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Pesquisa : D12.776.157.725.452.750 [Categoria DeCS]
Referências encontradas : 323 [refinar]
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[PMID]:28817800
[Au] Autor:Mackenzie IR; Nicholson AM; Sarkar M; Messing J; Purice MD; Pottier C; Annu K; Baker M; Perkerson RB; Kurti A; Matchett BJ; Mittag T; Temirov J; Hsiung GR; Krieger C; Murray ME; Kato M; Fryer JD; Petrucelli L; Zinman L; Weintraub S; Mesulam M; Keith J; Zivkovic SA; Hirsch-Reinshagen V; Roos RP; Züchner S; Graff-Radford NR; Petersen RC; Caselli RJ; Wszolek ZK; Finger E; Lippa C; Lacomis D; Stewart H; Dickson DW; Kim HJ; Rogaeva E; Bigio E; Boylan KB; Taylor JP; Rademakers R
[Ad] Endereço:Department of Pathology and Laboratory Medicine, Vancouver Coastal Health and the University of British Colombia, Vancouver, BC V6T 2B5, Canada.
[Ti] Título:TIA1 Mutations in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia Promote Phase Separation and Alter Stress Granule Dynamics.
[So] Source:Neuron;95(4):808-816.e9, 2017 Aug 16.
[Is] ISSN:1097-4199
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are age-related neurodegenerative disorders with shared genetic etiologies and overlapping clinical and pathological features. Here we studied a novel ALS/FTD family and identified the P362L mutation in the low-complexity domain (LCD) of T cell-restricted intracellular antigen-1 (TIA1). Subsequent genetic association analyses showed an increased burden of TIA1 LCD mutations in ALS patients compared to controls (p = 8.7 × 10 ). Postmortem neuropathology of five TIA1 mutations carriers showed a consistent pathological signature with numerous round, hyaline, TAR DNA-binding protein 43 (TDP-43)-positive inclusions. TIA1 mutations significantly increased the propensity of TIA1 protein to undergo phase transition. In live cells, TIA1 mutations delayed stress granule (SG) disassembly and promoted the accumulation of non-dynamic SGs that harbored TDP-43. Moreover, TDP-43 in SGs became less mobile and insoluble. The identification of TIA1 mutations in ALS/FTD reinforces the importance of RNA metabolism and SG dynamics in ALS/FTD pathogenesis.
[Mh] Termos MeSH primário: Esclerose Amiotrófica Lateral/genética
Esclerose Amiotrófica Lateral/patologia
Demência Frontotemporal/genética
Demência Frontotemporal/patologia
Mutação/genética
Proteínas de Ligação a Poli(A)/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Proteínas de Ligação a DNA/metabolismo
Saúde da Família
Feminino
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Células HeLa
Ribonucleoproteína Nuclear Heterogênea A1
Ribonucleoproteínas Nucleares Heterogêneas Grupo A-B/metabolismo
Seres Humanos
Masculino
Microscopia Confocal
Meia-Idade
Proteína FUS de Ligação a RNA/metabolismo
Estresse Fisiológico/fisiologia
Antígeno-1 Intracelular de Células T
Fatores de Tempo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (FUS protein, human); 0 (Heterogeneous Nuclear Ribonucleoprotein A1); 0 (Heterogeneous-Nuclear Ribonucleoprotein Group A-B); 0 (Poly(A)-Binding Proteins); 0 (RNA-Binding Protein FUS); 0 (T-Cell Intracellular Antigen-1); 0 (TDP-43 protein, human); 0 (TIA1 protein, human); 147336-22-9 (Green Fluorescent Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170818
[St] Status:MEDLINE


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[PMID]:28630277
[Au] Autor:Carrascoso I; Alcalde J; Sánchez-Jiménez C; González-Sánchez P; Izquierdo JM
[Ad] Endereço:Centro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Científicas, Universidad Autónoma de Madrid, Madrid, Spain.
[Ti] Título:T-Cell Intracellular Antigens and Hu Antigen R Antagonistically Modulate Mitochondrial Activity and Dynamics by Regulating Optic Atrophy 1 Gene Expression.
[So] Source:Mol Cell Biol;37(17), 2017 Sep 01.
[Is] ISSN:1098-5549
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondria undergo frequent morphological changes to control their function. We show here that T-cell intracellular antigens (TIA1b/TIARb) and Hu antigen R (HuR) have antagonistic roles in mitochondrial function by modulating the expression of mitochondrial shaping proteins. Expression of TIA1b/TIARb alters the mitochondrial dynamic network by enhancing fission and clustering, which is accompanied by a decrease in respiration. In contrast, HuR expression promotes fusion and cristae remodeling and increases respiratory activity. Mechanistically, TIA proteins downregulate the expression of optic atrophy 1 (OPA1) protein via switching of the splicing patterns of OPA1 to facilitate the production of OPA1 variant 5 (OPA1v5). Conversely, HuR enhances the expression of OPA1 mRNA isoforms through increasing steady-state levels and targeting translational efficiency at the 3' untranslated region. Knockdown of TIA1/TIAR or HuR partially reversed the expression profile of OPA1, whereas knockdown of OPA1 or overexpression of OPA1v5 provoked mitochondrial clustering. Middle-term expression of TIA1b/TIARb triggers reactive oxygen species production and mitochondrial DNA damage, which is accompanied by mitophagy, autophagy, and apoptosis. In contrast, HuR expression promotes mitochondrion-dependent cell proliferation. Collectively, these results provide molecular insights into the antagonistic functions of TIA1b/TIARb and HuR in mitochondrial activity dynamics and suggest that their balance might contribute to mitochondrial physiopathology.
[Mh] Termos MeSH primário: Proteína Semelhante a ELAV 1/metabolismo
Expressão Gênica/fisiologia
Mitocôndrias/metabolismo
Membranas Mitocondriais/metabolismo
Atrofia Óptica Autossômica Dominante/genética
Atrofia Óptica Autossômica Dominante/metabolismo
Proteínas de Ligação a Poli(A)/metabolismo
[Mh] Termos MeSH secundário: Proliferação Celular
Citoplasma/metabolismo
GTP Fosfo-Hidrolases/metabolismo
Seres Humanos
Mitocôndrias/genética
Dinâmica Mitocondrial/genética
Proteínas Mitocondriais/genética
Proteínas Mitocondriais/metabolismo
RNA Mensageiro/genética
Antígeno-1 Intracelular de Células T
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ELAV-Like Protein 1); 0 (ELAVL1 protein, human); 0 (Mitochondrial Proteins); 0 (Poly(A)-Binding Proteins); 0 (RNA, Messenger); 0 (T-Cell Intracellular Antigen-1); 0 (TIA1 protein, human); EC 3.6.1.- (GTP Phosphohydrolases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170621
[St] Status:MEDLINE


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[PMID]:28298474
[Au] Autor:Motohashi H; Mukudai Y; Ito C; Kato K; Shimane T; Kondo S; Shirota T
[Ad] Endereço:Department of Oral and Maxillofacial Surgery, School of Dentistry, Showa University, 2-1-1 Kitasenzoku, Ota-ku, Tokyo 145-8515, Japan.
[Ti] Título:Tumor protein D52 expression is post-transcriptionally regulated by T-cell intercellular antigen (TIA) 1 and TIA-related protein via mRNA stability.
[So] Source:Biochem J;474(10):1669-1687, 2017 May 04.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Although tumor protein D52 (TPD52) family proteins were first identified nearly 20 years ago, their molecular regulatory mechanisms remain unclear. Therefore, we investigated the post-transcriptional regulation of TPD52 family genes. An RNA immunoprecipitation (RIP) assay showed the potential binding ability of TPD52 family mRNAs to several RNA-binding proteins, and an RNA degradation assay revealed that TPD52 is subject to more prominent post-transcriptional regulation than are TPD53 and TPD54. We subsequently focused on the 3'-untranslated region (3'-UTR) of TPD52 as a -acting element in post-transcriptional gene regulation. Several deletion mutants of the 3'-UTR of TPD52 mRNA were constructed and ligated to the 3'-end of a reporter green fluorescence protein gene. An RNA degradation assay revealed that a minimal -acting region, located in the 78-280 region of the 5'-proximal region of the 3'-UTR, stabilized the reporter mRNA. Biotin pull-down and RIP assays revealed specific binding of the region to T-cell intracellular antigen 1 (TIA-1) and TIA-1-related protein (TIAR). Knockdown of TIA-1/TIAR decreased not only the expression, but also the stability of TPD52 mRNA; it also decreased the expression and stability of the reporter gene ligated to the 3'-end of the 78-280 fragment. Stimulation of transforming growth factor-ß and epidermal growth factor decreased the binding ability of these factors, resulting in decreased mRNA stability. These results indicate that the 78-280 fragment and TIA-1/TIAR concordantly contribute to mRNA stability as a -acting element and -acting factor(s), respectively. Thus, we here report the specific interactions between these elements in the post-transcriptional regulation of the TPD52 gene.
[Mh] Termos MeSH primário: Regulação Neoplásica da Expressão Gênica
Proteínas de Neoplasias/metabolismo
Proteínas de Ligação a Poli(A)/metabolismo
RNA Mensageiro/metabolismo
RNA Neoplásico/metabolismo
Proteínas de Ligação a RNA/metabolismo
Elementos de Resposta
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Linhagem Celular Tumoral
Células Cultivadas
Técnicas de Silenciamento de Genes
Genes Reporter
Seres Humanos
Imunoprecipitação
Proteínas de Neoplasias/antagonistas & inibidores
Proteínas de Neoplasias/química
Proteínas de Neoplasias/genética
Fragmentos de Peptídeos/antagonistas & inibidores
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Proteínas de Ligação a Poli(A)/antagonistas & inibidores
Proteínas de Ligação a Poli(A)/genética
Interferência de RNA
Estabilidade de RNA
RNA Mensageiro/antagonistas & inibidores
RNA Mensageiro/química
RNA Neoplásico/antagonistas & inibidores
RNA Neoplásico/química
Proteínas de Ligação a RNA/antagonistas & inibidores
Proteínas de Ligação a RNA/genética
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Deleção de Sequência
Antígeno-1 Intracelular de Células T
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Neoplasm Proteins); 0 (Peptide Fragments); 0 (Poly(A)-Binding Proteins); 0 (RNA, Messenger); 0 (RNA, Neoplasm); 0 (RNA-Binding Proteins); 0 (Recombinant Proteins); 0 (T-Cell Intracellular Antigen-1); 0 (TIA1 protein, human); 0 (TPD52 protein, human); 0 (TPD52L1 protein, human); 0 (TPD52L2 protein, human); 148592-68-1 (TIAL1 protein, human)
[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:170317
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20160942


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[PMID]:28257633
[Au] Autor:Liu Y; Liu R; Yang F; Cheng R; Chen X; Cui S; Gu Y; Sun W; You C; Liu Z; Sun F; Wang Y; Fu Z; Ye C; Zhang C; Li J; Chen X
[Ad] Endereço:State Key Laboratory of Pharmaceutical Biotechnology, Collaborative Innovation Center of Chemistry for Life Sciences, Jiangsu Engineering Research Center for MicroRNA Biology and Biotechnology, NJU Advanced Institute for Life Sciences (NAILS), School of Life Sciences, Nanjing University, 163 Xianlin
[Ti] Título:miR-19a promotes colorectal cancer proliferation and migration by targeting TIA1.
[So] Source:Mol Cancer;16(1):53, 2017 Mar 04.
[Is] ISSN:1476-4598
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Colorectal cancer (CRC) is a major worldwide health problem due to its high prevalence and mortality rate. T-cell intracellular antigen 1 (TIA1) is an important tumor suppressor involved in many aspects of carcinogenesis and cancer development. How TIA1 expression is regulated during CRC development remains to be carefully elucidated. METHODS: In CRC tissue sample pairs, TIA1 protein and mRNA levels were monitored by Western blot and qRT-PCR, respectively. Combining meta-analysis and miRNA target prediction software, we could predict microRNAs that targeted TIA1. Next, three CRC cell lines (SW480, Caco2 and HT29) were used to demonstrate the direct targeting of TIA1 by miR-19a. In addition, we investigated the biological effects of TIA1 inhibition by miR-19a both in vitro by CCK-8, EdU, Transwell, Ki67 immunofluorescence and Colony formation assays and in vivo by a xenograft mice model. RESULTS: In colorectal cancer (CRC), we found that TIA1 protein, but not its mRNA, was downregulated. We predicted that TIA1 was a target of miR-19a and validated that miR-19a binded directly to the 3'-UTR of TIA1 mRNA. miR-19a could promote cell proliferation and migration in CRC cells and accelerated tumor growth in xenograft mice by targeting TIA1. CONCLUSIONS: This study highlights an oncomiR role for miR-19a in regulating TIA1 in CRC and suggests that miR-19a may be a novel molecular therapeutic target for CRC.
[Mh] Termos MeSH primário: Neoplasias Colorretais/genética
MicroRNAs/genética
Proteínas de Ligação a Poli(A)/genética
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Animais
Proteínas Reguladoras de Apoptose/genética
Sítios de Ligação
Linhagem Celular Tumoral
Movimento Celular/genética
Proliferação Celular/genética
Neoplasias Colorretais/metabolismo
Neoplasias Colorretais/patologia
Modelos Animais de Doenças
Perfilação da Expressão Gênica
Regulação Neoplásica da Expressão Gênica
Genes myc
Xenoenxertos
Seres Humanos
Masculino
Metanálise como Assunto
Camundongos
Proteínas de Ligação a Poli(A)/metabolismo
Interferência de RNA
Processamento Pós-Transcricional do RNA
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Proteínas de Ligação a RNA/genética
Antígeno-1 Intracelular de Células T
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Apoptosis Regulatory Proteins); 0 (MIRN19 microRNA, human); 0 (MicroRNAs); 0 (PDCD4 protein, human); 0 (Poly(A)-Binding Proteins); 0 (RNA, Messenger); 0 (RNA-Binding Proteins); 0 (T-Cell Intracellular Antigen-1); 0 (TIA1 protein, human)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170305
[St] Status:MEDLINE
[do] DOI:10.1186/s12943-017-0625-8


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[PMID]:28193846
[Au] Autor:Huang SC; Zhang HS; Yu B; McMahon E; Nguyen DT; Yu FH; Ou AC; Ou JP; Benz EJ
[Ad] Endereço:Department of Medical Oncology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA shu-ching_huang@dfci.harvard.edu.
[Ti] Título:Protein 4.1R Exon 16 3' Splice Site Activation Requires Coordination among TIA1, Pcbp1, and RBM39 during Terminal Erythropoiesis.
[So] Source:Mol Cell Biol;37(9), 2017 May 01.
[Is] ISSN:1098-5549
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Exon 16 of protein 4.1R encodes a spectrin/actin-binding peptide critical for erythrocyte membrane stability. Its expression during erythroid differentiation is regulated by alternative pre-mRNA splicing. A UUUUCCCCCC motif situated between the branch point and the 3' splice site is crucial for inclusion. We show that the UUUU region and the last three C residues in this motif are necessary for the binding of splicing factors TIA1 and Pcbp1 and that these proteins appear to act in a collaborative manner to enhance exon 16 inclusion. This element also activates an internal exon when placed in a corresponding intronic position in a heterologous reporter. The impact of these two factors is further enhanced by high levels of RBM39, whose expression rises during erythroid differentiation as exon 16 inclusion increases. TIA1 and Pcbp1 associate in a complex containing RBM39, which interacts with U2AF65 and SF3b155 and promotes U2 snRNP recruitment to the branch point. Our results provide a mechanism for exon 16 3' splice site activation in which a coordinated effort among TIA1, Pcbp1, and RBM39 stabilizes or increases U2 snRNP recruitment, enhances spliceosome A complex formation, and facilitates exon definition through RBM39-mediated splicing regulation.
[Mh] Termos MeSH primário: Processamento Alternativo/genética
Proteínas do Citoesqueleto/genética
Eritropoese/fisiologia
Ribonucleoproteínas Nucleares Heterogêneas/metabolismo
Proteínas de Membrana/genética
Proteínas Nucleares/metabolismo
Proteínas de Ligação a Poli(A)/metabolismo
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação/genética
Linhagem Celular Tumoral
Eritropoese/genética
Células HEK293
Células HeLa
Seres Humanos
Camundongos
Fosfoproteínas/metabolismo
Ligação Proteica/genética
Fatores de Processamento de RNA/metabolismo
Ribonucleoproteínas Nucleares Pequenas/metabolismo
Spliceossomos/metabolismo
Fator de Processamento U2AF/metabolismo
Antígeno-1 Intracelular de Células T
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytoskeletal Proteins); 0 (HCC1 autoantigen); 0 (Heterogeneous-Nuclear Ribonucleoproteins); 0 (Membrane Proteins); 0 (Nuclear Proteins); 0 (PCBP1 protein, human); 0 (Phosphoproteins); 0 (Poly(A)-Binding Proteins); 0 (RNA Splicing Factors); 0 (RNA-Binding Proteins); 0 (Ribonucleoproteins, Small Nuclear); 0 (SF3B1 protein, human); 0 (Splicing Factor U2AF); 0 (T-Cell Intracellular Antigen-1); 0 (TIA1 protein, human); 0 (U2AF2 protein, human); 0 (erythrocyte membrane band 4.1 protein)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170215
[St] Status:MEDLINE


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[PMID]:28184449
[Au] Autor:Waris S; García-Mauriño SM; Sivakumaran A; Beckham SA; Loughlin FE; Gorospe M; Díaz-Moreno I; Wilce MCJ; Wilce JA
[Ad] Endereço:Monash Biomedicine Discovery Institute, Department of Biochemistry & Molecular Biology, Monash University, Victoria 3800, Australia.
[Ti] Título:TIA-1 RRM23 binding and recognition of target oligonucleotides.
[So] Source:Nucleic Acids Res;45(8):4944-4957, 2017 May 05.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:TIA-1 (T-cell restricted intracellular antigen-1) is an RNA-binding protein involved in splicing and translational repression. It mainly interacts with RNA via its second and third RNA recognition motifs (RRMs), with specificity for U-rich sequences directed by RRM2. It has recently been shown that RRM3 also contributes to binding, with preferential binding for C-rich sequences. Here we designed UC-rich and CU-rich 10-nt sequences for engagement of both RRM2 and RRM3 and demonstrated that the TIA-1 RRM23 construct preferentially binds the UC-rich RNA ligand (5΄-UUUUUACUCC-3΄). Interestingly, this binding depends on the presence of Lys274 that is C-terminal to RRM3 and binding to equivalent DNA sequences occurs with similar affinity. Small-angle X-ray scattering was used to demonstrate that, upon complex formation with target RNA or DNA, TIA-1 RRM23 adopts a compact structure, showing that both RRMs engage with the target 10-nt sequences to form the complex. We also report the crystal structure of TIA-1 RRM2 in complex with DNA to 2.3 Šresolution providing the first atomic resolution structure of any TIA protein RRM in complex with oligonucleotide. Together our data support a specific mode of TIA-1 RRM23 interaction with target oligonucleotides consistent with the role of TIA-1 in binding RNA to regulate gene expression.
[Mh] Termos MeSH primário: Proteínas de Ligação a DNA/química
DNA/química
Proteínas de Ligação a Poli(A)/química
Ribonucleosídeo Difosfato Redutase/química
[Mh] Termos MeSH secundário: Cristalografia por Raios X
DNA/genética
Proteínas de Ligação a DNA/genética
Regulação da Expressão Gênica
Seres Humanos
Oligonucleotídeos/química
Proteínas de Ligação a Poli(A)/genética
Ligação Proteica/genética
Mapas de Interação de Proteínas/genética
Motivo de Reconhecimento de RNA/genética
Ribonucleosídeo Difosfato Redutase/genética
Antígeno-1 Intracelular de Células T
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Oligonucleotides); 0 (Poly(A)-Binding Proteins); 0 (T-Cell Intracellular Antigen-1); 0 (TIA1 protein, human); 9007-49-2 (DNA); EC 1.17.4.- (ribonucleotide reductase M2); EC 1.17.4.1 (Ribonucleoside Diphosphate Reductase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170211
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx102


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[PMID]:28011649
[Au] Autor:Sun Y; Dong L; Yu S; Wang X; Zheng H; Zhang P; Meng C; Zhan Y; Tan L; Song C; Qiu X; Wang G; Liao Y; Ding C
[Ad] Endereço:Department of Avian Infectious Diseases, Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Science, Shanghai, China.
[Ti] Título:Newcastle disease virus induces stable formation of stress granules to facilitate viral replication through manipulating host protein translation.
[So] Source:FASEB J;31(4):1337-1353, 2017 Apr.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mammalian cells respond to various environmental stressors to form stress granules (SGs) by arresting cytoplasmic mRNA, protein translation element, and RNA binding proteins. Virus-induced SGs function in different ways, depending on the species of virus; however, the mechanism of SG regulation of virus replication is not well understood. In this study, Newcastle disease virus (NDV) triggered stable formation of SGs on HeLa cells through activating the protein kinase R (PKR)/eIF2α pathway. NDV-induced SGs contained classic SG markers T-cell internal antigen (TIA)-1, Ras GTPase-activating protein-binding protein (G3BP)-1, eukaryotic initiation factors, and small ribosomal subunit, which could be disassembled in the presence of cycloheximide. Treatment with nocodazole, a microtubule disruption drug, led to the formation of relatively small and circular granules, indicating that NDV infection induces canonical SGs. Furthermore, the role of SGs on NDV replication was investigated by knockdown of TIA-1 and TIA-1-related (TIAR) protein, the 2 critical components involved in SG formation from the HeLa cells, followed by NDV infection. Results showed that depletion of TIA-1 or TIAR inhibited viral protein synthesis, reduced extracellular virus yields, but increased global protein translation. FISH revealed that NDV-induced SGs contained predominantly cellular mRNA rather than viral mRNA. Deletion of TIA-1 or TIAR reduced NP mRNA levels in polysomes. These results demonstrate that NDV triggers stable formation of SGs, which benefit viral protein translation and virus replication by arresting cellular mRNA.-Sun, Y., Dong, L., Yu, S., Wang, X., Zheng, H., Zhang, P., Meng, C., Zhan, Y., Tan, L., Song, C., Qiu, X., Wang, G., Liao, Y., Ding, C. Newcastle disease virus induces stable formation of stress granules to facilitate viral replication through manipulating host protein translation.
[Mh] Termos MeSH primário: Grânulos Citoplasmáticos/metabolismo
Interações Hospedeiro-Patógeno
Vírus da Doença de Newcastle/fisiologia
Replicação Viral
[Mh] Termos MeSH secundário: Animais
Proteínas de Transporte/metabolismo
Células Cultivadas
Galinhas
DNA Helicases
Fator de Iniciação 2 em Eucariotos/metabolismo
Células HeLa
Seres Humanos
Vírus da Doença de Newcastle/metabolismo
Vírus da Doença de Newcastle/patogenicidade
Proteínas de Ligação a Poli(A)/metabolismo
Proteínas de Ligação a Poli-ADP-Ribose
Biossíntese de Proteínas
RNA Helicases
Proteínas com Motivo de Reconhecimento de RNA
Proteínas de Ligação a RNA
Subunidades Ribossômicas/metabolismo
Antígeno-1 Intracelular de Células T
eIF-2 Quinase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Eukaryotic Initiation Factor-2); 0 (Poly(A)-Binding Proteins); 0 (Poly-ADP-Ribose Binding Proteins); 0 (RNA Recognition Motif Proteins); 0 (RNA-Binding Proteins); 0 (T-Cell Intracellular Antigen-1); 0 (TIA1 protein, human); 148592-68-1 (TIAL1 protein, human); EC 2.7.11.1 (eIF-2 Kinase); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (G3BP1 protein, human); EC 3.6.4.13 (RNA Helicases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161225
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201600980R


  8 / 323 MEDLINE  
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[PMID]:27575817
[Au] Autor:Navratilova Z; Novosadova E; Hagemann-Jensen M; Kullberg S; Kolek V; Grunewald J; Petrek M
[Ad] Endereço:Laboratory of Immunogenomics and Immunoproteomics, Department of Pathological Physiology, Faculty of Medicine and Dentistry Palacky University, Olomouc, Czech Republic.
[Ti] Título:Expression Profile of Six RNA-Binding Proteins in Pulmonary Sarcoidosis.
[So] Source:PLoS One;11(8):e0161669, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Sarcoidosis is characterised by up-regulation of cytokines and chemokine ligands/receptors and proteolytic enzymes. This pro-inflammatory profile is regulated post-transcriptionally by RNA-binding proteins (RBPs). We investigated in vivo expression of six RBPs (AUF1, HuR, NCL, TIA, TIAR, PCBP2) and two inhibitors of proteolytic enzymes (RECK, PTEN) in pulmonary sarcoidosis and compared it to the expression in four control groups of healthy individuals and patients with other respiratory diseases: chronic obstructive pulmonary disease (COPD), asthma and idiopathic interstitial pneumonias (IIPs). METHODS: RT-PCR was used to quantify the mRNAs in bronchoalveolar (BA) cells obtained from 50 sarcoidosis patients, 23 healthy controls, 30 COPD, 19 asthmatic and 19 IIPs patients. Flow cytometry was used to assess intracellular protein expression of AUF1 and HuR in peripheral blood T lymphocytes (PBTLs) obtained from 9 sarcoidosis patients and 6 healthy controls. RESULTS: Taking the stringent conditions for multiple comparisons into consideration, we consistently observed in the primary analysis including all patients regardless of smoking status as well as in the subsequent sub-analysis limited for never smokers that the BA mRNA expression of AUF1 (p<0.001), TIA (p<0.001), NCL (p<0.01) and RECK (p<0.05) was decreased in sarcoidosis compared to healthy controls. TIA mRNA was also decreased in sarcoidosis compared to both obstructive pulmonary diseases (COPD and asthma; p<0.001) but not compared to IIPs. There were several positive correlations between RECK mRNA and RBP mRNAs in BA cells. Also sarcoidosis CD3+, CD4+ and CD8+ PBTLs displayed lower mean fluorescence intensity of AUF1 (p≤0.02) and HuR (p≤0.03) proteins than control healthy PBTLs. CONCLUSION: mRNA expressions of three RBPs (AUF1, TIA and NCL) and their potential target mRNA encoding RECK in BA cells and additionally protein expression of AUF1 and HuR in PBTLs were down-regulated in our sarcoidosis patients compared to healthy individuals. Its significance, e.g. for stability of mRNAs encoding pro-inflammatory factors, should be further explored in sarcoidosis.
[Mh] Termos MeSH primário: Asma/genética
Perfilação da Expressão Gênica/métodos
Pneumonias Intersticiais Idiopáticas/genética
Doença Pulmonar Obstrutiva Crônica/genética
Proteínas de Ligação a RNA/genética
Sarcoidose Pulmonar/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Asma/metabolismo
Proteína Semelhante a ELAV 1/genética
Proteína Semelhante a ELAV 1/metabolismo
Feminino
Proteínas Ligadas por GPI/genética
Proteínas Ligadas por GPI/metabolismo
Regulação da Expressão Gênica
Ribonucleoproteínas Nucleares Heterogêneas Grupo D/genética
Ribonucleoproteínas Nucleares Heterogêneas Grupo D/metabolismo
Seres Humanos
Pneumonias Intersticiais Idiopáticas/metabolismo
Masculino
Meia-Idade
PTEN Fosfo-Hidrolase/genética
PTEN Fosfo-Hidrolase/metabolismo
Fosfoproteínas/genética
Fosfoproteínas/metabolismo
Proteínas de Ligação a Poli(A)/genética
Proteínas de Ligação a Poli(A)/metabolismo
Doença Pulmonar Obstrutiva Crônica/metabolismo
Proteínas de Ligação a RNA/metabolismo
Sarcoidose Pulmonar/metabolismo
Antígeno-1 Intracelular de Células T
Linfócitos T/metabolismo
Adulto Jovem
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ELAV-Like Protein 1); 0 (ELAVL1 protein, human); 0 (GPI-Linked Proteins); 0 (Heterogeneous-Nuclear Ribonucleoprotein D); 0 (PCBP2 protein, human); 0 (Phosphoproteins); 0 (Poly(A)-Binding Proteins); 0 (RECK protein, human); 0 (RNA-Binding Proteins); 0 (T-Cell Intracellular Antigen-1); 0 (TIA1 protein, human); 0 (hnRNP D0); 0 (nucleolin); 148592-68-1 (TIAL1 protein, human); EC 3.1.3.67 (PTEN Phosphohydrolase); EC 3.1.3.67 (PTEN protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160831
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0161669


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[PMID]:27560627
[Au] Autor:Hashimoto S; Yamamoto S; Ogasawara N; Sato T; Yamamoto K; Katoh H; Kubota T; Shiraishi T; Kojima T; Himi T; Tsutsumi H; Yokota S
[Ad] Endereço:Department of Pediatrics, Sapporo Medical University School of Medicine, Sapporo, Japan.
[Ti] Título:Mumps Virus Induces Protein-Kinase-R-Dependent Stress Granules, Partly Suppressing Type III Interferon Production.
[So] Source:PLoS One;11(8):e0161793, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Stress granules (SGs) are cytoplasmic granular aggregations that are induced by cellular stress, including viral infection. SGs have opposing antiviral and proviral roles, which depend on virus species. The exact function of SGs during viral infection is not fully understood. Here, we showed that mumps virus (MuV) induced SGs depending on activation of protein kinase R (PKR). MuV infection strongly induced interferon (IFN)-λ1, 2 and 3, and IFN-ß through activation of IFN regulatory factor 3 (IRF3) via retinoic acid inducible gene-I (RIG-I) and the mitochondrial antiviral signaling (MAVS) pathway. MuV-induced IFNs were strongly upregulated in PKR-knockdown cells. MuV-induced SG formation was suppressed by knockdown of PKR and SG marker proteins, Ras-GTPase-activating protein SH3-domain-binding protein 1 and T-cell-restricted intracellular antigen-1, and significantly increased the levels of MuV-induced IFN-λ1. However, viral titer was not altered by suppression of SG formation. PKR was required for induction of SGs by MuV infection and regulated type III IFN (IFN-λ1) mRNA stability. MuV-induced SGs partly suppressed type III IFN production by MuV; however, the limited suppression was not sufficient to inhibit MuV replication in cell culture. Our results provide insight into the relationship between SGs and IFN production induced by MuV infection.
[Mh] Termos MeSH primário: Grânulos Citoplasmáticos/virologia
Interferons/biossíntese
Vírus da Caxumba/fisiologia
eIF-2 Quinase/metabolismo
[Mh] Termos MeSH secundário: Animais
Western Blotting
Proteínas de Transporte/genética
Linhagem Celular
Cercopithecus aethiops
Grânulos Citoplasmáticos/metabolismo
Proteína DEAD-box 58/metabolismo
DNA Helicases
Expressão Gênica
Interações Hospedeiro-Patógeno
Seres Humanos
Fator Regulador 3 de Interferon/metabolismo
Interferons/genética
Microscopia Confocal
Mitocôndrias/metabolismo
Proteínas de Ligação a Poli(A)/genética
Proteínas de Ligação a Poli-ADP-Ribose
RNA Helicases
Interferência de RNA
Proteínas com Motivo de Reconhecimento de RNA
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Transdução de Sinais
Estresse Fisiológico/fisiologia
Antígeno-1 Intracelular de Células T
Células Vero
eIF-2 Quinase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (IRF3 protein, human); 0 (Interferon Regulatory Factor-3); 0 (Poly(A)-Binding Proteins); 0 (Poly-ADP-Ribose Binding Proteins); 0 (RNA Recognition Motif Proteins); 0 (T-Cell Intracellular Antigen-1); 0 (TIA1 protein, human); 9008-11-1 (Interferons); EC 2.7.11.1 (eIF-2 Kinase); EC 3.6.1.- (DDX58 protein, human); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (G3BP1 protein, human); EC 3.6.4.13 (DEAD Box Protein 58); EC 3.6.4.13 (RNA Helicases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160826
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0161793


  10 / 323 MEDLINE  
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[PMID]:27457239
[Au] Autor:Ishibashi H; Nimura S; Kayashima Y; Takamatsu Y; Aoyagi K; Harada N; Kadowaki M; Kamio T; Sakisaka S; Takeshita M
[Ad] Endereço:Department of Gastroenterology and Medicine, Faculty of Medicine, Fukuoka University, Fukuoka, 814-0180, Japan.
[Ti] Título:Multiple lesions of gastrointestinal tract invasion by monomorphic epitheliotropic intestinal T-cell lymphoma, accompanied by duodenal and intestinal enteropathy-like lesions and microscopic lymphocytic proctocolitis: a case series.
[So] Source:Diagn Pathol;11(1):66, 2016 Jul 25.
[Is] ISSN:1746-1596
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: In East Asia, monomorphic epitheliotropic intestinal T-cell lymphoma (MEITL), previously known as type II enteropathy-associated T-cell lymphoma (EATL), occurs more frequently than type I EATL, and coeliac disease is rare. CASE PRESENTATION: Here we present four cases of MEITL in Japanese patients, including the endoscopic and pathological findings of their duodenal and colorectal lesions. Tumor specimens obtained from duodenal, intestinal, and colorectal biopsies in all four patients showed a diffuse intramucosal infiltration of small to/or medium-sized lymphoma cells and numerous atypical intraepithelial lymphocytes (IELs). These cells were immunohistologically positive for CD103, CD3, CD7, CD8, CD56, and T-cell intracellular antigen-1. Upper and lower gastrointestinal and antegrade double-balloon endoscopy revealed foci of edematous mucosa, with or without villous atrophy, in the non-neoplastic mucosa. Histological studies demonstrated duodenal and intestinal enteropathy-like lesions as well as microscopic (lymphocytic) proctocolitis with increased CD3- and CD8-positive and CD56-negative T-IELs in all four patients. The clinicopathological findings of the non-neoplastic lesions were similar to those characteristic of coeliac disease, suggesting that variants of coeliac disease may be present in the prodromal lesions of MEITL. CONCLUSIONS: Our study supports the need for random gastrointestinal biopsies to determine tumor spread, the features of MEITL in the particular patients, and the presence of prodromal non-neoplastic lesions.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/metabolismo
Linfoma de Células T Associado a Enteropatia/diagnóstico
Intestinos/patologia
Proctocolite/diagnóstico
[Mh] Termos MeSH secundário: Adulto
Idoso
Antígenos CD/metabolismo
Linfoma de Células T Associado a Enteropatia/metabolismo
Feminino
Seres Humanos
Intestinos/metabolismo
Japão
Masculino
Meia-Idade
Proteínas de Ligação a Poli(A)/metabolismo
Proctocolite/metabolismo
Antígeno-1 Intracelular de Células T
Linfócitos T/metabolismo
Linfócitos T/patologia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD); 0 (Biomarkers, Tumor); 0 (Poly(A)-Binding Proteins); 0 (T-Cell Intracellular Antigen-1); 0 (TIA1 protein, human)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160727
[St] Status:MEDLINE
[do] DOI:10.1186/s13000-016-0519-x



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