:DNA double-strand break (DSB) repair is essential for maintaining our genomes. Mre11-Rad50-Nbs1 (MRN) and Ku70-Ku80 (Ku) direct distinct DSB repair pathways, but the interplay between these complexes at a DSB remains unclear. Here, we use high-throughput single-molecule microscopy to show that MRN searches for free DNA ends by one-dimensional facilitated diffusion, even on nucleosome-coated DNA. Rad50 binds homoduplex DNA and promotes facilitated diffusion, whereas Mre11 is required for DNA end recognition and nuclease activities. MRN gains access to occluded DNA ends by removing Ku or other DNA adducts via an Mre11-dependent nucleolytic reaction. Next, MRN loads exonuclease 1 (Exo1) onto the free DNA ends to initiate DNA resection. In the presence of replication protein A (RPA), MRN acts as a processivity factor for Exo1, retaining the exonuclease on DNA for long-range resection. Our results provide a mechanism for how MRN promotes homologous recombination on nucleosome-coated DNA.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/metabolismo
Quebras de DNA de Cadeia Dupla
Enzimas Reparadoras do DNA/metabolismo
Proteínas de Ligação a DNA/metabolismo
Proteínas Nucleares/metabolismo
Nucleossomos/enzimologia
Reparo de DNA por Recombinação
Imagem Individual de Molécula
[Mh] Termos MeSH secundário: Proteínas de Ciclo Celular/genética
Adutos de DNA/genética
Adutos de DNA/metabolismo
Enzimas Reparadoras do DNA/genética
Proteínas de Ligação a DNA/genética
Difusão
Exodesoxirribonucleases/genética
Exodesoxirribonucleases/metabolismo
Seres Humanos
Autoantígeno Ku/genética
Autoantígeno Ku/metabolismo
Proteína Homóloga a MRE11
Microscopia de Fluorescência
Proteínas Nucleares/genética
Nucleossomos/genética
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (DNA Adducts); 0 (DNA-Binding Proteins); 0 (MRE11A protein, human); 0 (NBN protein, human); 0 (Nuclear Proteins); 0 (Nucleosomes); 0 (Rad50 protein, human); EC 3.1.- (EXO1 protein, human); EC 3.1.- (Exodeoxyribonucleases); EC 3.1.- (MRE11 Homologue Protein); EC 3.6.4.12 (XRCC5 protein, human); EC 3.6.4.12 (Xrcc6 protein, human); EC 4.2.99.- (Ku Autoantigen); EC 6.5.1.- (DNA Repair Enzymes)
[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:170905
[St] Status:MEDLINE


  4 / 1620 MEDLINE  
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[PMID]:28855246
[Au] Autor:Hollingworth R; Horniblow RD; Forrest C; Stewart GS; Grand RJ
[Ad] Endereço:Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, United Kingdom.
[Ti] Título:Localization of Double-Strand Break Repair Proteins to Viral Replication Compartments following Lytic Reactivation of Kaposi's Sarcoma-Associated Herpesvirus.
[So] Source:J Virol;91(22), 2017 Nov 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Double-strand breaks (DSBs) in DNA are recognized by the Ku70/80 heterodimer and the MRE11-RAD50-NBS1 (MRN) complex and result in activation of the DNA-PK and ATM kinases, which play key roles in regulating the cellular DNA damage response (DDR). DNA tumor viruses such as Kaposi's sarcoma-associated herpesvirus (KSHV) are known to interact extensively with the DDR during the course of their replicative cycles. Here we show that during lytic amplification of KSHV DNA, the Ku70/80 heterodimer and the MRN complex consistently colocalize with viral genomes in replication compartments (RCs), whereas other DSB repair proteins form foci outside RCs. Depletion of MRE11 and abrogation of its exonuclease activity negatively impact viral replication, while in contrast, knockdown of Ku80 and inhibition of the DNA-PK enzyme, which are involved in nonhomologous end joining (NHEJ) repair, enhance amplification of viral DNA. Although the recruitment of DSB-sensing proteins to KSHV RCs is a consistent occurrence across multiple cell types, activation of the ATM-CHK2 pathway during viral replication is a cell line-specific event, indicating that recognition of viral DNA by the DDR does not necessarily result in activation of downstream signaling pathways. We have also observed that newly replicated viral DNA is not associated with cellular histones. Since the presence and modification of these DNA-packaging proteins provide a scaffold for docking of multiple DNA repair factors, the absence of histone deposition may allow the virus to evade localization of DSB repair proteins that would otherwise have a detrimental effect on viral replication. Tumor viruses are known to interact with machinery responsible for detection and repair of double-strand breaks (DSBs) in DNA, although detail concerning how Kaposi's sarcoma-associated herpesvirus (KSHV) modulates these cellular pathways during its lytic replication phase was previously lacking. By undertaking a comprehensive assessment of the localization of DSB repair proteins during KSHV replication, we have determined that a DNA damage response (DDR) is directed to viral genomes but is distinct from the response to cellular DNA damage. We also demonstrate that although recruitment of the MRE11-RAD50-NBS1 (MRN) DSB-sensing complex to viral genomes and activation of the ATM kinase can promote KSHV replication, proteins involved in nonhomologous end joining (NHEJ) repair restrict amplification of viral DNA. Overall, this study extends our understanding of the virus-host interactions that occur during lytic replication of KSHV and provides a deeper insight into how the DDR is manipulated during viral infection.
[Mh] Termos MeSH primário: Proteínas Mutadas de Ataxia Telangiectasia/metabolismo
Proteínas de Ciclo Celular/metabolismo
Quebras de DNA de Cadeia Dupla
Enzimas Reparadoras do DNA/metabolismo
DNA Viral/metabolismo
Proteínas de Ligação a DNA/metabolismo
Herpesvirus Humano 8/fisiologia
Proteínas Nucleares/metabolismo
Sarcoma de Kaposi/metabolismo
Ativação Viral/fisiologia
[Mh] Termos MeSH secundário: Proteínas Mutadas de Ataxia Telangiectasia/genética
Proteínas de Ciclo Celular/genética
Quinase do Ponto de Checagem 2/genética
Quinase do Ponto de Checagem 2/metabolismo
Enzimas Reparadoras do DNA/genética
DNA Viral/genética
Proteínas de Ligação a DNA/genética
Células HEK293
Seres Humanos
Autoantígeno Ku/genética
Autoantígeno Ku/metabolismo
Proteína Homóloga a MRE11
Proteínas Nucleares/genética
Sarcoma de Kaposi/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (DNA, Viral); 0 (DNA-Binding Proteins); 0 (MRE11A protein, human); 0 (NBN protein, human); 0 (Nuclear Proteins); 0 (Rad50 protein, human); EC 2.7.1.11 (Checkpoint Kinase 2); EC 2.7.11.1 (ATM protein, human); EC 2.7.11.1 (Ataxia Telangiectasia Mutated Proteins); EC 2.7.11.1 (CHEK2 protein, human); EC 3.1.- (MRE11 Homologue Protein); EC 4.2.99.- (Ku Autoantigen); EC 6.5.1.- (DNA Repair Enzymes)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170901
[St] Status:MEDLINE


  5 / 1620 MEDLINE  
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[PMID]:28821586
[Au] Autor:Wang J; Kang L; Song D; Liu L; Yang S; Ma L; Guo Z; Ding H; Wang H; Yang B
[Ad] Endereço:Henan Collaborative Innovation Center of Molecular Diagnosis and Laboratory Medicine, School of Laboratory Medicine, Xinxiang Medical University, Xinxiang 453003, China.
[Ti] Título:Ku70 Senses HTLV-1 DNA and Modulates HTLV-1 Replication.
[So] Source:J Immunol;199(7):2475-2482, 2017 Oct 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human T lymphotropic virus type 1 (HTLV-1) belongs to the deltaretrovirus family and has been linked to multiple diseases. However, the innate host defense against HTLV-1 is unclear. In this study, we report that the expression of Ku70, a known DNA sensor against DNA viruses, could be induced by HTLV-1 infection in HeLa, PMA-differentiated THP1 cells, primary human monocytes, and human monocyte-derived macrophages. In these cells, the overexpression of Ku70 inhibited the HTLV-1 protein expression, whereas the knockdown of Ku70 promoted the HTLV-1 protein expression. Furthermore, the overexpression of Ku70 enhanced the cellular response to HTLV-1 infection, whereas Ku70 knockdown yielded the opposite effect. Additionally, Ku70 was found to interact with HTLV-1 reverse transcription intermediate ssDNA90. ssDNA90 stimulation induced Ku70 expression and Ku70 promoted ssDNA90-triggered innate immune responses. Finally, HTLV-1 infection enhanced the association between Ku70 and stimulator of IFN genes, suggesting that stimulator of IFN genes was involved in Ku70-mediated host defenses against HTLV-1 infection. Taken together, our findings suggest a new sensor that detects HTLV-1 reverse transcription intermediate and controls HTLV-1 replication. These findings may provide new angles to understand host defenses against HTLV-1 infection and HTLV-1-associated diseases.
[Mh] Termos MeSH primário: DNA Viral
Vírus 1 Linfotrópico T Humano/fisiologia
Autoantígeno Ku/genética
Autoantígeno Ku/metabolismo
Replicação Viral
[Mh] Termos MeSH secundário: Células Cultivadas
Produtos do Gene tax/genética
Células HeLa
Vírus 1 Linfotrópico T Humano/genética
Vírus 1 Linfotrópico T Humano/imunologia
Seres Humanos
Imunidade Inata
Interferons/genética
Interferons/imunologia
Autoantígeno Ku/deficiência
Autoantígeno Ku/imunologia
Macrófagos/virologia
Monócitos/virologia
Produtos do Gene gag do Vírus da Imunodeficiência Humana/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Viral); 0 (Gene Products, tax); 0 (gag Gene Products, Human Immunodeficiency Virus); 0 (p19 protein, Human T-lymphotropic virus 1); 9008-11-1 (Interferons); EC 4.2.99.- (Ku Autoantigen)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170820
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1700111


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[PMID]:28712728
[Au] Autor:Morchikh M; Cribier A; Raffel R; Amraoui S; Cau J; Severac D; Dubois E; Schwartz O; Bennasser Y; Benkirane M
[Ad] Endereço:Institut de Génétique Humaine, Laboratoire de Virologie Moléculaire, Université de Montpellier, CNRS UMR9002, 34000 Montpellier, France. Electronic address: mehdi.morchikh@igh.cnrs.fr.
[Ti] Título:HEXIM1 and NEAT1 Long Non-coding RNA Form a Multi-subunit Complex that Regulates DNA-Mediated Innate Immune Response.
[So] Source:Mol Cell;67(3):387-399.e5, 2017 Aug 03.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The DNA-mediated innate immune response underpins anti-microbial defenses and certain autoimmune diseases. Here we used immunoprecipitation, mass spectrometry, and RNA sequencing to identify a ribonuclear complex built around HEXIM1 and the long non-coding RNA NEAT1 that we dubbed the HEXIM1-DNA-PK-paraspeckle components-ribonucleoprotein complex (HDP-RNP). The HDP-RNP contains DNA-PK subunits (DNAPKc, Ku70, and Ku80) and paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATRIN3). We show that binding of HEXIM1 to NEAT1 is required for its assembly. We further demonstrate that the HDP-RNP is required for the innate immune response to foreign DNA, through the cGAS-STING-IRF3 pathway. The HDP-RNP interacts with cGAS and its partner PQBP1, and their interaction is remodeled by foreign DNA. Remodeling leads to the release of paraspeckle proteins, recruitment of STING, and activation of DNAPKc and IRF3. Our study establishes the HDP-RNP as a key nuclear regulator of DNA-mediated activation of innate immune response through the cGAS-STING pathway.
[Mh] Termos MeSH primário: DNA/imunologia
Herpesvirus Humano 8/imunologia
Imunidade Inata
RNA Longo não Codificante/imunologia
Proteínas de Ligação a RNA/imunologia
[Mh] Termos MeSH secundário: Proteínas de Ligação ao Cálcio/genética
Proteínas de Ligação ao Cálcio/imunologia
Proteínas de Ligação ao Cálcio/metabolismo
DNA/genética
DNA/metabolismo
Células HEK293
Células HeLa
Interações Hospedeiro-Patógeno
Células Endoteliais da Veia Umbilical Humana/imunologia
Células Endoteliais da Veia Umbilical Humana/metabolismo
Células Endoteliais da Veia Umbilical Humana/virologia
Seres Humanos
Fator Regulador 3 de Interferon/genética
Fator Regulador 3 de Interferon/imunologia
Fator Regulador 3 de Interferon/metabolismo
Peptídeos e Proteínas de Sinalização Intracelular/genética
Peptídeos e Proteínas de Sinalização Intracelular/imunologia
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Autoantígeno Ku/genética
Autoantígeno Ku/imunologia
Autoantígeno Ku/metabolismo
Proteínas de Membrana/genética
Proteínas de Membrana/imunologia
Proteínas de Membrana/metabolismo
Complexos Multiproteicos
Proteínas Associadas à Matriz Nuclear/genética
Proteínas Associadas à Matriz Nuclear/imunologia
Proteínas Associadas à Matriz Nuclear/metabolismo
Proteínas Nucleares/genética
Proteínas Nucleares/imunologia
Proteínas Nucleares/metabolismo
Nucleotidiltransferases/genética
Nucleotidiltransferases/imunologia
Nucleotidiltransferases/metabolismo
Fatores de Transcrição de Octâmero/genética
Fatores de Transcrição de Octâmero/imunologia
Fatores de Transcrição de Octâmero/metabolismo
Fator de Processamento Associado a PTB/genética
Fator de Processamento Associado a PTB/imunologia
Fator de Processamento Associado a PTB/metabolismo
Ligação Proteica
Interferência de RNA
RNA Longo não Codificante/genética
RNA Longo não Codificante/metabolismo
Proteínas de Ligação a RNA/genética
Proteínas de Ligação a RNA/metabolismo
Transdução de Sinais
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CIB1 protein, human); 0 (Calcium-Binding Proteins); 0 (HEXIM1 protein, human); 0 (IRF3 protein, human); 0 (Interferon Regulatory Factor-3); 0 (Intracellular Signaling Peptides and Proteins); 0 (MATR3 protein, human); 0 (MPYS protein, human); 0 (Membrane Proteins); 0 (Multiprotein Complexes); 0 (NEAT1 long non-coding RNA, human); 0 (NONO protein, human); 0 (Nuclear Matrix-Associated Proteins); 0 (Nuclear Proteins); 0 (Octamer Transcription Factors); 0 (PSPC1 protein, human); 0 (PTB-Associated Splicing Factor); 0 (RBM14 protein, human); 0 (RNA, Long Noncoding); 0 (RNA-Binding Proteins); 9007-49-2 (DNA); EC 2.7.7.- (MB21D1 protein, human); EC 2.7.7.- (Nucleotidyltransferases); EC 3.6.4.12 (XRCC5 protein, human); EC 3.6.4.12 (Xrcc6 protein, human); EC 4.2.99.- (Ku Autoantigen)
[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:170718
[St] Status:MEDLINE


  7 / 1620 MEDLINE  
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[PMID]:28578657
[Au] Autor:Lindström R; Lindholm P; Palgi M; Saarma M; Heino TI
[Ad] Endereço:Department of Biosciences, University of Helsinki, FI-00014, Helsinki, Finland. riitta.lindstrom@helsinki.fi.
[Ti] Título:In vivo screening reveals interactions between Drosophila Manf and genes involved in the mitochondria and the ubiquinone synthesis pathway.
[So] Source:BMC Genet;18(1):52, 2017 Jun 02.
[Is] ISSN:1471-2156
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Mesencephalic Astrocyte-derived Neurotrophic Factor (MANF) and Cerebral Dopamine Neurotrophic Factor (CDNF) form an evolutionarily conserved family of neurotrophic factors. Orthologues for MANF/CDNF are the only neurotrophic factors as yet identified in invertebrates with conserved amino acid sequence. Previous studies indicate that mammalian MANF and CDNF support and protect brain dopaminergic system in non-cell-autonomous manner. However, MANF has also been shown to function intracellularly in the endoplasmic reticulum. To date, the knowledge on the interacting partners of MANF/CDNF and signaling pathways they activate is rudimentary. Here, we have employed the Drosophila genetics to screen for potential interaction partners of Drosophila Manf (DmManf) in vivo. RESULTS: We first show that DmManf plays a role in the development of Drosophila wing. We exploited this function by using Drosophila UAS-RNAi lines and discovered novel genetic interactions of DmManf with genes known to function in the mitochondria. We also found evidence of an interaction between DmManf and the Drosophila homologue encoding Ku70, the closest structural homologue of SAP domain of mammalian MANF. CONCLUSIONS: In addition to the previously known functions of MANF/CDNF protein family, DmManf also interacts with mitochondria-related genes. Our data supports the functional importance of these evolutionarily significant proteins and provides new insights for the future studies.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Drosophila melanogaster/genética
Genes Mitocondriais
Fatores de Crescimento Neural/metabolismo
Ubiquinona/biossíntese
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados/crescimento & desenvolvimento
Proteínas de Drosophila/antagonistas & inibidores
Proteínas de Drosophila/genética
Drosophila melanogaster/crescimento & desenvolvimento
Drosophila melanogaster/metabolismo
Feminino
Autoantígeno Ku/genética
Autoantígeno Ku/metabolismo
Masculino
Fatores de Crescimento Neural/genética
RNA Interferente Pequeno
Asas de Animais/crescimento & desenvolvimento
Asas de Animais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (MANF protein, Drosophila); 0 (Nerve Growth Factors); 0 (RNA, Small Interfering); 1339-63-5 (Ubiquinone); EC 4.2.99.- (Ku Autoantigen)
[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:170606
[St] Status:MEDLINE
[do] DOI:10.1186/s12863-017-0509-3


  8 / 1620 MEDLINE  
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[PMID]:28238784
[Au] Autor:Tao NN; Ren JH; Tang H; Ran LK; Zhou HZ; Liu B; Huang AL; Chen J
[Ad] Endereço:The Second Affiliated Hospital and the Key Laboratory of Molecular Biology of Infectious Diseases Designated by the Chinese Ministry of Education, Chongqing Medical University, Chongqing, China.
[Ti] Título:Deacetylation of Ku70 by SIRT6 attenuates Bax-mediated apoptosis in hepatocellular carcinoma.
[So] Source:Biochem Biophys Res Commun;485(4):713-719, 2017 Apr 15.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:SIRT6 is a class III histone deacetylase that has been implicated in HCC development. We previously reported that SIRT6 potentiated apoptosis evasion in hepatocellular carcinoma by inhibiting both Bax expression and mitochondrial translocalization. However, the mechanism underlying SIRT6-mediated inhibition of Bax mitochondrial localization remains elusive. In this study, we found that although SIRT6 had no effect on the expression level of Ku70, SIRT6 could interact with Ku70 and deacetylate it. The increased acetylation of Ku70 in SIRT6-depleted cells disrupt its interaction with Bax, which finally resulted in Bax mitochondrial translocalization. Furthermore, lysine K542 on Ku70 was the target for deacetylation by SIRT6. Ku70 mutation abolished suppression of association between Ku70 and Bax and caused redistribution of Bax to the cytosol in SIRT6-depleted cells. Finally, Ku70 mutation could reversed the inhibition of growth and apoptosis promotion mediated by SIRT6 silencing. Together, our findings revealed SIRT6 could block the mitochondrial translocation of Bax and decrease the apoptotic ratio of HCC cells by deacetylation of Ku70. SIRT6 may serve as a promising target for developing targeted therapies for HCC in the future.
[Mh] Termos MeSH primário: Apoptose
Autoantígeno Ku/metabolismo
Sirtuínas/metabolismo
Proteína X Associada a bcl-2/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Western Blotting
Carcinoma Hepatocelular/genética
Carcinoma Hepatocelular/metabolismo
Carcinoma Hepatocelular/patologia
Linhagem Celular Tumoral
Expressão Gênica
Seres Humanos
Autoantígeno Ku/genética
Neoplasias Hepáticas/genética
Neoplasias Hepáticas/metabolismo
Neoplasias Hepáticas/patologia
Lisina/genética
Lisina/metabolismo
Microscopia de Fluorescência
Mitocôndrias/metabolismo
Mutação
Ligação Proteica
Transporte Proteico/genética
Interferência de RNA
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Sirtuínas/genética
Proteína X Associada a bcl-2/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (bcl-2-Associated X Protein); EC 3.5.1.- (SIRT6 protein, human); EC 3.5.1.- (Sirtuins); EC 4.2.99.- (Ku Autoantigen); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170612
[Lr] Data última revisão:
170612
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170228
[St] Status:MEDLINE


  9 / 1620 MEDLINE  
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[PMID]:28186989
[Au] Autor:Dong J; Zhang T; Ren Y; Wang Z; Ling CC; He F; Li GC; Wang C; Wen B
[Ad] Endereço:Department of Radiation Oncology, The First Affiliated Hospital, Sun Yat-sen University, Guangzhou 510080, China.
[Ti] Título:Inhibiting DNA-PKcs in a non-homologous end-joining pathway in response to DNA double-strand breaks.
[So] Source:Oncotarget;8(14):22662-22673, 2017 Apr 04.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:DNA-dependent protein kinase catalytic subunit (DNA-PKcs) is a distinct factor in the non-homologous end-joining (NHEJ) pathway involved in DNA double-strand break (DSB) repair. We examined the crosstalk between key proteins in the DSB NHEJ repair pathway and cell cycle regulation and found that mouse embryonic fibroblast (MEF) cells deficient in DNA-PKcs or Ku70 were more vulnerable to ionizing radiation (IR) compared with wild-type cells and that DSB repair was delayed. γH2AX was associated with phospho-Ataxia-telangiectasia mutated kinase (Ser1987) and phospho-checkpoint effector kinase 1 (Ser345) foci for the arrest of cell cycle through the G2/M phase. Inhibition of DNA-PKcs prolonged IR-induced G2/M phase arrest because of sequential activation of cell cycle checkpoints. DSBs were introduced, and cell cycle checkpoints were recruited after exposure to IR in nasopharyngeal carcinoma SUNE-1 cells. NU7441 radiosensitized MEF cells and SUNE-1 cells by interfering with DSB repair. Together, these results reveal a mechanism in which coupling of DSB repair with the cell cycle radiosensitizes NHEJ repair-deficient cells, justifying further development of DNA-PK inhibitors in cancer therapy.
[Mh] Termos MeSH primário: Carcinoma/genética
Quebras de DNA de Cadeia Dupla/efeitos dos fármacos
Reparo do DNA por Junção de Extremidades/genética
Proteína Quinase Ativada por DNA/antagonistas & inibidores
Proteínas de Ligação a DNA/antagonistas & inibidores
Autoantígeno Ku/fisiologia
Neoplasias Nasofaríngeas/genética
Proteínas Nucleares/antagonistas & inibidores
Tolerância a Radiação/genética
[Mh] Termos MeSH secundário: Animais
Apoptose
Proteínas Mutadas de Ataxia Telangiectasia/metabolismo
Carcinoma/patologia
Pontos de Checagem do Ciclo Celular/efeitos dos fármacos
Pontos de Checagem do Ciclo Celular/efeitos da radiação
Proliferação Celular
Quinase do Ponto de Checagem 1/metabolismo
Cromonas/farmacologia
Proteína Quinase Ativada por DNA/fisiologia
Proteínas de Ligação a DNA/fisiologia
Embrião de Mamíferos/citologia
Embrião de Mamíferos/efeitos dos fármacos
Embrião de Mamíferos/efeitos da radiação
Fibroblastos/citologia
Fibroblastos/efeitos dos fármacos
Fibroblastos/efeitos da radiação
Camundongos
Camundongos Knockout
Morfolinas/farmacologia
Neoplasias Nasofaríngeas/patologia
Proteínas Nucleares/fisiologia
Radiação Ionizante
Radiossensibilizantes/farmacologia
Células Tumorais Cultivadas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (8-dibenzothiophen-4-yl-2-morpholin-4-yl-chromen-4-one); 0 (Chromones); 0 (DNA-Binding Proteins); 0 (Morpholines); 0 (Nuclear Proteins); 0 (Radiation-Sensitizing Agents); EC 2.7.1.- (Atr protein, mouse); EC 2.7.11.1 (Ataxia Telangiectasia Mutated Proteins); EC 2.7.11.1 (Checkpoint Kinase 1); EC 2.7.11.1 (Chek1 protein, mouse); EC 2.7.11.1 (DNA-Activated Protein Kinase); EC 2.7.11.1 (Prkdc protein, mouse); EC 3.6.4.12 (Xrcc6 protein, mouse); EC 4.2.99.- (Ku Autoantigen)
[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:170211
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15153


  10 / 1620 MEDLINE  
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[PMID]:28154079
[Au] Autor:Sibanda BL; Chirgadze DY; Ascher DB; Blundell TL
[Ad] Endereço:Department of Biochemistry, University of Cambridge, Old Addenbrooke's Site, 80 Tennis Court Road, Cambridge CB2 1GA, UK.
[Ti] Título:DNA-PKcs structure suggests an allosteric mechanism modulating DNA double-strand break repair.
[So] Source:Science;355(6324):520-524, 2017 02 03.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:DNA-dependent protein kinase catalytic subunit (DNA-PKcs) is a central component of nonhomologous end joining (NHEJ), repairing DNA double-strand breaks that would otherwise lead to apoptosis or cancer. We have solved its structure in complex with the C-terminal peptide of Ku80 at 4.3 angstrom resolution using x-ray crystallography. We show that the 4128-amino acid structure comprises three large structural units: the N-terminal unit, the Circular Cradle, and the Head. Conformational differences between the two molecules in the asymmetric unit are correlated with changes in accessibility of the kinase active site, which are consistent with an allosteric mechanism to bring about kinase activation. The location of KU80ct in the vicinity of the breast cancer 1 (BRCA1) binding site suggests competition with BRCA1, leading to pathway selection between NHEJ and homologous recombination.
[Mh] Termos MeSH primário: Quebras de DNA de Cadeia Dupla
Reparo do DNA por Junção de Extremidades
Proteína Quinase Ativada por DNA/química
Proteína Quinase Ativada por DNA/metabolismo
Proteínas Nucleares/química
Proteínas Nucleares/metabolismo
[Mh] Termos MeSH secundário: Proteína BRCA1/química
Domínio Catalítico
Cristalografia por Raios X
DNA/química
DNA/ultraestrutura
Células HeLa
Seres Humanos
Autoantígeno Ku/química
Peptídeos/química
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (BRCA1 Protein); 0 (Nuclear Proteins); 0 (Peptides); 9007-49-2 (DNA); EC 2.7.11.1 (DNA-Activated Protein Kinase); EC 2.7.11.1 (PRKDC protein, human); EC 4.2.99.- (Ku Autoantigen)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170204
[St] Status:MEDLINE
[do] DOI:10.1126/science.aak9654



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