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Pesquisa : D12.776.660.650.875.500 [Categoria DeCS]
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[PMID]:29197877
[Au] Autor:Gerbino A; Bottillo I; Milano S; Lipari M; Zio R; Morlino S; Mola MG; Procino G; Re F; Zachara E; Grammatico P; Svelto M; Carmosino M
[Ad] Endereço:Department of Biosciences, Biotechnologies and Biopharmaceutics, University of Bari, Bari, Italy.
[Ti] Título:Functional Characterization of a Novel Truncating Mutation in Lamin A/C Gene in a Family with a Severe Cardiomyopathy with Conduction Defects.
[So] Source:Cell Physiol Biochem;44(4):1559-1577, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: Truncating LMNA gene mutations occur in many inherited cardiomyopathy cases, but the molecular mechanisms involved in the disease they cause have not yet been systematically investigated. Here, we studied a novel frameshift LMNA variant (p.D243Gfs*4) identified in three members of an Italian family co-segregating with a severe form of cardiomyopathy with conduction defects. METHODS: HEK293 cells and HL-1 cardiomyocytes were transiently transfected with either Lamin A or D243Gfs*4 tagged with GFP (or mCherry). D243Gfs*4 expression, cellular localization and its effects on diverse cellular mechanisms were evaluated with western blotting, laser-scanning confocal microscopy and video-imaging analysis in single cells. RESULTS: When expressed in HEK293 cells, GFP- (or mCherry)-tagged LMNA D243Gfs*4 colocalized with calnexin within the ER. ER mislocalization of LMNA D243Gfs*4 did not significantly induce ER stress response, abnormal Ca2+ handling and apoptosis when compared with HEK293 cells expressing another truncated mutant of LMNA (R321X) which similarly accumulates within the ER. Of note, HEK293-LMNA D243Gfs*4 cells showed a significant reduction of connexin 43 (CX43) expression level, which was completely rescued by activation of the WNT/ß-catenin signaling pathway. When expressed in HL-1 cardiomyocytes, D243Gfs*4 significantly impaired the spontaneous Ca2+ oscillations recorded in these cells as result of propagation of the depolarizing waves through the gap junctions between non-transfected cells surrounding a cell harboring the mutation. Furthermore, mCh-D243Gfs*4 HL-1 cardiomyocytes showed reduced CX43-dependent Lucifer Yellow (LY) loading and propagation. Of note, activation of ß-catenin rescued both LY loading and LMNA D243Gfs*4 -HL-1 cells spontaneous activity propagation. CONCLUSION: Overall, the present results clearly indicate the involvement of the aberrant CX43 expression/activity as a pathogenic mechanism for the conduction defects associated to this LMNA truncating alteration.
[Mh] Termos MeSH primário: Doença do Sistema de Condução Cardíaco/genética
Cardiomiopatias/genética
Lamina Tipo A/genética
[Mh] Termos MeSH secundário: Apoptose
Sequência de Bases
Cálcio/metabolismo
Calnexina/metabolismo
Doença do Sistema de Condução Cardíaco/complicações
Doença do Sistema de Condução Cardíaco/patologia
Cardiomiopatias/complicações
Cardiomiopatias/patologia
Linhagem Celular
Conexina 43
Retículo Endoplasmático/metabolismo
Feminino
Junções Comunicantes/metabolismo
Células HEK293
Seres Humanos
Lamina Tipo A/metabolismo
Repetições de Microssatélites/genética
Microscopia Confocal
Meia-Idade
Mutagênese Sítio-Dirigida
Miócitos Cardíacos/citologia
Miócitos Cardíacos/metabolismo
Linhagem
Polimorfismo de Nucleotídeo Único
Imagem com Lapso de Tempo
Via de Sinalização Wnt
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Connexin 43); 0 (LMNA protein, human); 0 (Lamin Type A); 139873-08-8 (Calnexin); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171204
[St] Status:MEDLINE
[do] DOI:10.1159/000485651


  2 / 1715 MEDLINE  
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[PMID]:29191657
[Au] Autor:Shiozawa K; Shuting J; Yoshioka Y; Ochiya T; Kondo T
[Ad] Endereço:Division of Rare Cancer Research, National Cancer Center Research Institute, Tokyo, Japan, 5-1-1 Tsukiji, Chuo-ku, Tokyo 104-0045, Japan. Electronic address: kshiozaw@ncc.go.jp.
[Ti] Título:Extracellular vesicle-encapsulated microRNA-761 enhances pazopanib resistance in synovial sarcoma.
[So] Source:Biochem Biophys Res Commun;495(1):1322-1327, 2018 01 01.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The development of drug resistance in tumor cells leads to relapse and distant metastasis. Secreted microRNAs (miRNAs) enclosed in extracellular vesicles (EVs) can act as intercellular messengers. The objective of our study was to elucidate the role of secreted miRNAs to better understand the regulatory network underlying pazopanib-resistance in synovial sarcoma cells. We performed a comprehensive analysis of secreted miRNA abundance in pazopanib treated/untreated synovial sarcoma cells from four different cell lines (SYO-1, HS-SYII, 1273/99, and YaFuSS) using microarray technology, and discovered miR-761 in EVs as a potential biomarker of pazopanib-resistance in synovial sarcoma. Furthermore, we showed that miR-761 putatively targeted three proteins, thyroid hormone receptor interactor 6 (TRIP6), lamin A/C (LMNA), and NAD-dependent protein deacetylase sirtuin-3 (SIRT3). Knockdown of any of these proteins was shown in previous studies to confer increased resistance to chemotherapeutic agents. Our findings provide new insight into the potential role of miR-761, an EV-secreted miRNA from synovial sarcoma cells, making it a potential candidate for use in sarcoma therapy in the future.
[Mh] Termos MeSH primário: Resistência a Medicamentos Antineoplásicos
Vesículas Extracelulares/metabolismo
MicroRNAs/metabolismo
Pirimidinas/administração & dosagem
Sarcoma Sinovial/tratamento farmacológico
Sarcoma Sinovial/metabolismo
Sulfonamidas/administração & dosagem
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Antineoplásicos/administração & dosagem
Apoptose/efeitos dos fármacos
Linhagem Celular Tumoral
Seres Humanos
Proteínas com Domínio LIM/metabolismo
Lamina Tipo A/metabolismo
Sarcoma Sinovial/patologia
Sirtuína 3/metabolismo
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Antineoplastic Agents); 0 (LIM Domain Proteins); 0 (LMNA protein, human); 0 (Lamin Type A); 0 (MicroRNAs); 0 (Pyrimidines); 0 (Sulfonamides); 0 (TRIP6 protein, human); 0 (Transcription Factors); 0 (microRNA761 microRNA, human); 7RN5DR86CK (pazopanib); EC 3.5.1.- (SIRT3 protein, human); EC 3.5.1.- (Sirtuin 3)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171202
[St] Status:MEDLINE


  3 / 1715 MEDLINE  
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[PMID]:29047356
[Au] Autor:Marian AJ
[Ad] Endereço:Center for Cardiovascular Genetics, Institute of Molecular Medicine, University of Texas Health Sciences Center at Houston, 6770 Bertner Street, DAC900, Houston, TX, 77030, USA. Ali.J.Marian@uth.tmc.edu.
[Ti] Título:Non-syndromic cardiac progeria in a patient with the rare pathogenic p.Asp300Asn variant in the LMNA gene.
[So] Source:BMC Med Genet;18(1):116, 2017 Oct 18.
[Is] ISSN:1471-2350
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Mutations in LMNA gene, encoding Lamin A/C, cause a diverse array of phenotypes, collectively referred to as laminopathies. The most common manifestation is dilated cardiomyopathy (DCM), occurring in conjunction with variable skeletal muscle involvement but without involvement of the coronary arteries. Much less commonly, LMNA mutations cause progeroid syndromes, whereby an early-onset coronary artery disease (CAD) is the hallmark of the disease. We report a hitherto unreported compound cardiac phenotype, dubbed as "non-syndromic cardiac progeria", in a young patient who carried a rare pathogenic variant in the LMNA gene and developed progressive degeneration of various cardiac structures, as seen in the elderly. The phenotype resembled the progeroid syndromes, except that it was restricted to the heart and did not involve other organs. CASE PRESENTATION: The patient was a well-developed Caucasian female who presented at age 29 years with an acute myocardial infarction (MI) and was found to have extensive CAD. She had none of the conventional risk factors for atherosclerosis. She underwent coronary artery bypass surgery but continued to require multiple percutaneous coronary interventions for symptomatic obstructive coronary lesions. During the course of next 10 years, she developed mitral regurgitation, degenerative mitral and aortic valve diseases, atrial flutter, and progressive conduction defects. She died from progressive heart failure with predominant involvement of the right ventricle and severe tricuspid regurgitation. Cardiac phenotype in this young patient resembled degenerative cardiac diseases of the elderly and the progeroid syndromes. However, in contrast to the progeroid syndromes, the phenotype was restricted to the heart and did not involve other organs. Thus, the phenotype was dubbed as a non-syndromic cardiac progeria. Genetic screening of several cardiomyopathy genes, including LMNA, which is a causal gene for progeroid syndromes, led to identification of a very rare pathogenic p.Asp300Asn variant in the LMNA gene. CONCLUSIONS: We infer that the LMNA p.Asp300Asn mutation is pathogenic in non-syndromic cardiac progeria. Mutations involving codon 300 in the LMNA gene have been associated with progeroid syndromes involving multiple organs. Collectively, the data provide credence to the causal role of p.Asp300Asn mutation in the pathogenesis of non-syndromic cardiac progeria.
[Mh] Termos MeSH primário: Lamina Tipo A/genética
Mutação de Sentido Incorreto
Progéria/genética
[Mh] Termos MeSH secundário: Adulto
Sequência de Aminoácidos
Asparagina/genética
Ácido Aspártico/genética
Sequência de Bases
Doença da Artéria Coronariana/diagnóstico
Doença da Artéria Coronariana/genética
Doença da Artéria Coronariana/fisiopatologia
Ecocardiografia/métodos
Eletrocardiografia/métodos
Evolução Fatal
Feminino
Seres Humanos
Infarto do Miocárdio/diagnóstico
Infarto do Miocárdio/genética
Infarto do Miocárdio/fisiopatologia
Linhagem
Progéria/diagnóstico
Progéria/fisiopatologia
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (LMNA protein, human); 0 (Lamin Type A); 30KYC7MIAI (Aspartic Acid); 7006-34-0 (Asparagine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171020
[St] Status:MEDLINE
[do] DOI:10.1186/s12881-017-0480-x


  4 / 1715 MEDLINE  
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[PMID]:28892082
[Au] Autor:Roman W; Martins JP; Carvalho FA; Voituriez R; Abella JVG; Santos NC; Cadot B; Way M; Gomes ER
[Ad] Endereço:Sorbonne Universités, UPMC Univ Paris 06, INSERM UMRS974, CNRS FRE3617, Center for Research in Myology, GH Pitié-Salpêtrière, 47 Boulevard de l'Hôpital, 75013 Paris, France.
[Ti] Título:Myofibril contraction and crosslinking drive nuclear movement to the periphery of skeletal muscle.
[So] Source:Nat Cell Biol;19(10):1189-1201, 2017 Oct.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Nuclear movements are important for multiple cellular functions, and are driven by polarized forces generated by motor proteins and the cytoskeleton. During skeletal myofibre formation or regeneration, nuclei move from the centre to the periphery of the myofibre for proper muscle function. Centrally located nuclei are also found in different muscle disorders. Using theoretical and experimental approaches, we demonstrate that nuclear movement to the periphery of myofibres is mediated by centripetal forces around the nucleus. These forces arise from myofibril contraction and crosslinking that 'zip' around the nucleus in combination with tight regulation of nuclear stiffness by lamin A/C. In addition, an Arp2/3 complex containing Arpc5L together with γ-actin is required to organize desmin to crosslink myofibrils for nuclear movement. Our work reveals that centripetal forces exerted by myofibrils squeeze the nucleus to the periphery of myofibres.
[Mh] Termos MeSH primário: Núcleo Celular/fisiologia
Movimento
Contração Muscular
Músculo Esquelético/fisiologia
Miofibrilas/fisiologia
[Mh] Termos MeSH secundário: Complexo 2-3 de Proteínas Relacionadas à Actina/genética
Complexo 2-3 de Proteínas Relacionadas à Actina/metabolismo
Actinas/genética
Actinas/metabolismo
Animais
Animais Recém-Nascidos
Células Cultivadas
Lamina Tipo A/genética
Lamina Tipo A/metabolismo
Camundongos Endogâmicos C57BL
Microscopia de Fluorescência
Microscopia de Vídeo
Modelos Biológicos
Interferência de RNA
Fatores de Tempo
Imagem com Lapso de Tempo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE; VIDEO-AUDIO MEDIA
[Nm] Nome de substância:
0 (Actin-Related Protein 2-3 Complex); 0 (Actins); 0 (Arpc5 protein, mouse); 0 (Lamin Type A); 0 (Lmna protein, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171115
[Lr] Data última revisão:
171115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170912
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3605


  5 / 1715 MEDLINE  
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[PMID]:28811278
[Au] Autor:Elzeneini E; Wickström SA
[Ad] Endereço:Paul Gerson Unna Group, Skin Homeostasis and Ageing, Max Planck Institute for Biology of Ageing, Cologne, Germany.
[Ti] Título:Lipodystrophic laminopathy: Lamin A mutation relaxes chromatin architecture to impair adipogenesis.
[So] Source:J Cell Biol;216(9):2607-2610, 2017 Sep 04.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The familial partial Dunnigan lipodystrophy, characterized by subcutaneous fat loss, is frequently caused by an R482W mutation in lamin A. In this issue, Oldenburg et al. (2017. https://doi.org/10.1083/jcb.201701043) demonstrate that this mutation impairs the ability of lamin A to repress the anti-adipogenic miR-335, providing a potential molecular mechanism for the disease.
[Mh] Termos MeSH primário: Cromatina
Lamina Tipo A/genética
[Mh] Termos MeSH secundário: Adipogenia
Lipodistrofia Parcial Familiar/genética
Mutação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (Lamin Type A)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170817
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201707090


  6 / 1715 MEDLINE  
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[PMID]:28806747
[Au] Autor:Kaspi E; Frankel D; Guinde J; Perrin S; Laroumagne S; Robaglia-Schlupp A; Ostacolo K; Harhouri K; Tazi-Mezalek R; Micallef J; Dutau H; Tomasini P; De Sandre-Giovannoli A; Lévy N; Cau P; Astoul P; Roll P
[Ad] Endereço:Aix Marseille Univ, INSERM, GMGF, Marseille, France.
[Ti] Título:Low lamin A expression in lung adenocarcinoma cells from pleural effusions is a pejorative factor associated with high number of metastatic sites and poor Performance status.
[So] Source:PLoS One;12(8):e0183136, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The type V intermediate filament lamins are the principal components of the nuclear matrix, including the nuclear lamina. Lamins are divided into A-type and B-type, which are encoded by three genes, LMNA, LMNB1, and LMNB2. The alternative splicing of LMNA produces two major A-type lamins, lamin A and lamin C. Previous studies have suggested that lamins are involved in cancer development and progression. A-type lamins have been proposed as biomarkers for cancer diagnosis, prognosis, and/or follow-up. The aim of the present study was to investigate lamins in cancer cells from metastatic pleural effusions using immunofluorescence, western blotting, and flow cytometry. In a sub-group of lung adenocarcinomas, we found reduced expression of lamin A but not of lamin C. The reduction in lamin A expression was correlated with the loss of epithelial membrane antigen (EMA)/MUC-1, an epithelial marker that is involved in the epithelial to mesenchymal transition (EMT). Finally, the lamin A expression was inversely correlated with the number of metastatic sites and the WHO Performance status, and association of pleural, bone and lung metastatic localizations was more frequent when lamin A expression was reduced. In conclusion, low lamin A but not lamin C expression in pleural metastatic cells could represent a major actor in the development of metastasis, associated with EMT and could account for a pejorative factor correlated with a poor Performance status.
[Mh] Termos MeSH primário: Adenocarcinoma/metabolismo
Adenocarcinoma/patologia
Lamina Tipo A/metabolismo
Neoplasias Pulmonares/metabolismo
Neoplasias Pulmonares/patologia
Derrame Pleural/metabolismo
Derrame Pleural/patologia
[Mh] Termos MeSH secundário: Idoso
Idoso de 80 Anos ou mais
Feminino
Citometria de Fluxo
Imunofluorescência
Seres Humanos
Masculino
Meia-Idade
Mucina-1/metabolismo
Metástase Neoplásica
Organização Mundial da Saúde
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lamin Type A); 0 (Mucin-1); 0 (lamin C)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170815
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183136


  7 / 1715 MEDLINE  
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[PMID]:28797100
[Au] Autor:Tao Y; Fang P; Kim S; Guo M; Young NL; Marshall AG
[Ad] Endereço:Department of Chemistry and Biochemistry, Florida State University, Tallahassee, Florida, United States of America.
[Ti] Título:Mapping the contact surfaces in the Lamin A:AIMP3 complex by hydrogen/deuterium exchange FT-ICR mass spectrometry.
[So] Source:PLoS One;12(8):e0181869, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Aminoacyl-tRNA synthetases-interacting multifunctional protein3 (AIMP3/p18) is involved in the macromolecular tRNA synthetase complex via its interaction with several aminoacyl-tRNA synthetases. Recent reports reveal a novel function of AIMP3 as a tumor suppressor by accelerating cellular senescence and causing defects in nuclear morphology. AIMP3 specifically mediates degradation of mature Lamin A (LmnA), a major component of the nuclear envelope matrix; however, the mechanism of how AIMP3 interacts with LmnA is unclear. Here we report solution-phase hydrogen/deuterium exchange (HDX) for AIMP3, LmnA, and AIMP3 in association with the LmnA C-terminus. Reversed-phase LC coupled with LTQ 14.5 T Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) results in high mass accuracy and resolving power for comparing the D-uptake profiles for AIMP3, LmnA, and their complex. The results show that the AIMP3-LmnA interaction involves one of the two putative binding sites and an adjacent novel interface on AIMP3. LmnA binds AIMP3 via its extreme C-terminus. Together these findings provide a structural insight for understanding the interaction between AIMP3 and LmnA in AIMP3 degradation.
[Mh] Termos MeSH primário: Lamina Tipo A/metabolismo
Fatores de Alongamento de Peptídeos/metabolismo
Proteínas Supressoras de Tumor/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Medição da Troca de Deutério/métodos
Seres Humanos
Lamina Tipo A/química
Espectrometria de Massas/métodos
Simulação de Acoplamento Molecular
Fatores de Alongamento de Peptídeos/química
Ligação Proteica
Mapeamento de Interação de Proteínas
Mapas de Interação de Proteínas
Proteólise
Proteínas Supressoras de Tumor/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (EEF1E1 protein, human); 0 (Lamin Type A); 0 (Peptide Elongation Factors); 0 (Tumor Suppressor Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170811
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181869


  8 / 1715 MEDLINE  
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[PMID]:28751304
[Au] Autor:Oldenburg A; Briand N; Sørensen AL; Cahyani I; Shah A; Moskaug JØ; Collas P
[Ad] Endereço:Department of Molecular Medicine, Institute of Basic Medical Sciences, Faculty of Medicine, University of Oslo, Oslo, Norway.
[Ti] Título:A lipodystrophy-causing lamin A mutant alters conformation and epigenetic regulation of the anti-adipogenic locus.
[So] Source:J Cell Biol;216(9):2731-2743, 2017 Sep 04.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mutations in the ( ) gene-encoding nuclear LMNA cause laminopathies, which include partial lipodystrophies associated with metabolic syndromes. The lipodystrophy-associated LMNA p.R482W mutation is known to impair adipogenic differentiation, but the mechanisms involved are unclear. We show in this study that the lamin A p.R482W hot spot mutation prevents adipogenic gene expression by epigenetically deregulating long-range enhancers of the anti-adipogenic microRNA gene in human adipocyte progenitor cells. The R482W mutation results in a loss of function of differentiation-dependent lamin A binding to the locus. This impairs H3K27 methylation and instead favors H3K27 acetylation on enhancers. The lamin A mutation further promotes spatial clustering of enhancer and promoter elements along with overexpression of the gene after adipogenic induction. Our results link a laminopathy-causing lamin A mutation to an unsuspected deregulation of chromatin states and spatial conformation of an miRNA locus critical for adipose progenitor cell fate.
[Mh] Termos MeSH primário: Adipócitos
Adipogenia/genética
Epigênese Genética
Fibroblastos
Lamina Tipo A/genética
Lipodistrofia Parcial Familiar/genética
MicroRNAs/genética
Mutação
Células-Tronco
[Mh] Termos MeSH secundário: Acetilação
Adipócitos/metabolismo
Adipócitos/patologia
Células Cultivadas
Cromatina/genética
Cromatina/metabolismo
Montagem e Desmontagem da Cromatina
Fibroblastos/metabolismo
Fibroblastos/patologia
Predisposição Genética para Doença
Histonas/metabolismo
Seres Humanos
Lamina Tipo A/metabolismo
Lipodistrofia Parcial Familiar/metabolismo
Lipodistrofia Parcial Familiar/patologia
Lipodistrofia Parcial Familiar/fisiopatologia
Metilação
MicroRNAs/química
MicroRNAs/metabolismo
Conformação de Ácido Nucleico
Fenótipo
Regiões Promotoras Genéticas
Células-Tronco/metabolismo
Células-Tronco/patologia
Relação Estrutura-Atividade
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (Histones); 0 (LMNA protein, human); 0 (Lamin Type A); 0 (MIRN335 microRNA, human); 0 (MicroRNAs)
[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:170729
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201701043


  9 / 1715 MEDLINE  
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[PMID]:28720531
[Au] Autor:Hou W; Cruz-Cosme R; Armstrong N; Obwolo LA; Wen F; Hu W; Luo MH; Tang Q
[Ad] Endereço:Department of Microbiology, Howard University College of Medicine, Seeley Mudd Building, 520 W Street, NW, Washington, DC 20059, United States.
[Ti] Título:Molecular cloning and characterization of the genes encoding the proteins of Zika virus.
[So] Source:Gene;628:117-128, 2017 Sep 10.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Zika virus (ZIKV) encodes a precursor protein (also called polyprotein) of about 3424 amino acids that is processed by proteases to generate 10 mature proteins and a small peptide. In the present study, we characterized the chemical features, suborganelle distribution and potential function of each protein using Flag-tagged protein expression system. Western blot analysis revealed the molecular weight of the proteins and the polymerization of E, NS1, and NS3 proteins. In addition, we performed multi-labeled fluorescent immunocytochemistry and subcellular fractionation to determine the subcellular localization of these proteins in host cells. We found that 1) the capsid protein colocalizes with 3 different cellular organelles: nucleoli, Golgi apparatus, and lipid droplet; NS2b and NS4a are associated with the Golgi apparatus; 2) the capsid and NS1proteins distribute in both cytoplasm and nucleus, NS5 is a nuclear protein; 3) NS3 protein colocalizes with tubulin and affects Lamin A; 4) Envelope, PrM, and NS2a proteins co-localize with the endoplasmic reticulum; 5) NS1 is associated with autophagosomes and NS4b is related to early endosome; 6) NS5 forms punctate structures in the nucleus that associate with splicing compartments shown by SC35, leading to reduction of SC35 protein level and trafficking of SC35 from the nucleus to the cytoplasm. These data suggest that ZIKV generates 10 functional viral proteins that exhibit distinctive subcellular distribution in host cells.
[Mh] Termos MeSH primário: Proteínas Virais/genética
Zika virus/genética
[Mh] Termos MeSH secundário: Animais
Autofagia
Nucléolo Celular/virologia
Núcleo Celular/virologia
Cercopithecus aethiops
Clonagem Molecular
Citoplasma/virologia
Retículo Endoplasmático/virologia
Endossomos/virologia
Genes Virais
Vetores Genéticos
Complexo de Golgi/virologia
Células HEK293
Seres Humanos
Lamina Tipo A/metabolismo
Transfecção
Tubulina (Proteína)/metabolismo
Células Vero
Proteínas não Estruturais Virais/genética
Proteínas Virais/metabolismo
Proteínas Estruturais Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lamin Type A); 0 (Tubulin); 0 (Viral Nonstructural Proteins); 0 (Viral Proteins); 0 (Viral Structural Proteins)
[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:170720
[St] Status:MEDLINE


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[PMID]:28712764
[Au] Autor:Ferri G; Storti B; Bizzarri R
[Ad] Endereço:NEST, Scuola Normale Superiore and Istituto Nanoscienze-CNR, Piazza San Silvestro 12, 56127 Pisa, Italy; Center for Nanotechnology Innovation @ NEST, Istituto Italiano di Tecnologia, Piazza San Silvestro 12, 56127 Pisa, Italy.
[Ti] Título:Nucleocytoplasmic transport in cells with progerin-induced defective nuclear lamina.
[So] Source:Biophys Chem;229:77-83, 2017 Oct.
[Is] ISSN:1873-4200
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Recent data indicate that nuclear lamina (NL) plays a relevant role in many fundamental cellular functions. The peculiar role of NL in cells is dramatically demonstrated by the Hutchinson-Gilford progeria syndrome (HGPS), an inherited laminopathy that causes premature, rapid aging shortly after birth. In HGPS, a mutant form of Lamin A (progeria) leads to a dysmorphic NL structure, but how this perturbation is transduced into cellular changes is still largely unknown. Owing to the close structural relationship between NL and the Nuclear Pore Complex (NPC), in this work we test whether HGPS affects passive and active nucleo-cytoplasmic shuttling of cargoes by means of an established model based of fluorescence recovery after photobleaching. Our findings clearly demonstrate that dysmorphic NL is decoupled from the dynamic characteristics of passive and active transport towards and from the nucleus, as well as from the binding affinity of transport protein mediators.
[Mh] Termos MeSH primário: Lamina Tipo A/metabolismo
Lâmina Nuclear/metabolismo
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular
Linhagem Celular Tumoral
Recuperação de Fluorescência Após Fotodegradação
Seres Humanos
Lamina Tipo A/genética
Microscopia de Fluorescência
Modelos Biológicos
Progéria/metabolismo
Progéria/patologia
Precursores de Proteínas/genética
Precursores de Proteínas/metabolismo
Proteínas Recombinantes de Fusão/biossíntese
Proteínas Recombinantes de Fusão/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lamin Type A); 0 (Protein Precursors); 0 (Recombinant Fusion Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE



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