Base de dados : MEDLINE
Pesquisa : D12.644.360.024.285 [Categoria DeCS]
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  1 / 431 MEDLINE  
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[PMID]:29325736
[Au] Autor:Dallel M; Sarray S; Douma Z; Hachani F; Al-Ansari AK; Letaifa DB; Mahjoub T; Almawi WY
[Ad] Endereço:Laboratory of Human Genome and Multifactorial Diseases (LR12ES07), Faculty of Pharmacy of Monastir, University of Monastir, Tunisia.
[Ti] Título:Differential association of DENND1A genetic variants with polycystic ovary syndrome in Tunisian but not Bahraini Arab women.
[So] Source:Gene;647:79-84, 2018 Mar 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND AND AIM: Polycystic ovary syndrome (PCOS) is a common endocrine disorder, and results from interaction between modifiable and non-modifiable factors, including genetic predisposition. Previous genome-wide association studies and meta-analysis identified DENND1A as PCOS susceptibility locus in some, but not all populations. We investigated whether the association of DENND1A gene variants with PCOS was similar between Tunisian and Bahraini Arab women. SUBJECTS AND METHODS: This was retrospective case-control study. Study subjects comprised 320 women with PCOS, and 446 age-and ethnically-matched control women. Genotyping of DENND1A rs10818854, rs2479106, and rs10986105 variants was done by real-time PCR. RESULTS: Minor allele frequency of rs10818854 and rs10986105 DENND1A variants were significantly higher among women with PCOS. Setting homozygous wild-type genotype carrier as reference, rs10818854 and rs10986105 were associated with increased risk of PCOS, which persisted after controlling for key covariates, while reduced PCOS risk was seen with only rs2479106 under the additive model. This assigned PCOS susceptibility and protective nature to these genotypes, respectively. Both rs10818854 and rs10986105 were positively associated with HOMA-IR and AMH in women with PCOS. Haploview analysis revealed limited linkage disequilibrium between the tested DENND1A variants. Extensive diversity in haplotypes assignment was seen, with most haplotypes (99.5%) captured by 5 haplotypes. Taking GAT haplotype as reference, AAG, and GAG haplotypes were positively, while GAT haplotype was negatively associated with PCOS. CONCLUSION: The association of DENND1A rs10818854 and rs10986105 variants with PCOS in Tunisian but not Bahraini women confirms the dependence of this association on the ethnic/racial origin of study subjects.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Sinalização de Receptores de Domínio de Morte/genética
Predisposição Genética para Doença/genética
Fatores de Troca do Nucleotídeo Guanina/genética
Síndrome do Ovário Policístico/genética
Polimorfismo de Nucleotídeo Único/genética
[Mh] Termos MeSH secundário: Adulto
Árabes
Estudos de Casos e Controles
Feminino
Frequência do Gene/genética
Estudo de Associação Genômica Ampla/métodos
Haplótipos/genética
Seres Humanos
Desequilíbrio de Ligação/genética
Estudos Retrospectivos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DENND1A protein, human); 0 (Death Domain Receptor Signaling Adaptor Proteins); 0 (Guanine Nucleotide Exchange Factors)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180113
[St] Status:MEDLINE


  2 / 431 MEDLINE  
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Barreto, Mauricio L
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[PMID]:28668455
[Au] Autor:Fiuza BSD; Silva MJ; Alcântara-Neves NM; Barreto ML; Costa RDS; Figueiredo CA
[Ad] Endereço:Departamento de Biorregulação, Laboratório de Imunofarmacologia e Biologia Molecular, Universidade Federal da Bahia (ICS), Bahia, Brazil.
[Ti] Título:Polymorphisms in DENND1B gene are associated with asthma and atopy phenotypes in Brazilian children.
[So] Source:Mol Immunol;90:33-41, 2017 Oct.
[Is] ISSN:1872-9142
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Asthma is a heterogeneous disease associated with a complex basis involving environmental factors and individual variabilities. The DENN Domain Containing 1B (DENND1B) gene has an important role on T cell receptor (TCR) down-regulation on Th2 cells and studies have shown that mutations or loss of this factor can be associated with increased Th2 responses and asthma. The aim of this work is to evaluate the association of polymorphisms in the DENND1B with asthma and allergy markers phenotypes in Brazilian children. Genotyping was performed using a commercial panel from Illumina (2.5 Human Omni bead chip) in 1309 participants of SCAALA (Social Change, Asthma, Allergy in Latin American) program. Logistic regressions for asthma and atopy markers were performed using PLINK software 1.9. The analyzes were adjusted for sex, age, helminth infections and ancestry markers. The DENND1B gene was associated with different phenotypes such as severe asthma and atopic markers (specific IgE production, skin prick test and IL-13 production). Among the 166 SNPs analyzed, 72 were associated with asthma and/or allergy markers. In conclusion, polymorphisms in the DENND1B are significantly associated with development of asthma and atopy and these polymorphisms can influence DENND1B expression and consequently, asthma.
[Mh] Termos MeSH primário: Asma/genética
Proteínas Adaptadoras de Sinalização de Receptores de Domínio de Morte/genética
Predisposição Genética para Doença
Fatores de Troca do Nucleotídeo Guanina/genética
Hipersensibilidade Imediata/genética
[Mh] Termos MeSH secundário: Adolescente
Asma/imunologia
Brasil
Criança
Pré-Escolar
Citocinas/biossíntese
Feminino
Estudos de Associação Genética
Seres Humanos
Hipersensibilidade Imediata/imunologia
Imunoglobulina E/sangue
Masculino
Polimorfismo de Nucleotídeo Único/genética
Inquéritos e Questionários
Células Th2/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (DENND1B protein, human); 0 (Death Domain Receptor Signaling Adaptor Proteins); 0 (Guanine Nucleotide Exchange Factors); 37341-29-0 (Immunoglobulin E)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170703
[St] Status:MEDLINE


  3 / 431 MEDLINE  
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[PMID]:28432080
[Au] Autor:Ando K; Parsons MJ; Shah RB; Charendoff CI; Paris SL; Liu PH; Fassio SR; Rohrman BA; Thompson R; Oberst A; Sidi S; Bouchier-Hayes L
[Ad] Endereço:Department of Medicine, Division of Hematology/Oncology, Tisch Cancer Institute at Mount Sinai, New York, NY 10029.
[Ti] Título:NPM1 directs PIDDosome-dependent caspase-2 activation in the nucleolus.
[So] Source:J Cell Biol;216(6):1795-1810, 2017 Jun 05.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The PIDDosome (PIDD-RAIDD-caspase-2 complex) is considered to be the primary signaling platform for caspase-2 activation in response to genotoxic stress. Yet studies of PIDD-deficient mice show that caspase-2 activation can proceed in the absence of PIDD. Here we show that DNA damage induces the assembly of at least two distinct activation platforms for caspase-2: a cytoplasmic platform that is RAIDD dependent but PIDD independent, and a nucleolar platform that requires both PIDD and RAIDD. Furthermore, the nucleolar phosphoprotein nucleophosmin (NPM1) acts as a scaffold for PIDD and is essential for PIDDosome assembly in the nucleolus after DNA damage. Inhibition of NPM1 impairs caspase-2 processing, apoptosis, and caspase-2-dependent inhibition of cell growth, demonstrating that the NPM1-dependent nucleolar PIDDosome is a key initiator of the caspase-2 activation cascade. Thus we have identified the nucleolus as a novel site for caspase-2 activation and function.
[Mh] Termos MeSH primário: Apoptose
Caspase 2/metabolismo
Nucléolo Celular/enzimologia
Cisteína Endopeptidases/metabolismo
Dano ao DNA
Proteínas Adaptadoras de Sinalização de Receptores de Domínio de Morte/metabolismo
Proteínas Nucleares/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteína Adaptadora de Sinalização CRADD/metabolismo
Caspase 2/genética
Cisteína Endopeptidases/genética
Proteínas Adaptadoras de Sinalização de Receptores de Domínio de Morte/genética
Ativação Enzimática
Genótipo
Células HEK293
Células HeLa
Seres Humanos
Camundongos Knockout
Microscopia Confocal
Microscopia de Fluorescência
Microscopia de Vídeo
Complexos Multiproteicos
Proteínas Nucleares/genética
Fenótipo
Ligação Proteica
Interferência de RNA
Transdução de Sinais
Transfecção
Peixe-Zebra/genética
Peixe-Zebra/metabolismo
Proteínas de Peixe-Zebra/genética
Proteínas de Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; VIDEO-AUDIO MEDIA
[Nm] Nome de substância:
0 (CRADD Signaling Adaptor Protein); 0 (CRADD protein, human); 0 (Death Domain Receptor Signaling Adaptor Proteins); 0 (Lrdd protein, mouse); 0 (Multiprotein Complexes); 0 (Nuclear Proteins); 0 (PIDD protein, human); 0 (Zebrafish Proteins); 117896-08-9 (nucleophosmin); EC 3.4.22.- (CASP2 protein, human); EC 3.4.22.- (Casp2 protein, mouse); EC 3.4.22.- (Caspase 2); EC 3.4.22.- (Cysteine Endopeptidases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170423
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201608095


  4 / 431 MEDLINE  
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[PMID]:28323882
[Au] Autor:Ghorbani S; Talebi F; Ghasemi S; Jahanbazi Jahan Abad A; Vojgani M; Noorbakhsh F
[Ad] Endereço:Department of Immunology, School of Medicine, Tehran University of Medical Sciences, Tehran, Iran.
[Ti] Título:miR-181 interacts with signaling adaptor molecule DENN/MADD and enhances TNF-induced cell death.
[So] Source:PLoS One;12(3):e0174368, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:MicroRNAs are small noncoding RNAs, which regulate the expression of protein coding transcripts through mRNA degradation or translational inhibition. Numerous reports have highlighted the role of miRNAs in regulating cell death pathways including the expression of genes involved in the induction of apoptosis. Tumor necrosis factor alpha (TNF-α) is a proinflammatory cytokine which can send pro-death signals through its receptor TNFR1. Diverse adaptor molecules including DENN/MADD adaptor protein have been shown to modulate TNF-α pro-death signaling via recruitment of MAP kinases to TNFR1 and activation of pro-survival NFκB signaling. Herein, we investigated the role of microRNA-181 (miR-181) in regulating DENN/MADD expression levels and its subsequent effects on TNF-α-induced cell death. Using bioinformatics analyses followed by luciferase reporter assays we showed that miR-181 interacts with the 3' UTR of DENN/MADD transcripts. miR-181 overexpression also led to decreased endogenous DENN/MADD mRNA levels in L929 murine fibroblasts. Flow cytometric analysis of miR-181 transfected cells showed this miRNA accentuates mitochondrial membrane potential loss caused by TNF-α. These findings were associated with enhanced apoptosis of L929 cells following TNF-α treatment. Overall, these data point to the potential role of miR-181 in regulating TNF-α pro-death signaling, which could be of importance from pathogenesis and therapeutic perspectives in inflammatory disorders associated with tissue degeneration and cell death.
[Mh] Termos MeSH primário: Apoptose/genética
Proteínas Adaptadoras de Sinalização de Receptores de Domínio de Morte/metabolismo
Fatores de Troca do Nucleotídeo Guanina/metabolismo
Potencial da Membrana Mitocondrial/fisiologia
MicroRNAs/genética
Receptores Tipo I de Fatores de Necrose Tumoral/metabolismo
Fator de Necrose Tumoral alfa/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Sobrevivência Celular/genética
Células L (Linhagem Celular)
Camundongos
MicroRNAs/metabolismo
NF-kappa B/metabolismo
Transdução de Sinais/genética
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Death Domain Receptor Signaling Adaptor Proteins); 0 (Guanine Nucleotide Exchange Factors); 0 (Madd protein, mouse); 0 (MicroRNAs); 0 (NF-kappa B); 0 (Receptors, Tumor Necrosis Factor, Type I); 0 (Tnfrsf1a protein, mouse); 0 (Tumor Necrosis Factor-alpha); 0 (mirn181 microRNA, mouse)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0174368


  5 / 431 MEDLINE  
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[PMID]:28270653
[Au] Autor:Sun J; Yu X; Wang C; Yu C; Li Z; Nie W; Xu X; Miao X; Jin X
[Ad] Endereço:Department of General Surgery, The 3rd Xiangya Hospital, Central South University, Changsha, Hunan, China (mainland).
[Ti] Título:RIP-1/c-FLIPL Induce Hepatic Cancer Cell Apoptosis Through Regulating Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand (TRAIL).
[So] Source:Med Sci Monit;23:1190-1199, 2017 Mar 08.
[Is] ISSN:1643-3750
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND Almost all hepatic cancer cells have resistance to tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis. c-FLIPL and RIP-1 are apoptotic negative regulatory factors. This study investigated the role of c-FLIPL and RIP-1 in hepatic cancer cell resistance to TRAIL-induced apoptosis. MATERIAL AND METHODS HepG2 cells were treated by TRAIL, RIP-1 siRNA, and/or BY11-7082. Cell viability was detected by MTT assay. Cell apoptosis was tested by flow cytometry. DISC component proteins, RIP-1, and p-p65 were measured by Western blot. Caspase-8 and caspase-3 were determined by spectrophotometry. RESULTS Single TRAIL treatment showed no significant impact on cell proliferation and apoptosis. HepG2 cells expressed high levels of RIP1 and c-FLIPL, while a high concentration of TRAIL upregulated RIP-1 and c-FLIPL expression but not DR4 and DR5. Single TRAIL treatment did not obviously activate caspase-8 and caspase-3. RIP-1 or c-FLIPL siRNA markedly induced cell apoptosis and enhanced caspase-8 and caspase-3 activities. Combined transfection obviously increased apoptotic cells. TRAIL markedly upregulated RIP-1 expression and enhanced p-p65 protein. Downregulating RIP-1 and/or BAY11-7082 significantly reduced NF-kB transcriptional activity, blocked cells in G0/G1 phase, weakened proliferation, elevated caspase-8 and caspase-3 activities, and promoted cell apoptosis. CONCLUSIONS TRAIL can enhance RIP1 and c-FLIPL expression in HepG2 cells. High expression of RIP1 and c-FLIPL is an important reason for TRAIL resistance. Downregulation of RIP1 and c-FLIPL can relieve caspase-8 suppression, activate caspase-3, and promote cell apoptosis. TRAIL mediates apoptosis resistance through upregulating RIP-1 expression, enhancing NF-kB transcriptional activity, and weakening caspase activity.
[Mh] Termos MeSH primário: Apoptose
Proteína Reguladora de Apoptosis Semelhante a CASP8 e FADD/metabolismo
Neoplasias Hepáticas/metabolismo
Neoplasias Hepáticas/patologia
Proteína Serina-Treonina Quinases de Interação com Receptores/metabolismo
Ligante Indutor de Apoptose Relacionado a TNF/metabolismo
[Mh] Termos MeSH secundário: Apoptose/efeitos dos fármacos
Caspases/metabolismo
Proliferação Celular/efeitos dos fármacos
Proteínas Adaptadoras de Sinalização de Receptores de Domínio de Morte/metabolismo
Regulação para Baixo/efeitos dos fármacos
Citometria de Fluxo
Técnicas de Silenciamento de Genes
Células Hep G2
Seres Humanos
NF-kappa B/metabolismo
Ligante Indutor de Apoptose Relacionado a TNF/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CASP8 and FADD-Like Apoptosis Regulating Protein); 0 (Death Domain Receptor Signaling Adaptor Proteins); 0 (NF-kappa B); 0 (TNF-Related Apoptosis-Inducing Ligand); EC 2.7.11.1 (RIPK1 protein, human); EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases); EC 3.4.22.- (Caspases)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170424
[Lr] Data última revisão:
170424
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170309
[St] Status:MEDLINE


  6 / 431 MEDLINE  
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[PMID]:28130345
[Au] Autor:Fava LL; Schuler F; Sladky V; Haschka MD; Soratroi C; Eiterer L; Demetz E; Weiss G; Geley S; Nigg EA; Villunger A
[Ad] Endereço:Division of Developmental Immunology, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.
[Ti] Título:The PIDDosome activates p53 in response to supernumerary centrosomes.
[So] Source:Genes Dev;31(1):34-45, 2017 Jan 01.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Centrosomes, the main microtubule-organizing centers in animal cells, are replicated exactly once during the cell division cycle to form the poles of the mitotic spindle. Supernumerary centrosomes can lead to aberrant cell division and have been causally linked to chromosomal instability and cancer. Here, we report that an increase in the number of mature centrosomes, generated by disrupting cytokinesis or forcing centrosome overduplication, triggers the activation of the PIDDosome multiprotein complex, leading to Caspase-2-mediated MDM2 cleavage, p53 stabilization, and p21-dependent cell cycle arrest. This pathway also restrains the extent of developmentally scheduled polyploidization by regulating p53 levels in hepatocytes during liver organogenesis. Taken together, the PIDDosome acts as a first barrier, engaging p53 to halt the proliferation of cells carrying more than one mature centrosome to maintain genome integrity.
[Mh] Termos MeSH primário: Centrossomo/fisiologia
Genes p53/genética
Complexos Multiproteicos/metabolismo
Ativação Transcricional/genética
[Mh] Termos MeSH secundário: Células A549
Animais
Proteína Adaptadora de Sinalização CRADD/metabolismo
Caspase 2/metabolismo
Pontos de Checagem do Ciclo Celular/genética
Células Cultivadas
Centrossomo/patologia
Citocinese/genética
Proteínas Adaptadoras de Sinalização de Receptores de Domínio de Morte/metabolismo
Seres Humanos
Fígado/citologia
Fígado/embriologia
Camundongos
Organogênese/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CRADD Signaling Adaptor Protein); 0 (Cradd protein, mouse); 0 (Death Domain Receptor Signaling Adaptor Proteins); 0 (Lrdd protein, mouse); 0 (Multiprotein Complexes); EC 3.4.22.- (Caspase 2)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171117
[Lr] Data última revisão:
171117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170129
[St] Status:MEDLINE
[do] DOI:10.1101/gad.289728.116


  7 / 431 MEDLINE  
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[PMID]:28034876
[Au] Autor:Wang C; Li L; Yin Z; Zhang Q; Zhao H; Tao R; Wang S; Hu S; He Y; Wang D; Li C; Zhang S; Xu J; Jiang X; Zhu S; Gao Y
[Ad] Endereço:Department of Forensic Medicine, Medical College of Soochow University, Suzhou 215123, Jiangsu, P.R. China.
[Ti] Título:An indel polymorphism within pre-miR3131 confers risk for hepatocellular carcinoma.
[So] Source:Carcinogenesis;38(2):168-176, 2017 Feb 01.
[Is] ISSN:1460-2180
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Polymorphisms in pre-miRNAs may affect its expression, then have effect on its target mRNAs and be associated with cancer susceptibility. In this study, we evaluated the association of an indel polymorphism rs57408770 in pre-miR-3131 with hepatocellular carcinoma (HCC) susceptibility in a Chinese population. The contribution of rs57408770 to HCC risk was investigated in two independent case-control sets (1051 HCC and 1058 controls). Logistic regression analysis showed that the insertion allele of rs57408770 was significantly associated with an increased risk for HCC occurrence in both case-control studies. Moreover, the results of genotype-phenotype correlation analysis from both in vivo and in vitro experiments showed that the insertion allele was significantly correlated with higher expression of mature miR-3131 comparing with the deletion allele. The RNA-Binding Protein Immunoprecipitation assay results indicated that rs57408770 could affect the expression level of mature miR-3131 probably through disturbing the binding of splicing factor SRp20 with pre-miR-3131. Furthermore, overexpression of miR-3131 displayed a proliferation promoting and anti-apoptosis effect on HCC cell lines, suggesting that miR-3131 may act as a proto-oncogene in HCC. Finally, human genome-wide gene expression profile assay was used to screen the targets of miR-3131. The overexpressed miR-3131 could lead to a significant decrease of DTHD1 and XAF1 mRNA level. Taken together, our findings provided evidence that rs57408770 may play a functional role in the carcinogenesis of HCC by affecting SRp20 binding with pre-miR-3131 and affecting the expression of mature miR-3131, subsequently affecting the expression of DTHD1 and XAF1, thus confers risk for HCC.
[Mh] Termos MeSH primário: Carcinoma Hepatocelular/genética
Proteínas Adaptadoras de Sinalização de Receptores de Domínio de Morte/genética
Peptídeos e Proteínas de Sinalização Intracelular/genética
Neoplasias Hepáticas/genética
MicroRNAs/genética
Proteínas de Neoplasias/genética
[Mh] Termos MeSH secundário: Idoso
Carcinoma Hepatocelular/patologia
China
Feminino
Regulação Neoplásica da Expressão Gênica
Estudos de Associação Genética
Predisposição Genética para Doença
Seres Humanos
Mutação INDEL/genética
Neoplasias Hepáticas/patologia
Masculino
MicroRNAs/biossíntese
Meia-Idade
Fatores de Risco
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DTHD1 protein, human); 0 (Death Domain Receptor Signaling Adaptor Proteins); 0 (Intracellular Signaling Peptides and Proteins); 0 (MicroRNAs); 0 (Neoplasm Proteins); 0 (XAF1 protein, human); 0 (microRNA 3131, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170830
[Lr] Data última revisão:
170830
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161231
[St] Status:MEDLINE
[do] DOI:10.1093/carcin/bgw206


  8 / 431 MEDLINE  
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[PMID]:28000900
[Au] Autor:Yu G; Jia Z; Dou Z
[Ad] Endereço:Department of Urological Surgery, The First Affiliated Hospital and College of Clinical Medicine of Henan University of Science and Technology, Luoyang, Henan 471003, P.R. China.
[Ti] Título:miR-24-3p regulates bladder cancer cell proliferation, migration, invasion and autophagy by targeting DEDD.
[So] Source:Oncol Rep;37(2):1123-1131, 2017 Feb.
[Is] ISSN:1791-2431
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:microRNAs (miRNAs), a class of small non-coding RNA molecules, can regulate gene expression by interacting with the 3'-untranslated regions (3'UTR) of target genes and influence various biological processes. We investigated the potential role of miR-24-3p in the development of bladder cancer by regulating DEDD, a member of the death effector domain-containing protein family. First, we found that miR-24-3p was highly expressed and that DEDD was expressed at a low level in bladder cancer tissues compared with that in adjacent bladder tissues by qRT-PCR (P<0.0001). Second, we found that miR-24-3p promoted the proliferation ability of bladder cancer cells using the MTT assay and colony forming assay; and showed that miR-24-3p accelerated the migration and invasion of bladder cancer cells using migration and invasion assays (P<0.05). Moreover, miR-24-3p inhibited apoptosis of bladder cancer cells, as shown by flow cytometry (P<0.05). Western blot results demonstrated that miR-24-3p participated in autophagy of bladder cancer cells by DEDD. In addition, the tumor formation assay showed that miR-24-3p promoted the growth of bladder tumor in vivo. Furthermore, the luciferase reporter gene assay indicated that miR-24-3p suppressed DEDD gene transcription. Therefore, our study indicated that miR-24-3p promoted bladder cancer progression by inhibiting DEDD.
[Mh] Termos MeSH primário: Autofagia/genética
Proteínas de Ligação a DNA/genética
Proteínas Adaptadoras de Sinalização de Receptores de Domínio de Morte/genética
MicroRNAs/genética
Neoplasias da Bexiga Urinária/patologia
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Animais
Apoptose/genética
Linhagem Celular Tumoral
Movimento Celular/genética
Proliferação Celular/genética
Proteínas de Ligação a DNA/metabolismo
Proteínas Adaptadoras de Sinalização de Receptores de Domínio de Morte/metabolismo
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Camundongos Endogâmicos BALB C
Proteínas Associadas aos Microtúbulos/genética
Proteínas Associadas aos Microtúbulos/metabolismo
Neoplasias da Bexiga Urinária/genética
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (DEDD protein, human); 0 (DNA-Binding Proteins); 0 (Death Domain Receptor Signaling Adaptor Proteins); 0 (MIRN24 microRNA, human); 0 (MicroRNAs); 0 (Microtubule-Associated Proteins); 0 (light chain 3, human)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170323
[Lr] Data última revisão:
170323
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161222
[St] Status:MEDLINE
[do] DOI:10.3892/or.2016.5326


  9 / 431 MEDLINE  
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[PMID]:27810922
[Au] Autor:Zinngrebe J; Rieser E; Taraborrelli L; Peltzer N; Hartwig T; Ren H; Kovács I; Endres C; Draber P; Darding M; von Karstedt S; Lemke J; Dome B; Bergmann M; Ferguson BJ; Walczak H
[Ad] Endereço:Centre for Cell Death, Cancer, and Inflammation, UCL Cancer Institute, University College London, London WC1E 6DD, England, UK.
[Ti] Título:--LUBAC deficiency perturbs TLR3 signaling to cause immunodeficiency and autoinflammation.
[So] Source:J Exp Med;213(12):2671-2689, 2016 Nov 14.
[Is] ISSN:1540-9538
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The linear ubiquitin chain assembly complex (LUBAC), consisting of SHANK-associated RH-domain-interacting protein (SHARPIN), heme-oxidized IRP2 ubiquitin ligase-1 (HOIL-1), and HOIL-1-interacting protein (HOIP), is a critical regulator of inflammation and immunity. This is highlighted by the fact that patients with perturbed linear ubiquitination caused by mutations in the Hoip or Hoil-1 genes, resulting in knockouts of these proteins, may simultaneously suffer from immunodeficiency and autoinflammation. TLR3 plays a crucial, albeit controversial, role in viral infection and tissue damage. We identify a pivotal role of LUBAC in TLR3 signaling and discover a functional interaction between LUBAC components and TLR3 as crucial for immunity to influenza A virus infection. On the biochemical level, we identify LUBAC components as interacting with the TLR3-signaling complex (SC), thereby enabling TLR3-mediated gene activation. Absence of LUBAC components increases formation of a previously unrecognized TLR3-induced death-inducing SC, leading to enhanced cell death. Intriguingly, excessive TLR3-mediated cell death, induced by double-stranded RNA present in the skin of SHARPIN-deficient chronic proliferative dermatitis mice (cpdm), is a major contributor to their autoinflammatory skin phenotype, as genetic coablation of Tlr3 substantially ameliorated cpdm dermatitis. Thus, LUBAC components control TLR3-mediated innate immunity, thereby preventing development of immunodeficiency and autoinflammation.
[Mh] Termos MeSH primário: Síndromes de Imunodeficiência/metabolismo
Inflamação/patologia
Proteínas do Tecido Nervoso/metabolismo
Transdução de Sinais
Receptor 3 Toll-Like/metabolismo
Fatores de Transcrição/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
[Mh] Termos MeSH secundário: Animais
Morte Celular/efeitos dos fármacos
Proteínas Adaptadoras de Sinalização de Receptores de Domínio de Morte/metabolismo
Dermatite/patologia
Inativação Gênica/efeitos dos fármacos
Interações Hospedeiro-Patógeno/imunologia
Seres Humanos
Inflamação/imunologia
Vírus da Influenza A/efeitos dos fármacos
Vírus da Influenza A/fisiologia
Queratinócitos/efeitos dos fármacos
Queratinócitos/metabolismo
Camundongos
Poli I-C/farmacologia
Transdução de Sinais/efeitos dos fármacos
Receptor 3 Toll-Like/deficiência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Death Domain Receptor Signaling Adaptor Proteins); 0 (Nerve Tissue Proteins); 0 (Toll-Like Receptor 3); 0 (Transcription Factors); 0 (sharpin); EC 2.3.2.27 (RBCK1 protein, human); EC 2.3.2.27 (RNF31 protein, human); EC 2.3.2.27 (Ubiquitin-Protein Ligases); O84C90HH2L (Poly I-C)
[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:161105
[St] Status:MEDLINE


  10 / 431 MEDLINE  
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[PMID]:27746017
[Au] Autor:Fu TM; Li Y; Lu A; Li Z; Vajjhala PR; Cruz AC; Srivastava DB; DiMaio F; Penczek PA; Siegel RM; Stacey KJ; Egelman EH; Wu H
[Ad] Endereço:Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA; Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.
[Ti] Título:Cryo-EM Structure of Caspase-8 Tandem DED Filament Reveals Assembly and Regulation Mechanisms of the Death-Inducing Signaling Complex.
[So] Source:Mol Cell;64(2):236-250, 2016 Oct 20.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Caspase-8 activation can be triggered by death receptor-mediated formation of the death-inducing signaling complex (DISC) and by the inflammasome adaptor ASC. Caspase-8 assembles with FADD at the DISC and with ASC at the inflammasome through its tandem death effector domain (tDED), which is regulated by the tDED-containing cellular inhibitor cFLIP and the viral inhibitor MC159. Here we present the caspase-8 tDED filament structure determined by cryoelectron microscopy. Extensive assembly interfaces not predicted by the previously proposed linear DED chain model were uncovered, and were further confirmed by structure-based mutagenesis in filament formation in vitro and Fas-induced apoptosis and ASC-mediated caspase-8 recruitment in cells. Structurally, the two DEDs in caspase-8 use quasi-equivalent contacts to enable assembly. Using the tDED filament structure as a template, structural analyses reveal the interaction surfaces between FADD and caspase-8 and the distinct mechanisms of regulation by cFLIP and MC159 through comingling and capping, respectively.
[Mh] Termos MeSH primário: Proteína Reguladora de Apoptosis Semelhante a CASP8 e FADD/química
Caspase 8/química
Proteínas Adaptadoras de Sinalização de Receptores de Domínio de Morte/química
Proteína de Domínio de Morte Associada a Fas/química
Proteínas Virais/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Apoptose/efeitos dos fármacos
Sítios de Ligação
Proteínas Adaptadoras de Sinalização CARD
Proteína Reguladora de Apoptosis Semelhante a CASP8 e FADD/genética
Proteína Reguladora de Apoptosis Semelhante a CASP8 e FADD/metabolismo
Caspase 8/genética
Caspase 8/metabolismo
Microscopia Crioeletrônica
Proteínas do Citoesqueleto/química
Proteínas do Citoesqueleto/genética
Proteínas do Citoesqueleto/metabolismo
Proteínas Adaptadoras de Sinalização de Receptores de Domínio de Morte/genética
Proteínas Adaptadoras de Sinalização de Receptores de Domínio de Morte/metabolismo
Domínio Efetor de Morte
Proteína de Domínio de Morte Associada a Fas/genética
Proteína de Domínio de Morte Associada a Fas/metabolismo
Expressão Gênica
Seres Humanos
Células Jurkat
Plasmídeos/química
Plasmídeos/metabolismo
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Transfecção
Proteínas Virais/genética
Proteínas Virais/metabolismo
Receptor fas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CARD Signaling Adaptor Proteins); 0 (CASP8 and FADD-Like Apoptosis Regulating Protein); 0 (Cytoskeletal Proteins); 0 (Death Domain Receptor Signaling Adaptor Proteins); 0 (FADD protein, human); 0 (FAS protein, human); 0 (Fas-Associated Death Domain Protein); 0 (PYCARD protein, human); 0 (Recombinant Fusion Proteins); 0 (Viral Proteins); 0 (fas Receptor); 0 (viral FLIP protein, Molluscum contagiosum virus); EC 3.4.22.- (CASP8 protein, human); EC 3.4.22.- (Caspase 8)
[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:161018
[St] Status:MEDLINE



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