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Referências encontradas : 616 [refinar]
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[PMID]:28464980
[Au] Autor:Moleirinho S; Hoxha S; Mandati V; Curtale G; Troutman S; Ehmer U; Kissil JL
[Ad] Endereço:Department of Molecular Medicine, The Scripps Research Institute, Jupiter, United States.
[Ti] Título:Regulation of localization and function of the transcriptional co-activator YAP by angiomotin.
[So] Source:Elife;6, 2017 05 03.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The Hippo-YAP pathway is a central regulator of cell contact inhibition, proliferation and death. There are conflicting reports regarding the role of Angiomotin (Amot) in regulating this pathway. While some studies suggest a YAP-inhibitory function other studies indicate Amot is required for YAP activity. Here, we describe an Amot-dependent complex comprised of Amot, YAP and Merlin. The phosphorylation of Amot at Serine 176 shifts localization of this complex to the plasma membrane, where it associates with the tight-junction proteins Pals1/PATJ and E-cadherin. Conversely, hypophosphorylated Amot shifts localization of the complex to the nucleus, where it facilitates the association of YAP and TEAD, induces transcriptional activation of YAP target genes and promotes YAP-dependent cell proliferation. We propose that phosphorylation of Amot is a critical post-translational modification that suppresses YAP's ability to promote cell proliferation and tumorigenesis by altering the subcellular localization of an essential YAP co-factor.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Peptídeos e Proteínas de Sinalização Intercelular/metabolismo
Proteínas de Membrana/metabolismo
Neurofibromina 2/metabolismo
Fosfoproteínas/metabolismo
Multimerização Proteica
Processamento de Proteína Pós-Traducional
[Mh] Termos MeSH secundário: Membrana Celular/química
Núcleo Celular/química
Células HEK293
Células Hep G2
Seres Humanos
Fosforilação
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (AMOT protein, human); 0 (Adaptor Proteins, Signal Transducing); 0 (Intercellular Signaling Peptides and Proteins); 0 (Membrane Proteins); 0 (Neurofibromin 2); 0 (Phosphoproteins); 0 (YAP1 (Yes-associated) protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180211
[Lr] Data última revisão:
180211
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


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[PMID]:28919412
[Au] Autor:Xing W; Li M; Zhang F; Ma X; Long J; Zhou H
[Ad] Endereço:State Key Laboratory of Medicinal Chemical Biology, Tianjin Key Laboratory of Protein Science, College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China.
[Ti] Título:The conformation change and tumor suppressor role of Merlin are both independent of Serine 518 phosphorylation.
[So] Source:Biochem Biophys Res Commun;493(1):46-51, 2017 Nov 04.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Merlin functions as a tumor suppressor and suppresses malignant activity of cancer cells through multiple mechanisms. However, whether Serine 518 phosphorylation regulates the conformation of Merlin as well as the open-closed conformational changes affect Merlin's tumor inhibitory activity remain controversial. In this study, we used different mutants to mimic related conformational states of Merlin and investigated its physiological functions. Our results showed that the phosphorylation at Serine 518 has no influence on Merlin's conformation, subcellular localization, or cell proliferation inhibitory activity. As a fully closed conformational state, the A585W mutant loses the ability to recruit Lats2 to the cell membrane, but it does not affect its subcellular distribution or cell proliferation inhibitory activity. As a fully open conformational state, mimicking the conformation of Merlin isoform II, the ΔEL mutant has the same physiological function as the wild type Merlin isoform I. Collectively, we provide for the first time in vivo evidence that the function of Merlin, as a tumor suppressor is independent of its conformational change.
[Mh] Termos MeSH primário: Neoplasias Experimentais/metabolismo
Neoplasias Experimentais/patologia
Neurofibromina 2/metabolismo
Neurofibromina 2/ultraestrutura
Fosfotransferases/metabolismo
Serina/metabolismo
Frações Subcelulares/metabolismo
[Mh] Termos MeSH secundário: Apoptose/genética
Linhagem Celular Tumoral
Proliferação Celular
Sobrevivência Celular/genética
Genes Supressores de Tumor
Seres Humanos
Neoplasias Experimentais/genética
Neurofibromina 2/genética
Fosforilação
Conformação Proteica
Serina/genética
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Neurofibromin 2); 452VLY9402 (Serine); EC 2.7.- (Phosphotransferases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170919
[St] Status:MEDLINE


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[PMID]:28729415
[Au] Autor:Stepanova DS; Semenova G; Kuo YM; Andrews AJ; Ammoun S; Hanemann CO; Chernoff J
[Ad] Endereço:Pirogov Russian National Research Medical University, Moscow, Russia.
[Ti] Título:An Essential Role for the Tumor-Suppressor Merlin in Regulating Fatty Acid Synthesis.
[So] Source:Cancer Res;77(18):5026-5038, 2017 Sep 15.
[Is] ISSN:1538-7445
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neurofibromatosis type 2 (NF2) is an autosomal dominant disorder characterized by the development of multiple tumors in the central nervous system, most notably schwannomas, and meningiomas. Mutational inactivation of the gene encoding the protein Merlin is found in most sporadic and inherited schwannomas, but the molecular mechanisms underlying neoplastic changes in schwannoma cells remain unclear. We report here that Nf2-deficient cells display elevated expression levels of key enzymes involved in lipogenesis and that this upregulation is caused by increased activity of Torc1. Inhibition or knockdown of fatty acid synthase (FASN), the enzyme that catalyzes the formation of palmitic acid from malonyl-CoA, drove -deficient cells into apoptosis. Treatment of -mutant cells with agents that inhibit the production of malonyl-CoA reduced their sensitivity to FASN inhibitors. Collectively, these results suggest that the altered lipid metabolism found in -mutant cells renders them sensitive to elevated levels of malonyl-CoA, as occurs following blockade of FASN, suggesting new targeted strategies in the treatment of -deficient tumors. .
[Mh] Termos MeSH primário: Biomarcadores Tumorais/metabolismo
Ácido Graxo Sintase Tipo I/metabolismo
Ácidos Graxos/metabolismo
Meningioma/patologia
Complexos Multiproteicos/metabolismo
Neurilemoma/patologia
Neurofibromina 2/metabolismo
Serina-Treonina Quinases TOR/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose
Biomarcadores Tumorais/genética
Proliferação Celular
Células Cultivadas
Embrião de Mamíferos/citologia
Embrião de Mamíferos/metabolismo
Ácido Graxo Sintase Tipo I/genética
Feminino
Fibroblastos/citologia
Fibroblastos/metabolismo
Seres Humanos
Lipogênese
Alvo Mecanístico do Complexo 1 de Rapamicina
Neoplasias Meníngeas/genética
Neoplasias Meníngeas/metabolismo
Neoplasias Meníngeas/patologia
Meningioma/genética
Meningioma/metabolismo
Camundongos
Camundongos Nus
Complexos Multiproteicos/genética
Neurilemoma/genética
Neurilemoma/metabolismo
Neurofibromina 2/genética
Ratos
Taxa de Sobrevida
Serina-Treonina Quinases TOR/genética
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Fatty Acids); 0 (Multiprotein Complexes); 0 (Neurofibromin 2); EC 2.3.1.85 (FASN protein, human); EC 2.3.1.85 (Fatty Acid Synthase, Type I); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 1)
[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:170722
[St] Status:MEDLINE
[do] DOI:10.1158/0008-5472.CAN-16-2834


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[PMID]:28553954
[Au] Autor:Kato T; Sato T; Yokoi K; Sekido Y
[Ad] Endereço:Division of Molecular Oncology, Aichi Cancer Center Research Institute, Nagoya, Japan.
[Ti] Título:E-cadherin expression is correlated with focal adhesion kinase inhibitor resistance in Merlin-negative malignant mesothelioma cells.
[So] Source:Oncogene;36(39):5522-5531, 2017 Sep 28.
[Is] ISSN:1476-5594
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Malignant mesothelioma (MM) is an aggressive tumor commonly caused by asbestos exposure after a long latency. Focal adhesion kinase (FAK) inhibitors inhibit the cell growth of Merlin-deficient MM cells; however, their clinical efficacy has not been clearly determined. The aim of this study was to evaluate the growth inhibitory effect of the FAK inhibitor VS-4718 on MM cell lines and identify biomarkers for its efficacy. Although most Merlin-deficient cell lines were sensitive to VS-4718 compared with control MeT-5A cells, a subset of these cell lines exhibited resistance to this drug. Microarray and qRT-PCR analyses using RNA isolated from Merlin-deficient MM cell lines revealed a significant correlation between E-cadherin mRNA levels and VS-4718 resistance. Merlin- and E-cadherin-negative Y-MESO-22 cells underwent apoptosis upon treatment with a low concentration of VS-4718, whereas Merlin-negative, E-cadherin-positive Y-MESO-9 cells did not undergo VS-4718-induced apoptosis. Furthermore, E-cadherin knockdown in Merlin-negative MM cells significantly sensitized cells to VS-4718 and induced apoptotic cell death upon VS-4718 treatment. Together, our results suggest that E-cadherin serves as a predictive biomarker for molecular target therapy with FAK inhibitors for patients with mesothelioma and that its expression endows MM cells with resistance to FAK inhibitors.
[Mh] Termos MeSH primário: Caderinas/biossíntese
Quinase 1 de Adesão Focal/antagonistas & inibidores
Neoplasias Pulmonares/tratamento farmacológico
Neoplasias Pulmonares/metabolismo
Mesotelioma/tratamento farmacológico
Mesotelioma/metabolismo
Neurofibromina 2/deficiência
Inibidores de Proteínas Quinases/farmacologia
[Mh] Termos MeSH secundário: Apoptose/efeitos dos fármacos
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Resistência a Medicamentos Antineoplásicos
Expressão Gênica
Seres Humanos
Neoplasias Pulmonares/patologia
Mesotelioma/patologia
Neurofibromina 2/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CDH1 protein, human); 0 (Cadherins); 0 (Neurofibromin 2); 0 (Protein Kinase Inhibitors); EC 2.7.10.2 (Focal Adhesion Kinase 1); EC 2.7.10.2 (PTK2 protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170530
[St] Status:MEDLINE
[do] DOI:10.1038/onc.2017.147


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[PMID]:28407626
[Au] Autor:Seo HH; Lee SY; Lee CY; Kim R; Kim P; Oh S; Lee H; Lee MY; Kim J; Kim LK; Hwang KC; Chang W
[Ad] Endereço:Brain Korea 21 PLUS Project for Medical Science, Yonsei University College of Medicine, Seoul, Republic of Korea.
[Ti] Título:Exogenous miRNA-146a Enhances the Therapeutic Efficacy of Human Mesenchymal Stem Cells by Increasing Vascular Endothelial Growth Factor Secretion in the Ischemia/Reperfusion-Injured Heart.
[So] Source:J Vasc Res;54(2):100-108, 2017.
[Is] ISSN:1423-0135
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Adult stem cells have been studied as a promising therapeutic modality for the functional restoration of the damaged heart. In the present study, a strategy for enhancing the angiogenic efficacy of human mesenchymal stem cells (hMSCs) using micro-RNA was examined. We investigated whether micro-RNA-146a (miR-146a) influences the secretion of vascular endothelial growth factor (VEGF) and angiogenesis of MSCs. Our data indicated that miR-146a-transfected hMSCs (hMSCmiR-146a) decreased the expression of neurofibromin 2, an inhibitor of p21-activated kinase-1 (PAK1). miR-146a also increased the expression of Ras-related C3 botulinum toxin substrate 1 and PAK1, which are known to induce VEGF expression, and the formation of vascular branches was increased in hMSCmiR-146a compared to hMSCs treated with VEGF. VEGF and p-Akt were increased in hMSCmiR-146a. Furthermore, injection of hMSCmiR-146a after ischemia/reperfusion (I/R) injury led to a reduction of fibrosis area and increased VEGF expression, confirming the regenerative capacity such as reparative angiogenesis in the infarcted area. Cardiac functions in I/R injury were improved following injection of hMSCmiR-146a compared to the I/R group. Taken together, these data suggest that miR-146 is a novel microRNA that regulates VEGF expression, and its use may be an effective strategy for enhancing the therapeutic efficacy of hMSC transplantation into the I/R-injured heart.
[Mh] Termos MeSH primário: Transplante de Células-Tronco Mesenquimais
Células Mesenquimais Estromais/metabolismo
MicroRNAs/metabolismo
Infarto do Miocárdio/cirurgia
Traumatismo por Reperfusão Miocárdica/cirurgia
Miocárdio/metabolismo
Fator A de Crescimento do Endotélio Vascular/metabolismo
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Animais
Sítios de Ligação
Células Cultivadas
Modelos Animais de Doenças
Fibrose
Seres Humanos
Masculino
Células Mesenquimais Estromais/secreção
MicroRNAs/genética
Infarto do Miocárdio/genética
Infarto do Miocárdio/metabolismo
Infarto do Miocárdio/patologia
Traumatismo por Reperfusão Miocárdica/genética
Traumatismo por Reperfusão Miocárdica/metabolismo
Traumatismo por Reperfusão Miocárdica/patologia
Miocárdio/patologia
Neovascularização Fisiológica
Neurofibromina 2/genética
Neurofibromina 2/metabolismo
Ratos Sprague-Dawley
Recuperação de Função Fisiológica
Regeneração
Transdução de Sinais
Transfecção
Regulação para Cima
Fator A de Crescimento do Endotélio Vascular/genética
Fator A de Crescimento do Endotélio Vascular/secreção
Quinases Ativadas por p21/metabolismo
Proteínas rac de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (MIRN146 microRNA, human); 0 (MicroRNAs); 0 (Neurofibromin 2); 0 (VEGFA protein, human); 0 (Vascular Endothelial Growth Factor A); EC 2.7.11.1 (PAK1 protein, human); EC 2.7.11.1 (p21-Activated Kinases); EC 3.6.5.2 (rac GTP-Binding Proteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170619
[Lr] Data última revisão:
170619
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170414
[St] Status:MEDLINE
[do] DOI:10.1159/000461596


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[PMID]:28314689
[Au] Autor:Sahm F; Schrimpf D; Stichel D; Jones DTW; Hielscher T; Schefzyk S; Okonechnikov K; Koelsche C; Reuss DE; Capper D; Sturm D; Wirsching HG; Berghoff AS; Baumgarten P; Kratz A; Huang K; Wefers AK; Hovestadt V; Sill M; Ellis HP; Kurian KM; Okuducu AF; Jungk C; Drueschler K; Schick M; Bewerunge-Hudler M; Mawrin C; Seiz-Rosenhagen M; Ketter R; Simon M; Westphal M; Lamszus K; Becker A; Koch A; Schittenhelm J; Rushing EJ; Collins VP; Brehmer S; Chavez L; Platten M; Hänggi D; Unterberg A; Paulus W; Wick W; Pfister SM; Mittelbronn M; Preusser M; Herold-Mende C; Weller M; von Deimling A
[Ad] Endereço:Department of Neuropathology, Institute of Pathology, Ruprecht-Karls-University Heidelberg, Heidelberg, Germany; Clinical Cooperation Unit Neuropathology, German Cancer Research Center (DKFZ), Heidelberg, Germany.
[Ti] Título:DNA methylation-based classification and grading system for meningioma: a multicentre, retrospective analysis.
[So] Source:Lancet Oncol;18(5):682-694, 2017 May.
[Is] ISSN:1474-5488
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The WHO classification of brain tumours describes 15 subtypes of meningioma. Nine of these subtypes are allotted to WHO grade I, and three each to grade II and grade III. Grading is based solely on histology, with an absence of molecular markers. Although the existing classification and grading approach is of prognostic value, it harbours shortcomings such as ill-defined parameters for subtypes and grading criteria prone to arbitrary judgment. In this study, we aimed for a comprehensive characterisation of the entire molecular genetic landscape of meningioma to identify biologically and clinically relevant subgroups. METHODS: In this multicentre, retrospective analysis, we investigated genome-wide DNA methylation patterns of meningiomas from ten European academic neuro-oncology centres to identify distinct methylation classes of meningiomas. The methylation classes were further characterised by DNA copy number analysis, mutational profiling, and RNA sequencing. Methylation classes were analysed for progression-free survival outcomes by the Kaplan-Meier method. The DNA methylation-based and WHO classification schema were compared using the Brier prediction score, analysed in an independent cohort with WHO grading, progression-free survival, and disease-specific survival data available, collected at the Medical University Vienna (Vienna, Austria), assessing methylation patterns with an alternative methylation chip. FINDINGS: We retrospectively collected 497 meningiomas along with 309 samples of other extra-axial skull tumours that might histologically mimic meningioma variants. Unsupervised clustering of DNA methylation data clearly segregated all meningiomas from other skull tumours. We generated genome-wide DNA methylation profiles from all 497 meningioma samples. DNA methylation profiling distinguished six distinct clinically relevant methylation classes associated with typical mutational, cytogenetic, and gene expression patterns. Compared with WHO grading, classification by individual and combined methylation classes more accurately identifies patients at high risk of disease progression in tumours with WHO grade I histology, and patients at lower risk of recurrence among WHO grade II tumours (p=0·0096) from the Brier prediction test). We validated this finding in our independent cohort of 140 patients with meningioma. INTERPRETATION: DNA methylation-based meningioma classification captures clinically more homogenous groups and has a higher power for predicting tumour recurrence and prognosis than the WHO classification. The approach presented here is potentially very useful for stratifying meningioma patients to observation-only or adjuvant treatment groups. We consider methylation-based tumour classification highly relevant for the future diagnosis and treatment of meningioma. FUNDING: German Cancer Aid, Else Kröner-Fresenius Foundation, and DKFZ/Heidelberg Institute of Personalized Oncology/Precision Oncology Program.
[Mh] Termos MeSH primário: Metilação de DNA
Neoplasias Meníngeas/classificação
Neoplasias Meníngeas/genética
Meningioma/classificação
Meningioma/genética
Recidiva Local de Neoplasia/genética
[Mh] Termos MeSH secundário: Variações do Número de Cópias de DNA
Análise Mutacional de DNA
Proteínas de Ligação a DNA/genética
Progressão da Doença
Intervalo Livre de Doença
Feminino
Genoma
Seres Humanos
Fatores de Transcrição Kruppel-Like/genética
Masculino
Neoplasias Meníngeas/patologia
Meningioma/patologia
Gradação de Tumores
Recidiva Local de Neoplasia/patologia
Neurofibromina 2/genética
Proteínas Nucleares/genética
Proteínas Proto-Oncogênicas c-akt/genética
Estudos Retrospectivos
Análise de Sequência de RNA
Receptor Smoothened/genética
Taxa de Sobrevida
Fatores de Transcrição/genética
Transcriptoma
Peptídeos e Proteínas Associados a Receptores de Fatores de Necrose Tumoral/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; MULTICENTER STUDY
[Nm] Nome de substância:
0 (ARID1A protein, human); 0 (ARID1B protein, human); 0 (DNA-Binding Proteins); 0 (GKLF protein); 0 (Kruppel-Like Transcription Factors); 0 (Neurofibromin 2); 0 (Nuclear Proteins); 0 (SMO protein, human); 0 (Smoothened Receptor); 0 (TRAF7 protein, human); 0 (Transcription Factors); 0 (Tumor Necrosis Factor Receptor-Associated Peptides and Proteins); EC 2.7.11.1 (AKT1 protein, human); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170810
[Lr] Data última revisão:
170810
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170319
[St] Status:MEDLINE


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[PMID]:28292426
[Au] Autor:Su T; Ludwig MZ; Xu J; Fehon RG
[Ad] Endereço:Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL 60637, USA.
[Ti] Título:Kibra and Merlin Activate the Hippo Pathway Spatially Distinct from and Independent of Expanded.
[So] Source:Dev Cell;40(5):478-490.e3, 2017 Mar 13.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Hippo pathway is emerging as a key evolutionarily conserved signaling mechanism that controls organ size. Three membrane-associated proteins, Kibra, Merlin, and Expanded, regulate pathway activity, but the precise molecular mechanism by which they function is still poorly understood. Here we provide evidence that Merlin and Kibra activate Hippo signaling in parallel to Expanded at a spatially distinct cellular domain, the medial apical cortex. Merlin and Kibra together recruit the adapter protein Salvador, which in turn recruits the core kinase Hippo. In addition, we show that Crumbs has a dual effect on Hippo signaling. Crumbs promotes the ability of Expanded to activate the pathway but also sequesters Kibra to downregulate Hippo signaling. Together, our findings elucidate the mechanism of Hippo pathway activation by Merlin and Kibra, identify a subcellular domain for Hippo pathway regulation, and demonstrate differential activity of upstream regulators in different subcellular domains.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Drosophila melanogaster/citologia
Drosophila melanogaster/metabolismo
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Proteínas de Membrana/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Transdução de Sinais
Proteínas Supressoras de Tumor/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Ciclo Celular/metabolismo
Polaridade Celular
Proliferação Celular
Células Epiteliais/citologia
Células Epiteliais/metabolismo
Discos Imaginais/citologia
Modelos Biológicos
Neurofibromina 2
Asas de Animais/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (Drosophila Proteins); 0 (Intracellular Signaling Peptides and Proteins); 0 (Membrane Proteins); 0 (Neurofibromin 2); 0 (Tumor Suppressor Proteins); 0 (expanded protein, Drosophila); 0 (kibra protein, Drosophila); 0 (merlin, Drosophila); 0 (salvador protein, Drosophila); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (hpo protein, Drosophila)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170316
[St] Status:MEDLINE


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[PMID]:28285878
[Au] Autor:Blum W; Pecze L; Felley-Bosco E; Wu L; de Perrot M; Schwaller B
[Ad] Endereço:Unit of Anatomy, Department of Medicine, University of Fribourg, Route Albert-Gockel 1, 1700 Fribourg, Switzerland. Electronic address: walter-vincent.blum@unifr.ch.
[Ti] Título:Stem Cell Factor-Based Identification and Functional Properties of In Vitro-Selected Subpopulations of Malignant Mesothelioma Cells.
[So] Source:Stem Cell Reports;8(4):1005-1017, 2017 Apr 11.
[Is] ISSN:2213-6711
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Malignant mesothelioma (MM) is an aggressive neoplasm characterized by a poor patient survival rate, because of rapid tumor recurrence following first-line therapy. Cancer stem cells (CSCs) are assumed to be responsible for initiating tumorigenesis and driving relapse after therapeutic interventions. CSC-enriched MM cell subpopulations were identified by an OCT4/SOX2 reporter approach and were characterized by (1) increased resistance to cisplatin, (2) increased sensitivity toward the FAK inhibitor VS-6063 in vitro, and (3) a higher tumor-initiating capacity in vivo in orthotopic xenograft and allograft mouse models. Overexpression of NF2 (neurofibromatosis 2, merlin), a tumor suppressor often mutated or lost in MM, did not affect proliferation and viability of CSC-enriched MM populations but robustly decreased the viability of reporter-negative cells. In contrast, downregulation of calretinin strongly decreased proliferation and viability of both populations. In summary, we have enriched and characterized a small MM cell subpopulation that bears the expected CSC characteristics.
[Mh] Termos MeSH primário: Neoplasias Pulmonares/patologia
Pulmão/patologia
Mesotelioma/patologia
Células-Tronco Neoplásicas/patologia
Fator de Células-Tronco/análise
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/farmacologia
Calbindina 2/análise
Proliferação Celular
Cisplatino/farmacologia
Resistência a Medicamentos Antineoplásicos
Seres Humanos
Pulmão/efeitos dos fármacos
Neoplasias Pulmonares/tratamento farmacológico
Mesotelioma/tratamento farmacológico
Camundongos
Células-Tronco Neoplásicas/efeitos dos fármacos
Neurofibromina 2/análise
Fator 3 de Transcrição de Octâmero/análise
Fatores de Transcrição SOXB1/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Calbindin 2); 0 (Neurofibromin 2); 0 (Octamer Transcription Factor-3); 0 (SOXB1 Transcription Factors); 0 (Stem Cell Factor); Q20Q21Q62J (Cisplatin)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170516
[Lr] Data última revisão:
170516
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170314
[St] Status:MEDLINE


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[PMID]:28177878
[Au] Autor:Tang M; Wei H; Han L; Deng J; Wang Y; Yang M; Tang Y; Guo G; Zhou L; Tong A
[Ad] Endereço:The State Key Laboratory of Biotherapy and Cancer Center/Collaborative Innovation Center of Biotherapy, West China Hospital, West China Medical School, Sichuan University, Chengdu 610041, China.
[Ti] Título:Whole-genome sequencing identifies new genetic alterations in meningiomas.
[So] Source:Oncotarget;8(10):17070-17080, 2017 Mar 07.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The major known genetic contributor to meningioma formation was NF2, which is disrupted by mutation or loss in about 50% of tumors. Besides NF2, several recurrent driver mutations were recently uncovered through next-generation sequencing. Here, we performed whole-genome sequencing across 7 tumor-normal pairs to identify somatic genetic alterations in meningioma. As a result, Chromatin regulators, including multiple histone members, histone-modifying enzymes and several epigenetic regulators, are the major category among all of the identified copy number variants and single nucleotide variants. Notably, all samples contained copy number variants in histone members. Recurrent chromosomal rearrangements were detected on chromosome 22q, 6p21-p22 and 1q21, and most of the histone copy number variants occurred in these regions. These results will help to define the genetic landscape of meningioma and facilitate more effective genomics-guided personalized therapy.
[Mh] Termos MeSH primário: Genoma Humano/genética
Sequenciamento de Nucleotídeos em Larga Escala/métodos
Neoplasias Meníngeas/genética
Meningioma/genética
Mutação
[Mh] Termos MeSH secundário: Aberrações Cromossômicas
Cromossomos Humanos Par 1/genética
Cromossomos Humanos Par 22/genética
Cromossomos Humanos Par 6/genética
Variações do Número de Cópias de DNA
Rearranjo Gênico
Redes Reguladoras de Genes
Seres Humanos
Neurofibromina 2/genética
Polimorfismo de Nucleotídeo Único
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Neurofibromin 2)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170801
[Lr] Data última revisão:
170801
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170209
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15043


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[PMID]:28137778
[Au] Autor:Mindos T; Dun XP; North K; Doddrell RD; Schulz A; Edwards P; Russell J; Gray B; Roberts SL; Shivane A; Mortimer G; Pirie M; Zhang N; Pan D; Morrison H; Parkinson DB
[Ad] Endereço:Plymouth University Peninsula Schools of Medicine and Dentistry, Plymouth PL6 8BU, England, UK.
[Ti] Título:Merlin controls the repair capacity of Schwann cells after injury by regulating Hippo/YAP activity.
[So] Source:J Cell Biol;216(2):495-510, 2017 Feb.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Loss of the Merlin tumor suppressor and activation of the Hippo signaling pathway play major roles in the control of cell proliferation and tumorigenesis. We have identified completely novel roles for Merlin and the Hippo pathway effector Yes-associated protein (YAP) in the control of Schwann cell (SC) plasticity and peripheral nerve repair after injury. Injury to the peripheral nervous system (PNS) causes a dramatic shift in SC molecular phenotype and the generation of repair-competent SCs, which direct functional repair. We find that loss of Merlin in these cells causes a catastrophic failure of axonal regeneration and remyelination in the PNS. This effect is mediated by activation of YAP expression in Merlin-null SCs, and loss of YAP restores axonal regrowth and functional repair. This work identifies new mechanisms that control the regenerative potential of SCs and gives new insight into understanding the correct control of functional nerve repair in the PNS.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Proliferação Celular
Lesões por Esmagamento/metabolismo
Regeneração Nervosa
Neurofibromina 2/metabolismo
Fosfoproteínas/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Células de Schwann/metabolismo
Nervo Isquiático/metabolismo
Neuropatia Ciática/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/deficiência
Proteínas Adaptadoras de Transdução de Sinal/genética
Animais
Axônios/metabolismo
Axônios/patologia
Lesões por Esmagamento/genética
Lesões por Esmagamento/patologia
Lesões por Esmagamento/fisiopatologia
Modelos Animais de Doenças
Feminino
Genótipo
Masculino
Camundongos Knockout
Proteínas Quinases Ativadas por Mitógeno/metabolismo
Atividade Motora
Bainha de Mielina/metabolismo
Fatores de Crescimento Neural/metabolismo
Neurofibromina 2/deficiência
Neurofibromina 2/genética
Plasticidade Neuronal
Fenótipo
Fosfoproteínas/deficiência
Fosfoproteínas/genética
Proteínas Proto-Oncogênicas c-jun/metabolismo
Recuperação de Função Fisiológica
Células de Schwann/patologia
Nervo Isquiático/lesões
Nervo Isquiático/patologia
Nervo Isquiático/fisiopatologia
Neuropatia Ciática/genética
Neuropatia Ciática/patologia
Neuropatia Ciática/fisiopatologia
Transdução de Sinais
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Nerve Growth Factors); 0 (Neurofibromin 2); 0 (Phosphoproteins); 0 (Proto-Oncogene Proteins c-jun); 0 (Yap protein, mouse); EC 2.7.11.1 (Hippo protein, mouse); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170201
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201606052



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