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[PMID]:28457968
[Au] Autor:Xu D; Aka JA; Wang R; Lin SX
[Ad] Endereço:Laboratory of Molecular Endocrinology and Oncology, Centre Hospitalier Universitaire de Québec Research Centre (CHUQ, CHUL) and Department of Molecular Medicine, Laval University, 2705 Boulevard Laurier, Quebec City, Québec G1V 4G2, Canada.
[Ti] Título:17beta-hydroxysteroid dehydrogenase type 5 is negatively correlated to apoptosis inhibitor GRP78 and tumor-secreted protein PGK1, and modulates breast cancer cell viability and proliferation.
[So] Source:J Steroid Biochem Mol Biol;171:270-280, 2017 07.
[Is] ISSN:1879-1220
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:17beta-hydroxysteroid dehydrogenase type 5 (17ß-HSD5) is an important enzyme associated with sex steroid metabolism in hormone-dependent cancer. However, reports on its expression and its prognostic value in breast cancer are inconsistent. Here, we demonstrate the impact of 17ß-HSD5 expression modulation on the proteome of estrogen receptor-positive (ER+) breast cancer cells. RNA interference technique (siRNA) was used to knock down 17ß-HSD5 gene expression in the ER+ breast cancer cell line MCF-7 and the proteome of the 17ß-HSD5-knockdown cells was compared to that of MCF-7 cells using two-dimensional (2-D) gel electrophoresis followed by mass spectrometry analysis. Ingenuity pathway analysis (IPA) was additionally used to assess functional enrichment analyses of the proteomic dataset, including protein network and canonical pathways. Our proteomic analysis revealed only four differentially expressed protein spots (fold change > 2, p<0.05) between the two cell lines. The four spots were up-regulated in 17ß-HSD5-knockdown MCF-7 cells, and comprised 21 proteins involved in two networks and in functions that include apoptosis inhibition, regulation of cell growth and differentiation, signal transduction and tumor metastasis. Among the proteins are nucleoside diphosphate kinase A (NME1), 78kDa glucose-regulated protein (GRP78) and phosphoglycerate kinase 1 (PGK1). We also showed that expression of 17ß-HSD5 and that of the apoptosis inhibitor GRP78 are strongly but negatively correlated. Consistent with their opposite regulation, GRP78 knockdown decreased MCF-7 cell viability whereas 17ß-HSD5 knockdown or inhibition increased cell viability and proliferation. Besides, IPA analysis revealed that ubiquitination pathway is significantly affected by 17ß-HSD5 knockdown. Furthermore, IPA predicted the proto-oncogene c-Myc as an upstream regulator linked to the tumor-secreted protein PGK1. The latter is over-expressed in invasive ductal breast carcinoma as compared with normal breast tissue and its expression increased following 17ß-HSD5 knockdown. Our present results indicate a 17ß-HSD5 role in down-regulating breast cancer development. We thus propose that 17ß-HSD5 may not be a potent target for breast cancer treatment but its low expression could represent a poor prognosis factor.
[Mh] Termos MeSH primário: 3-Hidroxiesteroide Desidrogenases/metabolismo
Neoplasias da Mama/metabolismo
Regulação Neoplásica da Expressão Gênica
Proteínas de Choque Térmico/metabolismo
Hidroxiprostaglandina Desidrogenases/metabolismo
Proteínas de Neoplasias/metabolismo
Fosfoglicerato Quinase/metabolismo
[Mh] Termos MeSH secundário: 3-Hidroxiesteroide Desidrogenases/antagonistas & inibidores
3-Hidroxiesteroide Desidrogenases/química
3-Hidroxiesteroide Desidrogenases/genética
Membro C3 da Família 1 de alfa-Ceto Redutase
Neoplasias da Mama/patologia
Proliferação Celular
Sobrevivência Celular
Ativação Enzimática
Feminino
Perfilação da Expressão Gênica
Proteínas de Choque Térmico/antagonistas & inibidores
Proteínas de Choque Térmico/química
Proteínas de Choque Térmico/genética
Seres Humanos
Hidroxiprostaglandina Desidrogenases/antagonistas & inibidores
Hidroxiprostaglandina Desidrogenases/química
Hidroxiprostaglandina Desidrogenases/genética
Processamento de Imagem Assistida por Computador
Células MCF-7
Nucleosídeo NM23 Difosfato Quinases/química
Nucleosídeo NM23 Difosfato Quinases/genética
Nucleosídeo NM23 Difosfato Quinases/metabolismo
Proteínas de Neoplasias/antagonistas & inibidores
Proteínas de Neoplasias/química
Proteínas de Neoplasias/genética
Fosfoglicerato Quinase/química
Fosfoglicerato Quinase/genética
Proteômica/métodos
Proteínas Proto-Oncogênicas c-myc/química
Proteínas Proto-Oncogênicas c-myc/genética
Proteínas Proto-Oncogênicas c-myc/metabolismo
Interferência de RNA
Receptores Estrogênicos/metabolismo
Eletroforese em Gel Diferencial Bidimensional
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Heat-Shock Proteins); 0 (MYC protein, human); 0 (NM23 Nucleoside Diphosphate Kinases); 0 (Neoplasm Proteins); 0 (Proto-Oncogene Proteins c-myc); 0 (Receptors, Estrogen); 0 (molecular chaperone GRP78); EC 1.1.- (3-Hydroxysteroid Dehydrogenases); EC 1.1.1.- (Hydroxyprostaglandin Dehydrogenases); EC 1.1.1.357 (AKR1C3 protein, human); EC 1.1.1.357 (Aldo-Keto Reductase Family 1 Member C3); EC 2.7.2.3 (PGK1 protein, human); EC 2.7.2.3 (Phosphoglycerate Kinase); EC 2.7.4.6 (NME1 protein, human)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171208
[Lr] Data última revisão:
171208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE


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[PMID]:28767310
[Au] Autor:Parada-Sanchez MT; Chu EY; Cox LL; Undurty SS; Standley JM; Murray JC; Cox TC
[Ad] Endereço:1 School of Dentistry, Universidad de Antioquia, Medellín, Colombia.
[Ti] Título:Disrupted IRF6-NME1/2 Complexes as a Cause of Cleft Lip/Palate.
[So] Source:J Dent Res;96(11):1330-1338, 2017 Oct.
[Is] ISSN:1544-0591
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mutations and common polymorphisms in interferon regulatory factor 6 ( IRF6) are associated with both syndromic and nonsyndromic forms of cleft lip/palate (CLP). To date, much of the focus on this transcription factor has been on identifying its direct targets and the gene regulatory network in which it operates. Notably, however, IRF6 is found predominantly in the cytoplasm, with its import into the nucleus tightly regulated like other members of the IRF family. To provide further insight into the role of IRF6 in the pathogenesis of CLP, we sought to identify direct IRF6 protein interactors using a combination of yeast 2-hybrid screens and co-immunoprecipitation assays. Using this approach, we identified NME1 and NME2, well-known regulators of Rho-type GTPases, E-cadherin endocytosis, and epithelial junctional remodeling, as bona fide IRF6 partner proteins. The NME proteins co-localize with IRF6 in the cytoplasm of primary palatal epithelial cells in vivo, and their interaction with IRF6 is significantly enhanced by phosphorylation of key serine residues in the IRF6 C-terminus. Furthermore, CLP associated IRF6 missense mutations disrupt the ability of IRF6 to bind the NME proteins and result in elevated activation of Rac1 and RhoA, compared to wild-type IRF6, when ectopically expressed in 293T epithelial cells. Significantly, we also report the identification of 2 unique missense mutations in the NME proteins in patients with CLP (NME1 R18Q in an IRF6 and GRHL3 mutation-negative patient with van der Woude syndrome and NME2 G71V in a patient with nonsyndromic CLP). Both variants disrupted the ability of the respective proteins to interact with IRF6. The data presented suggest an important role for cytoplasmic IRF6 in regulating the availability or localization of the NME1/2 complex and thus the dynamic behavior of epithelia during lip/palate development.
[Mh] Termos MeSH primário: Fenda Labial/genética
Fissura Palatina/genética
Fatores Reguladores de Interferon/genética
Nucleosídeo NM23 Difosfato Quinases/genética
[Mh] Termos MeSH secundário: Animais
Embrião de Galinha
Variação Genética
Seres Humanos
Imunoprecipitação
Mutação
Fosforilação
Reação em Cadeia da Polimerase
Aderências Teciduais/genética
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (IRF6 protein, human); 0 (Interferon Regulatory Factors); 0 (NM23 Nucleoside Diphosphate Kinases); 0 (Transcription Factors); EC 2.7.4.6 (NME1 protein, human); EC 2.7.4.6 (NME2 protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:D; IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE
[do] DOI:10.1177/0022034517723615


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[PMID]:28717007
[Au] Autor:Saha D; Singh A; Hussain T; Srivastava V; Sengupta S; Kar A; Dhapola P; Dhople V; Ummanni R; Chowdhury S
[Ad] Endereço:From the Genomics and Molecular Medicine Unit.
[Ti] Título:Epigenetic suppression of human telomerase ( ) is mediated by the metastasis suppressor NME2 in a G-quadruplex-dependent fashion.
[So] Source:J Biol Chem;292(37):15205-15215, 2017 Sep 15.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Transcriptional activation of the human telomerase reverse transcriptase ( ) gene, which remains repressed in adult somatic cells, is critical during tumorigenesis. Several transcription factors and the epigenetic state of the promoter are known to be important for tight control of in normal tissues, but the molecular mechanisms leading to reactivation in cancer are not well-understood. Surprisingly, here we found occupancy of the metastasis suppressor non-metastatic 2 (NME2) within the core promoter in HT1080 fibrosarcoma cells and HCT116 colon cancer cells and NME2-mediated transcriptional repression of in these cells. We also report that loss of NME2 results in up-regulated expression. Mechanistically, additional results indicated that the RE1-silencing transcription factor (REST)-lysine-specific histone demethylase 1 (LSD1) co-repressor complex associates with the promoter in an NME2-dependent way and that this assembly is required for maintaining repressive chromatin at the promoter. Interestingly, a G-quadruplex motif at the promoter was essential for occupancy of NME2 and the REST repressor complex on the promoter. In light of this mechanistic insight, we studied the effects of G-quadruplex-binding ligands on expression and observed that several of these ligands repressed expression. Together, our results support a mechanism of epigenetic control involving a G-quadruplex promoter motif, which potentially can be targeted by tailored small molecules.
[Mh] Termos MeSH primário: Carcinoma/metabolismo
Repressão Epigenética
Fibrossarcoma/metabolismo
Quadruplex G
Nucleosídeo NM23 Difosfato Quinases/metabolismo
Regiões Promotoras Genéticas
Telomerase/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Carcinoma/enzimologia
Carcinoma/patologia
Linhagem Celular Tumoral
Células Cultivadas
Imunoprecipitação da Cromatina
Fibrossarcoma/enzimologia
Fibrossarcoma/patologia
Genes Reporter
Histona Desmetilases/química
Histona Desmetilases/metabolismo
Seres Humanos
Mutagênese Sítio-Dirigida
Nucleosídeo NM23 Difosfato Quinases/antagonistas & inibidores
Nucleosídeo NM23 Difosfato Quinases/química
Nucleosídeo NM23 Difosfato Quinases/genética
Proteínas de Neoplasias/antagonistas & inibidores
Proteínas de Neoplasias/química
Proteínas de Neoplasias/genética
Proteínas de Neoplasias/metabolismo
Mutação Puntual
Multimerização Proteica
Interferência de RNA
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Proteínas Repressoras/antagonistas & inibidores
Proteínas Repressoras/química
Proteínas Repressoras/genética
Proteínas Repressoras/metabolismo
Telomerase/antagonistas & inibidores
Telomerase/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NM23 Nucleoside Diphosphate Kinases); 0 (Neoplasm Proteins); 0 (RE1-silencing transcription factor); 0 (Recombinant Proteins); 0 (Repressor Proteins); EC 1.14.11.- (Histone Demethylases); EC 1.5.- (KDM1A protein, human); EC 2.7.4.6 (NME1 protein, human); EC 2.7.4.6 (NME2 protein, human); EC 2.7.7.49 (TERT protein, human); EC 2.7.7.49 (Telomerase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170927
[Lr] Data última revisão:
170927
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170719
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.792077


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[PMID]:28714689
[Au] Autor:Wang YQ; Huang ZL; Chen SB; Wang CX; Shan C; Yin QK; Ou TM; Li D; Gu LQ; Tan JH; Huang ZS
[Ad] Endereço:School of Pharmaceutical Sciences, Sun Yat-sen University , Guangzhou 510006, People's Republic of China.
[Ti] Título:Design, Synthesis, and Evaluation of New Selective NM23-H2 Binders as c-MYC Transcription Inhibitors via Disruption of the NM23-H2/G-Quadruplex Interaction.
[So] Source:J Med Chem;60(16):6924-6941, 2017 Aug 24.
[Is] ISSN:1520-4804
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:c-MYC is one of the important human proto-oncogenes, and transcriptional factor NM23-H2 can activate c-MYC transcription by recognizing the G-quadruplex in the promoter of the gene. Small molecules that inhibit c-MYC transcription by disrupting the NM23-H2/G-quadruplex interaction might be a promising strategy for developing selective anticancer agents. In recent studies, we developed a series of isaindigotone derivatives, which can bind to G-quadruplex and NM23-H2, thus down-regulating c-MYC ( J. Med. Chem. 2017 , 60 , 1292 - 1308 ). Herein, a series of novel isaindigotone derivatives were designed, synthesized, and screened for NM23-H2 selective binding ligands. Among them, compound 37 showed a high specific binding affinity to NM23-H2, effectively disrupting the interaction of NM23-H2 with G-quadruplex, and it strongly down-regulated c-MYC transcription. Furthermore, 37 induced cell cycle arrest and apoptosis, and it exhibited good tumor growth inhibition in a mouse xenograft model. This work provides a new strategy to modulate c-MYC transcription for the development of selective anticancer drugs.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Quadruplex G
Nucleosídeo NM23 Difosfato Quinases/antagonistas & inibidores
Proteínas Proto-Oncogênicas c-myc/antagonistas & inibidores
Pirróis/farmacologia
Quinazolinas/farmacologia
Quinazolinonas/farmacologia
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/administração & dosagem
Antineoplásicos/síntese química
Antineoplásicos/química
Apoptose/efeitos dos fármacos
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Regulação para Baixo
Doxorrubicina/farmacologia
Desenho de Drogas
Pontos de Checagem da Fase G1 do Ciclo Celular/efeitos dos fármacos
Seres Humanos
Ligantes
Camundongos Endogâmicos BALB C
Simulação de Acoplamento Molecular
Nucleosídeo NM23 Difosfato Quinases/química
Nucleosídeo NM23 Difosfato Quinases/genética
Regiões Promotoras Genéticas
Proteínas Proto-Oncogênicas c-myc/genética
Pirróis/administração & dosagem
Pirróis/síntese química
Pirróis/química
Quinazolinas/administração & dosagem
Quinazolinas/síntese química
Quinazolinas/química
Quinazolinonas/administração & dosagem
Quinazolinonas/síntese química
Quinazolinonas/química
Relação Estrutura-Atividade
Transcrição Genética
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3-(4-(benzyloxy)-2-hydroxybenzylidene)-6-((3-(dimethylamino)propyl)amino)-7-fluoro-2,3-dihydropyrrolo(2,1-b)quinazolin-9(1H)-one); 0 (Antineoplastic Agents); 0 (Ligands); 0 (MYC protein, human); 0 (NM23 Nucleoside Diphosphate Kinases); 0 (Proto-Oncogene Proteins c-myc); 0 (Pyrroles); 0 (Quinazolines); 0 (Quinazolinones); 80168379AG (Doxorubicin); EC 2.7.4.6 (NME2 protein, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jmedchem.7b00421


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[PMID]:28614246
[Au] Autor:Yuan C; Xu XH; Xu L; Sun M; Ni LH; Liu Y; Ran F; Wang XL; Chen Z; Zhang K; Zeng G
[Ad] Endereço:aThe First College of Clinical Medical Science, China Three Gorges University bDepartment of Oncology, Yichang Central People's Hospital, Yichang cDepartment of Oncology, Zhongnan Hospital of Wuhan University, Hubei Key Laboratory of Tumor Biological Behaviors & Hubei Cancer Clinical Study Center, Wuhan, China dZhongda Hospital, Southeast University, Nanjing eCentral Hospital of Enshi Autonomous Prefecture, Enshi, China fKlinikum rechts der Isar Technical University of Munich, München, Germany gBiomedical Engineering, Stony Brook University, Stony Brook, NY, USA.
[Ti] Título:Low expression of nm23-H1 associates with poor survival of nasopharyngeal carcinoma patients: A prisma-compliant meta-analysis.
[So] Source:Medicine (Baltimore);96(24):e7153, 2017 Jun.
[Is] ISSN:1536-5964
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Developing a new reliable prognostic marker to predict the prognosis and supply better and more suitable therapy for patients with nasopharyngeal carcinoma (NPC) is urgent. Therefore, we performed this systematic review of the literature with meta-analysis to clarify and explore the associate expression of nm23-H1 with prognosis of NPC patients. METHODS: Literature research in Cochrane Library, PubMed, and EMBASE was performed up to July 2016. Eligible case-control studies of associate expression of nm23-H1 with prognosis of NPC patients were included. RESULTS: Nine studies met our inclusion criteria and were finally included for the analysis, involving 861 participants. Our meta-analysis revealed that the low expression of nm23-H1 in NPC was: RR = 2.13, 95% CI 1.15-3.95 and R = 2.56, 95% CI 2.03-3.22; and poorer overall survival (OS) rate was 3-year OS rate: RR: 0.55; 95% CI: 0.45-0.67 and 5-year OS rate: RR: 0.60; 95% CI: 0.52-0.69. Furthermore, the statistical significance was constant irrespective of different NPC subtypes. CONCLUSION: The low expression of nm23-H1 is associated with poorer prognosis in patients with NPC, suggesting that it is a prognostic factor and potential biomarker for survival in NPC.
[Mh] Termos MeSH primário: Carcinoma/enzimologia
Carcinoma/mortalidade
Nucleosídeo NM23 Difosfato Quinases/metabolismo
Neoplasias Nasofaríngeas/enzimologia
Neoplasias Nasofaríngeas/mortalidade
[Mh] Termos MeSH secundário: Biomarcadores Tumorais/metabolismo
Carcinoma/diagnóstico
Seres Humanos
Neoplasias Nasofaríngeas/diagnóstico
[Pt] Tipo de publicação:JOURNAL ARTICLE; META-ANALYSIS; REVIEW
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (NM23 Nucleoside Diphosphate Kinases); EC 2.7.4.6 (NME1 protein, human)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170706
[Lr] Data última revisão:
170706
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170615
[St] Status:MEDLINE
[do] DOI:10.1097/MD.0000000000007153


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[PMID]:28442010
[Au] Autor:Sheng Y; Xiong Y; Xu M; Kuang X; Wang D; Yang X
[Ad] Endereço:Cancer Center, Daping Hospital and Research Institute of Surgery, Third Military Medical University, Chongqing 400042, China.
[Ti] Título:[Effect of Nm23-H1 Nuclear Localization on Proliferation of 
Human Lung Adenocarcinoma Cell Line A549].
[So] Source:Zhongguo Fei Ai Za Zhi;20(4):226-232, 2017 Apr 20.
[Is] ISSN:1999-6187
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:BACKGROUND: Recent studies have indicated that Nm23-H1 is found in the nucleus, but previous studies have been based on the overexpression or suppression of Nm23-H1 in the cytoplasm. Due to the lacking nuclear localization signal of Nm23-H1, these results cannot reflect or repeat cells in which Nm23-H1 mainly positioned in nuclei and whether they cause clinical biological effects. Therefore, to explore the effects of transposing Nm23-H1 from the cytoplasm to the nucleus during lung cancer cell proliferation, a vector with a nuclear localization signal of Nm23-H1 was constructed and A549 cells were transfected. METHODS: Gene recombination technology was used to construct pLentis-CMV-NME1-IRES2-PURO lentiviral vectors using a nuclear localization signal sequence, and the recombinant plasmid was verified using restriction enzyme analysis and sequencing. Nm23-H1 positioning and expression were performed after the stably transfected A549 cells were assessed by Western blot and confocal laser scanning microscope. The A549 cell proliferation was assessed using a cell counting kit-8. Flow cytometry was performed to assess the cell cycle distribution of A549 cells. RESULTS: The directional Nm23-H1 lentiviral vector was successfully constructed within the nucleus. Compared with that of the empty vector group, the proliferation rates of the transfection groups at 72 h, 96 h, and 120 h were remarkably increased (P<0.000,1). Moreover, the empty vector group of A549 cells in the G0/G1 phase proportion was 35.69%, which was higher than the 28.28% of the transfection group (t=1.461, P=0.217); furthermore, the transfection group of A549 cells in the G2/M phase proportion was 58.7% and that of the empty vector group was 31.30% (t=4.560, P=0.010). CONCLUSIONS: Human lung adenocarcinoma cell line A549 cells of Nm23-H1 nuclear localized mainly in the G2/M phase and the nuclear Nm23-H1 promoted A549 cell proliferation in vitro.
[Mh] Termos MeSH primário: Adenocarcinoma/enzimologia
Neoplasias Pulmonares/enzimologia
Nucleosídeo NM23 Difosfato Quinases/metabolismo
[Mh] Termos MeSH secundário: Células A549
Adenocarcinoma/genética
Adenocarcinoma/fisiopatologia
Ciclo Celular
Núcleo Celular/enzimologia
Núcleo Celular/genética
Proliferação Celular
Citoplasma/enzimologia
Citoplasma/genética
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Neoplasias Pulmonares/genética
Neoplasias Pulmonares/fisiopatologia
Nucleosídeo NM23 Difosfato Quinases/genética
Transporte Proteico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NM23 Nucleoside Diphosphate Kinases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170630
[Lr] Data última revisão:
170630
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170427
[St] Status:MEDLINE
[do] DOI:10.3779/j.issn.1009-3419.2017.04.02


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[PMID]:28401162
[Au] Autor:Fang M; Tao Y; Liu Z; Huang H; Lao M; Huang L; Zhu B
[Ad] Endereço:Department of Clinical Laboratory, The Affiliated Tumor Hospital of Guangxi Medical University, Nanning, Guangxi, China.
[Ti] Título:Meta-Analysis of the Relationship between NM23 Expression to Gastric Cancer Risk and Clinical Features.
[So] Source:Biomed Res Int;2017:8047183, 2017.
[Is] ISSN:2314-6141
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The prognostic value of reduced NM23 expression for gastric cancer (GC) patients is still contradictory. Thus, we conducted a meta-analysis to quantitatively evaluate the association of NM23 expression with GC risk and clinical features by analyzing 27 publications. The result of our meta-analysis indicated that NM23 expression is markedly reduced in gastric cancer tissues (OR = 3.15; 95% CI = 1.97-5.03; < 0.001). Furthermore, NM23 expression was negatively correlated with N stage, TNM stage, and histological grade. However, NM23 expression was not correlated with T stage, lymphatic invasion, vascular invasion, and 5-year overall survival rate. In conclusion, reduced NM23 expression correlated with gastric cancer risk, but its association with GC clinical features remains inconclusive. Therefore, large-scale and well-designed studies, which use uniform antibody and criterion of NM23 positive expression, are required to further validate the role of the NM23 in predicting GC progression.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/biossíntese
Nucleosídeo NM23 Difosfato Quinases/biossíntese
Prognóstico
Neoplasias Gástricas/genética
[Mh] Termos MeSH secundário: Biomarcadores Tumorais/genética
Progressão da Doença
Intervalo Livre de Doença
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Nucleosídeo NM23 Difosfato Quinases/genética
Estadiamento de Neoplasias
Fatores de Risco
Neoplasias Gástricas/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; META-ANALYSIS; REVIEW
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (NM23 Nucleoside Diphosphate Kinases); EC 2.7.4.6 (NME1 protein, human)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170428
[Lr] Data última revisão:
170428
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170413
[St] Status:MEDLINE
[do] DOI:10.1155/2017/8047183


  8 / 1220 MEDLINE  
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[PMID]:28376369
[Au] Autor:Khera L; Paul C; Kaul R
[Ad] Endereço:Department of Microbiology, University of Delhi, South Campus, New Delhi, India.
[Ti] Título:Hepatitis C Virus E1 protein promotes cell migration and invasion by modulating cellular metastasis suppressor Nm23-H1.
[So] Source:Virology;506:110-120, 2017 Jun.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hepatocellular carcinoma (HCC) is the most prevalent primary liver cancer and its incidence is on the rise largely attributed to Hepatitis C virus (HCV) related liver cancer. A distinct feature of HCV associated HCC is the substantially increased incidence of metastasis compared to non-viral or HBV associated HCC. Nm23-H1 is the first reported human metastasis suppressor down-regulated in many human metastatic cancers. Nm23-H1 functions are modulated in several virus associated cancers. Our study now shows that HCV E1 protein expression as well as HCV infection induces pro-metastatic effect on cancer cells which is simultaneous to Nm23-H1 transcriptional down-regulation and Nm23-H1 protein degradation. Moreover, Nm23-H1 intracellular localization is significantly altered in cells expressing HCV E1 protein. Importantly, overexpression of Nm23-H1 can rescue the cancer cells from pro-metastatic effects of HCV E1 and HCV infection. Our limited study provides evidence for role for Nm23-H1 in HCV mediated cancer metastasis.
[Mh] Termos MeSH primário: Carcinoma Hepatocelular/enzimologia
Carcinoma Hepatocelular/fisiopatologia
Hepacivirus/metabolismo
Neoplasias Hepáticas/fisiopatologia
Nucleosídeo NM23 Difosfato Quinases/metabolismo
Proteínas do Envelope Viral/metabolismo
[Mh] Termos MeSH secundário: Carcinoma Hepatocelular/patologia
Carcinoma Hepatocelular/virologia
Movimento Celular
Regulação para Baixo
Regulação Neoplásica da Expressão Gênica
Hepacivirus/genética
Seres Humanos
Neoplasias Hepáticas/enzimologia
Neoplasias Hepáticas/patologia
Neoplasias Hepáticas/virologia
Nucleosídeo NM23 Difosfato Quinases/genética
Invasividade Neoplásica
Proteínas do Envelope Viral/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (E1 protein, Hepatitis C virus); 0 (NM23 Nucleoside Diphosphate Kinases); 0 (Viral Envelope Proteins); EC 2.7.4.6 (NME1 protein, human)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170705
[Lr] Data última revisão:
170705
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170405
[St] Status:MEDLINE


  9 / 1220 MEDLINE  
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[PMID]:28366719
[Au] Autor:Li SW; Chen YC; Sheen JM; Hsu MH; Tain YL; Chang KA; Huang LT
[Ad] Endereço:Department of Pediatrics, Kaohsiung Chang Gung Memorial Hospital and Chang Gung University College of Medicine, Kaohsiung, Taiwan; Department of Medical Research, Kaohsiung Chang Gung Memorial Hospital, Kaohsiung, Taiwan.
[Ti] Título:Minocycline restores cognitive-relative altered proteins in young bile duct-ligated rat prefrontal cortex.
[So] Source:Life Sci;180:75-82, 2017 Jul 01.
[Is] ISSN:1879-0631
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:AIMS: Bile duct ligation (BDL) model is used to study hepatic encephalopathy accompanied by cognitive impairment. We employed the proteomic analysis approach to evaluate cognition-related proteins in the prefrontal cortex of young BDL rats and analyzed the effect of minocycline on these proteins and spatial memory. MAIN METHODS: BDL was induced in young rats at postnatal day 17. Minocycline as a slow-release pellet was implanted into the peritoneum. Morris water maze test and two-dimensional liquid chromatography-tandem mass spectrometry were used to evaluate spatial memory and prefrontal cortex protein expression, respectively. We used 2D/LC-MS/MS to analyze for affected proteins in the prefrontal cortex of young BDL rats. Results were verified with Western blotting, immunohistochemistry, and quantitative real-time PCR. The effect of minocycline in BDL rats was assessed. KEY FINDINGS: BDL induced spatial deficits, while minocycline rescued it. Collapsin response mediator protein 2 (CRMP2) and manganese-dependent superoxide dismutase (MnSOD) were upregulated and nucleoside diphosphate kinase B (NME2) was downregulated in young BDL rats. BDL rats exhibited decreased levels of brain-derived neurotrophic factor (BDNF) mRNA as compared with those by the control. However, minocycline treatment restored CRMP2 and NME2 protein expression, BDNF mRNA level, and MnSOD activity to control levels. SIGNIFICANCE: We demonstrated that BDL altered the expression of CRMP2, NME2, MnSOD, and BDNF in the prefrontal cortex of young BDL rats. However, minocycline treatment restored the expression of the affected mediators that are implicated in cognition.
[Mh] Termos MeSH primário: Transtornos Cognitivos/tratamento farmacológico
Encefalopatia Hepática/tratamento farmacológico
Minociclina/farmacologia
Córtex Pré-Frontal/efeitos dos fármacos
Memória Espacial/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Ductos Biliares/patologia
Western Blotting
Fator Neurotrófico Derivado do Encéfalo/efeitos dos fármacos
Cromatografia Líquida
Transtornos Cognitivos/etiologia
Preparações de Ação Retardada
Modelos Animais de Doenças
Encefalopatia Hepática/complicações
Masculino
Aprendizagem em Labirinto/efeitos dos fármacos
Minociclina/administração & dosagem
Nucleosídeo NM23 Difosfato Quinases/genética
Proteínas do Tecido Nervoso/genética
Proteômica/métodos
Ratos
Ratos Sprague-Dawley
Reação em Cadeia da Polimerase em Tempo Real
Superóxido Dismutase/metabolismo
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Brain-Derived Neurotrophic Factor); 0 (CRMP2 protein, rat); 0 (Delayed-Action Preparations); 0 (NM23 Nucleoside Diphosphate Kinases); 0 (Nerve Tissue Proteins); EC 1.15.1.1 (Superoxide Dismutase); FYY3R43WGO (Minocycline)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170629
[Lr] Data última revisão:
170629
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE


  10 / 1220 MEDLINE  
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[PMID]:28283480
[Au] Autor:Liyanage SU; Hurren R; Voisin V; Bridon G; Wang X; Xu C; MacLean N; Siriwardena TP; Gronda M; Yehudai D; Sriskanthadevan S; Avizonis D; Shamas-Din A; Minden MD; Bader GD; Laposa R; Schimmer AD
[Ad] Endereço:Princess Margaret Cancer Centre, Toronto, ON, Canada.
[Ti] Título:Leveraging increased cytoplasmic nucleoside kinase activity to target mtDNA and oxidative phosphorylation in AML.
[So] Source:Blood;129(19):2657-2666, 2017 May 11.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondrial DNA (mtDNA) biosynthesis requires replication factors and adequate nucleotide pools from the mitochondria and cytoplasm. We performed gene expression profiling analysis of 542 human acute myeloid leukemia (AML) samples and identified 55% with upregulated mtDNA biosynthesis pathway expression compared with normal hematopoietic cells. Genes that support mitochondrial nucleotide pools, including mitochondrial nucleotide transporters and a subset of cytoplasmic nucleoside kinases, were also increased in AML compared with normal hematopoietic samples. Knockdown of cytoplasmic nucleoside kinases reduced mtDNA levels in AML cells, demonstrating their contribution in maintaining mtDNA. To assess cytoplasmic nucleoside kinase pathway activity, we used a nucleoside analog 2'3'-dideoxycytidine (ddC), which is phosphorylated to the activated antimetabolite, 2'3'-dideoxycytidine triphosphate by cytoplasmic nucleoside kinases. ddC is a selective inhibitor of the mitochondrial DNA polymerase γ. ddC was preferentially activated in AML cells compared with normal hematopoietic progenitor cells. ddC treatment inhibited mtDNA replication, oxidative phosphorylation, and induced cytotoxicity in a panel of AML cell lines. Furthermore, ddC preferentially inhibited mtDNA replication in a subset of primary human leukemia cells and selectively targeted leukemia cells while sparing normal progenitor cells. In animal models of human AML, treatment with ddC decreased mtDNA, electron transport chain proteins, and induced tumor regression without toxicity. ddC also targeted leukemic stem cells in secondary AML xenotransplantation assays. Thus, AML cells have increased cytidine nucleoside kinase activity that regulates mtDNA biogenesis and can be leveraged to selectively target oxidative phosphorylation in AML.
[Mh] Termos MeSH primário: DNA Mitocondrial/genética
Leucemia Mieloide Aguda/genética
Leucemia Mieloide Aguda/metabolismo
Fosforilação Oxidativa
Fosfotransferases/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Células Cultivadas
Replicação do DNA
Seres Humanos
Camundongos SCID
Nucleosídeo NM23 Difosfato Quinases/metabolismo
Núcleosídeo-Fosfato Quinase/metabolismo
Transdução de Sinais
Células Tumorais Cultivadas
Zalcitabina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Mitochondrial); 0 (NM23 Nucleoside Diphosphate Kinases); 6L3XT8CB3I (Zalcitabine); EC 2.7.- (Phosphotransferases); EC 2.7.1.77 (nucleoside phosphotransferase); EC 2.7.4.4 (Nucleoside-Phosphate Kinase); EC 2.7.4.6 (NME1 protein, human); EC 2.7.4.6 (NME2 protein, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170908
[Lr] Data última revisão:
170908
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170312
[St] Status:MEDLINE
[do] DOI:10.1182/blood-2016-10-741207



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