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Pesquisa : E05.196.150.639 [Categoria DeCS]
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  1 / 16727 MEDLINE  
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[PMID]:29339073
[Au] Autor:Roginski RS; Lau CW; Santoiemma PP; Weaver SJ; Du P; Soteropoulos P; Yang J
[Ad] Endereço:Department of Anesthesiology, CMC VA Medical Center, Philadelphia, PA 19104, United States; Department of Anesthesiology and Critical Care, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, United States. Electronic address: raymond.roginski@va.gov.
[Ti] Título:The human GCOM1 complex gene interacts with the NMDA receptor and internexin-alpha.
[So] Source:Gene;648:42-53, 2018 Mar 30.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The known functions of the human GCOM1 complex hub gene include transcription elongation and the intercalated disk of cardiac myocytes. However, in all likelihood, the gene's most interesting, and thus far least understood, roles will be found in the central nervous system. To investigate the functions of the GCOM1 gene in the CNS, we have cloned human and rat brain cDNAs encoding novel, 105 kDa GCOM1 combined (Gcom) proteins, designated Gcom15, and identified a new group of GCOM1 interacting genes, termed Gints, from yeast two-hybrid (Y2H) screens. We showed that Gcom15 interacts with the NR1 subunit of the NMDA receptor by co-expression in heterologous cells, in which we observed bi-directional co-immunoprecipitation of human Gcom15 and murine NR1. Our Y2H screens revealed 27 novel GCOM1 interacting genes, many of which are synaptic proteins and/or play roles in neurologic diseases. Finally, we showed, using rat brain protein preparations, that the Gint internexin-alpha (INA), a known interactor of the NMDAR, co-IPs with GCOM1 proteins, suggesting a GCOM1-GRIN1-INA interaction and a novel pathway that may be relevant to neuroprotection.
[Mh] Termos MeSH primário: Proteínas de Filamentos Intermediários/metabolismo
RNA Polimerase II/metabolismo
Receptores de N-Metil-D-Aspartato/metabolismo
[Mh] Termos MeSH secundário: Adulto
Animais
Encéfalo/metabolismo
Células HEK293
Seres Humanos
Imunoprecipitação
Proteínas de Filamentos Intermediários/genética
Masculino
Camundongos
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
Ligação Proteica
Mapas de Interação de Proteínas
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
RNA Polimerase II/genética
Ratos Wistar
Receptores de N-Metil-D-Aspartato/genética
Técnicas do Sistema de Duplo-Híbrido
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GRIN1 protein, human); 0 (Intermediate Filament Proteins); 0 (NR1 NMDA receptor); 0 (Nerve Tissue Proteins); 0 (POLR2M protein, human); 0 (Protein Subunits); 0 (Receptors, N-Methyl-D-Aspartate); 0 (alpha-internexin); EC 2.7.7.- (RNA Polymerase II)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE


  2 / 16727 MEDLINE  
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[PMID]:29298345
[Au] Autor:Siegel D; Dehn DD; Bokatzian SS; Quinn K; Backos DS; Di Francesco A; Bernier M; Reisdorph N; de Cabo R; Ross D
[Ad] Endereço:Department of Pharmaceutical Sciences, Skaggs School of Pharmacy, University of Colorado Anschutz Medical Campus, Aurora, Colorado, United States of America.
[Ti] Título:Redox modulation of NQO1.
[So] Source:PLoS One;13(1):e0190717, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:NQO1 is a FAD containing NAD(P)H-dependent oxidoreductase that catalyzes the reduction of quinones and related substrates. In cells, NQO1 participates in a number of binding interactions with other proteins and mRNA and these interactions may be influenced by the concentrations of reduced pyridine nucleotides. NAD(P)H can protect NQO1 from proteolytic digestion suggesting that binding of reduced pyridine nucleotides results in a change in NQO1 structure. We have used purified NQO1 to demonstrate the addition of NAD(P)H induces a change in the structure of NQO1; this results in the loss of immunoreactivity to antibodies that bind to the C-terminal domain and to helix 7 of the catalytic core domain. Under normal cellular conditions NQO1 is not immunoprecipitated by these antibodies, however, following treatment with ß-lapachone which caused rapid oxidation of NAD(P)H NQO1 could be readily pulled-down. Similarly, immunostaining for NQO1 was significantly increased in cells following treatment with ß-lapachone demonstrating that under non-denaturing conditions the immunoreactivity of NQO1 is reflective of the NAD(P)+/NAD(P)H ratio. In untreated human cells, regions with high intensity immunostaining for NQO1 co-localize with acetyl α-tubulin and the NAD+-dependent deacetylase Sirt2 on the centrosome(s), the mitotic spindle and midbody during cell division. These data provide evidence that during the centriole duplication cycle NQO1 may provide NAD+ for Sirt2-mediated deacetylation of microtubules. Overall, NQO1 may act as a redox-dependent switch where the protein responds to the NAD(P)+/NAD(P)H redox environment by altering its structure promoting the binding or dissociation of NQO1 with target macromolecules.
[Mh] Termos MeSH primário: NAD(P)H Desidrogenase (Quinona)/metabolismo
[Mh] Termos MeSH secundário: Domínio Catalítico
Linhagem Celular
Eletroforese em Gel de Poliacrilamida
Técnicas de Silenciamento de Genes
Seres Humanos
Imunoprecipitação
Espectrometria de Massas
NAD(P)H Desidrogenase (Quinona)/genética
Naftoquinonas/farmacologia
Eletroforese em Gel de Poliacrilamida Nativa
Oxirredução
RNA Interferente Pequeno/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Naphthoquinones); 0 (RNA, Small Interfering); 4707-32-8 (beta-lapachone); EC 1.6.5.2 (NAD(P)H Dehydrogenase (Quinone)); EC 1.6.5.2 (NQO1 protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180104
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190717


  3 / 16727 MEDLINE  
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[PMID]:29203246
[Au] Autor:Popielarski M; Ponamarczuk H; Stasiak M; Michalec L; Bednarek R; Studzian M; Pulaski L; Swiatkowska M
[Ad] Endereço:Department of Cytobiology and Proteomics, Medical University of Lodz, 6/8 Mazowiecka St., 92-215 Lodz, Poland. Electronic address: marcin.popielarski@umed.lodz.pl.
[Ti] Título:The role of Protein Disulfide Isomerase and thiol bonds modifications in activation of integrin subunit alpha11.
[So] Source:Biochem Biophys Res Commun;495(2):1635-1641, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Integrins belong to a family of transmembrane receptors that mediate cell migration and adhesion to ECM. Extracellular domains of integrin heterodimers contain cysteine-rich regions, which are potential sites of thiol-disulfide exchanges. Rearrangements of extracellular disulfide bonds regulate activation of integrin receptors by promoting transition from an inactive state into a ligand-binding competent state. Modifications of integrin disulfide bonds dependent on oxidation-reduction can be mediated by Protein Disulfide Isomerse (PDI). This paper provides evidences that binding to integrin ligands initiate changes in free thiol pattern on cell surface and that thiol-disulfide exchange mediated by PDI leads to activation of integrin subunit α11. By employing co-immunoprecipitation and confocal microscopy analysis we showed that α11ß1 and PDI create complexes bounded by disulfide bonds. Using surface plasmon resonance we provide biochemical evidence that PDI can interact directly with integrin subunit α11.
[Mh] Termos MeSH primário: Cadeias alfa de Integrinas/química
Cadeias alfa de Integrinas/metabolismo
Isomerases de Dissulfetos de Proteínas/metabolismo
[Mh] Termos MeSH secundário: Adesão Celular
Movimento Celular
Células Cultivadas
Seres Humanos
Imunoprecipitação
Integrina beta1/química
Integrina beta1/metabolismo
Microscopia Confocal
Domínios e Motivos de Interação entre Proteínas
Compostos de Sulfidrila/química
Compostos de Sulfidrila/metabolismo
Ressonância de Plasmônio de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ITGA11 protein, human); 0 (Integrin alpha Chains); 0 (Integrin beta1); 0 (Sulfhydryl Compounds); EC 5.3.4.1 (Protein Disulfide-Isomerases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171206
[St] Status:MEDLINE


  4 / 16727 MEDLINE  
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[PMID]:29293569
[Au] Autor:Ding CJ; Liang LX; Diao S; Su XH; Zhang BY
[Ad] Endereço:State Key Laboratory of Tree Genetics and Breeding, Research Institute of Forestry, Chinese Academy of Forestry, Beijing, China.
[Ti] Título:Genome-wide analysis of day/night DNA methylation differences in Populus nigra.
[So] Source:PLoS One;13(1):e0190299, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:DNA methylation is an important mechanism of epigenetic modification. Methylation changes during stress responses and developmental processes have been well studied; however, their role in plant adaptation to the day/night cycle is poorly understood. In this study, we detected global methylation patterns in leaves of the black poplar Populus nigra 'N46' at 8:00 and 24:00 by methylated DNA immunoprecipitation sequencing (MeDIP-seq). We found 10,027 and 10,242 genes to be methylated in the 8:00 and 24:00 samples, respectively. The methylated genes appeared to be involved in multiple biological processes, molecular functions, and cellular components, suggesting important roles for DNA methylation in poplar cells. Comparing the 8:00 and 24:00 samples, only 440 differentially methylated regions (DMRs) overlapped with genic regions, including 193 hyper- and 247 hypo-methylated DMRs, and may influence the expression of 137 downstream genes. Most hyper-methylated genes were associated with transferase activity, kinase activity, and phosphotransferase activity, whereas most hypo-methylated genes were associated with protein binding, ATP binding, and adenyl ribonucleotide binding, suggesting that different biological processes were activated during the day and night. Our results indicated that methylated genes were prevalent in the poplar genome, but that only a few of these participated in diurnal gene expression regulation.
[Mh] Termos MeSH primário: Ritmo Circadiano
Metilação de DNA
Genoma de Planta
Populus/genética
[Mh] Termos MeSH secundário: Adaptação Fisiológica
Escuridão
Imunoprecipitação
Luz
Folhas de Planta/metabolismo
Populus/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190299


  5 / 16727 MEDLINE  
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[PMID]:28455558
[Au] Autor:O'Connor HF; Huibregtse JM
[Ad] Endereço:Department of Molecular Biosciences, University of Texas at Austin, Austin, TX, 78712, USA.
[Ti] Título:Enzyme-substrate relationships in the ubiquitin system: approaches for identifying substrates of ubiquitin ligases.
[So] Source:Cell Mol Life Sci;74(18):3363-3375, 2017 09.
[Is] ISSN:1420-9071
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Protein ubiquitylation is an important post-translational modification, regulating aspects of virtually every biochemical pathway in eukaryotic cells. Hundreds of enzymes participate in the conjugation and deconjugation of ubiquitin, as well as the recognition, signaling functions, and degradation of ubiquitylated proteins. Regulation of ubiquitylation is most commonly at the level of recognition of substrates by E3 ubiquitin ligases. Characterization of the network of E3-substrate relationships is a major goal and challenge in the field, as this expected to yield fundamental biological insights and opportunities for drug development. There has been remarkable success in identifying substrates for some E3 ligases, in many instances using the standard protein-protein interaction techniques (e.g., two-hybrid screens and co-immunoprecipitations paired with mass spectrometry). However, some E3s have remained refractory to characterization, while others have simply not yet been studied due to the sheer number and diversity of E3s. This review will discuss the range of tools and techniques that can be used for substrate profiling of E3 ligases.
[Mh] Termos MeSH primário: Ubiquitina-Proteína Ligases/metabolismo
Ubiquitina/metabolismo
[Mh] Termos MeSH secundário: Sistemas CRISPR-Cas/genética
Seres Humanos
Imunoprecipitação
Análise Serial de Proteínas
Especificidade por Substrato
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Ubiquitin); EC 2.3.2.27 (Ubiquitin-Protein Ligases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180131
[Lr] Data última revisão:
180131
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE
[do] DOI:10.1007/s00018-017-2529-6


  6 / 16727 MEDLINE  
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[PMID]:29281702
[Au] Autor:Urban JA; Urban JM; Kuzu G; Larschan EN
[Ad] Endereço:Department of Molecular Biology, Cellular Biology and Biochemistry, Brown University, Providence, RI, United States of America.
[Ti] Título:The Drosophila CLAMP protein associates with diverse proteins on chromatin.
[So] Source:PLoS One;12(12):e0189772, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Gaining new insights into gene regulation involves an in-depth understanding of protein-protein interactions on chromatin. A powerful model for studying mechanisms of gene regulation is dosage compensation, a process that targets the X-chromosome to equalize gene expression between XY males and XX females. We previously identified a zinc finger protein in Drosophila melanogaster that plays a sex-specific role in targeting the Male-specific lethal (MSL) dosage compensation complex to the male X-chromosome, called the Chromatin-Linked Adapter for MSL Proteins (CLAMP). More recently, we established that CLAMP has non-sex-specific roles as an essential protein that regulates chromatin accessibility at promoters genome-wide. To identify associations between CLAMP and other factors in both male and female cells, we used two complementary mass spectrometry approaches. We demonstrate that CLAMP associates with the transcriptional regulator complex Negative Elongation Factor (NELF) in both sexes and determine that CLAMP reduces NELF recruitment to several target genes. In sum, we have identified many new CLAMP-associated factors and provide a resource for further study of this little understood essential protein.
[Mh] Termos MeSH primário: Cromatina/metabolismo
Proteínas de Ligação a DNA/metabolismo
Proteínas de Drosophila/metabolismo
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação
Feminino
Imunoprecipitação
Masculino
Ligação Proteica
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CLAMP protein, Drosophila); 0 (Chromatin); 0 (DNA-Binding Proteins); 0 (Drosophila Proteins); 0 (Transcription Factors)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171228
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189772


  7 / 16727 MEDLINE  
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[PMID]:29273565
[Au] Autor:Maier MY; Luks L; Baudendistel OR; Wittmann V; Dietrich DR
[Ad] Endereço:Human and Environmental Toxicology, Department of Biology, University of Konstanz, Germany; Konstanz Research School Chemical Biology (KoRS-CB), University of Konstanz, Germany.
[Ti] Título:Identification of d-amino acid oxidase and propiverine interaction partners and their potential role in the propiverine-mediated nephropathy.
[So] Source:Chem Biol Interact;281:69-80, 2018 Feb 01.
[Is] ISSN:1872-7786
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Propiverine, a frequently-prescribed pharmaceutical for the treatment of symptoms associated with overactive bladder syndrome, provoked massive intranuclear and cytosolic protein inclusions in rat proximal tubule epithelium, primarily consisting of the peroxisomal targeting signal 1 (PTS1) containing protein d-amino acid oxidase (DAAO). As this type of nephropathy was also observed for other drugs, the aim was to determine whether propiverine interferes with trafficking and/or import of peroxisomal proteins. To elucidate this, DAAO- and propiverine-specific interaction partners from human HEK293 and rat WKPT cell lines and rat kidney and liver homogenate were determined using co-immunoprecipitation with subsequent nano-ESI-LC-MS/MS analyses. Corroboration of the role of DAAO- and/or propiverine-specific interaction partners in the drug-induced DAAO accumulation was sought via specific immunofluorescence staining of rat kidney sections from control and propiverine-treated rats. Above analyses demonstrated the interaction of propiverine with several protein classes, foremost peroxisomal proteins (DAAO, MFE2, HAOX2) and proteins of the protein quality control system, i.e. chaperones (HSP70 and DnaJ co-chaperones), proteases and proteasomal proteins (regulatory subunits of the 26S proteasome; Rpn1/2). The immunofluorescence analysis revealed mislocalization of many PTS1-proteins (DAAO, CAT, MFE2, ACOX1, EHHADH) in rat renal sections, strongly suggesting that propiverine primarily binds to PTS1 proteins resulting in the formation of PTS1 but not PTS2 or peroxisomal membrane protein (PMP) accumulations. Moreover, chaperones involved in peroxisomal trafficking (HSC70, DnaJB1) and peroxisomal biogenesis factor proteins (PEX3, PEX5, PEX7), also presented with distinct mislocalization patterns. Concomitantly, an increased number of peroxisomes was observed, suggestive of a compensatory mechanism for the presumably suboptimally functioning peroxisomes. Overall, the data presented suggested that propiverine interacts exclusively with DAAO or with a selected number of PTS1 proteins. The consequence of this interaction is the abrogated trafficking and peroxisomal import of PTS1 proteins concomitant with their nuclear and cytosolic accumulation due to inhibited degradation and imbalanced protein homeostasis.
[Mh] Termos MeSH primário: Aminoácido Oxirredutases/metabolismo
Benzilatos/metabolismo
Nefropatias Diabéticas/etiologia
[Mh] Termos MeSH secundário: 17-Hidroxiesteroide Desidrogenases/metabolismo
Oxirredutases do Álcool/metabolismo
Aminoácido Oxirredutases/química
Aminoácido Oxirredutases/genética
Animais
Benzilatos/química
Benzilatos/toxicidade
Linhagem Celular
Cromatografia Líquida de Alta Pressão
Células HEK293
Seres Humanos
Imunoprecipitação
Rim/metabolismo
Rim/patologia
Fígado/metabolismo
Microscopia Confocal
Chaperonas Moleculares/metabolismo
Proteína Multifuncional do Peroxissomo-2/metabolismo
Receptor 1 de Sinal de Orientação para Peroxissomos/química
Receptor 1 de Sinal de Orientação para Peroxissomos/metabolismo
Transporte Proteico/efeitos dos fármacos
Ratos
Proteínas Recombinantes de Fusão/biossíntese
Proteínas Recombinantes de Fusão/química
Espectrometria de Massas por Ionização por Electrospray
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzilates); 0 (Molecular Chaperones); 0 (Peroxisome-Targeting Signal 1 Receptor); 0 (Recombinant Fusion Proteins); 468GE2241L (propiverine); EC 1.1.- (17-Hydroxysteroid Dehydrogenases); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.119 (Hsd17b4 protein, rat); EC 1.4.- (Amino Acid Oxidoreductases); EC 4.2.1.107 (Peroxisomal Multifunctional Protein-2)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171224
[St] Status:MEDLINE


  8 / 16727 MEDLINE  
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[PMID]:28471449
[Au] Autor:Özata DM; Li X; Lee L; Liu J; Warsito D; Hajeri P; Hultman I; Fotouhi O; Marklund S; Ährlund-Richter L; Juhlin CC; Larsson C; Lui WO
[Ad] Endereço:Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
[Ti] Título:Loss of miR-514a-3p regulation of PEG3 activates the NF-kappa B pathway in human testicular germ cell tumors.
[So] Source:Cell Death Dis;8(5):e2759, 2017 May 04.
[Is] ISSN:2041-4889
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Deregulation of microRNAs (miRNAs) contributes to the development and progression of many cancer types; however, their functions in the pathogenesis of testicular germ cell tumor (TGCT) remain unclear. Here, we determined miRNA expression profiles of TGCTs and normal testes using small RNA sequencing, and identified several deregulated miRNAs in TGCTs, including the miR-506~514 cluster. In functional studies in vitro we demonstrated that miR-514a-3p induced apoptosis through direct regulation of the paternally expressed gene 3 (PEG3), and ectopically expressed PEG3 could rescue the apoptotic effect of miR-514a-3p overexpression. Silencing of PEG3 or miR-514a-3p overexpression reduced nuclear accumulation of p50 and NF-κB reporter activity. Furthermore, PEG3 was co-immunoprecipitated with tumor necrosis factor receptor-associated factor 2 (TRAF2) in TGCT cell lysates. We propose a model of PEG3-mediated activation of NF-κB in TGCT. Loss of miR-514a-3p expression in TGCT increases PEG3 expression that recruits TRAF2 and activates the NF-kappa B pathway, which protects germ cells from apoptosis. Importantly, we observed strong expression of PEG3 and nuclear p50 in the majority of TGCTs (83% and 78%, respectively). In conclusion, our study describes a novel function for miR-514a-3p in TGCT and highlights an unrecognized mechanism of PEG3 regulation and NF-κB activation in TGCT.
[Mh] Termos MeSH primário: Fatores de Transcrição Kruppel-Like/metabolismo
MicroRNAs/metabolismo
NF-kappa B/metabolismo
Neoplasias Embrionárias de Células Germinativas/patologia
Neoplasias Testiculares/patologia
[Mh] Termos MeSH secundário: Antagomirs/metabolismo
Apoptose
Sequência de Bases
Linhagem Celular Tumoral
Metilação de DNA
Seres Humanos
Imunoprecipitação
Fatores de Transcrição Kruppel-Like/antagonistas & inibidores
Fatores de Transcrição Kruppel-Like/genética
Masculino
MicroRNAs/antagonistas & inibidores
MicroRNAs/genética
Subunidade p50 de NF-kappa B/metabolismo
Neoplasias Embrionárias de Células Germinativas/metabolismo
Poli(ADP-Ribose) Polimerases/metabolismo
Regiões Promotoras Genéticas
Interferência de RNA
Alinhamento de Sequência
Transdução de Sinais
Fator 2 Associado a Receptor de TNF/metabolismo
Neoplasias Testiculares/metabolismo
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antagomirs); 0 (Kruppel-Like Transcription Factors); 0 (MicroRNAs); 0 (NF-kappa B); 0 (NF-kappa B p50 Subunit); 0 (PEG3 protein, human); 0 (TNF Receptor-Associated Factor 2); EC 2.4.2.30 (Poly(ADP-ribose) Polymerases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1038/cddis.2016.464


  9 / 16727 MEDLINE  
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[PMID]:29212066
[Au] Autor:Jin X; Nie E; Zhou X; Zeng A; Yu T; Zhi T; Jiang K; Wang Y; Zhang J; You Y
[Ad] Endereço:Department of Neurosurgery, the First Affiliated Hospital of Nanjing Medical University, Nanjing, China.
[Ti] Título:Fstl1 Promotes Glioma Growth Through the BMP4/Smad1/5/8 Signaling Pathway.
[So] Source:Cell Physiol Biochem;44(4):1616-1628, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Gliomas result in the highest morbidity and mortality rates of intracranial primary central nervous system tumors because of their aggressive growth characteristics and high postoperative recurrence. They are characterized by genetic instability, intratumoral histopathological variability and unpredictable clinical behavior in patients. Proliferation is a key aspect of the clinical progression of malignant gliomas, complicating complete surgical resection and enabling tumor regrowth and further proliferation of the surviving tumor cells. METHODS: The expression of Fstl1 was detected by western blotting and qRT-PCR. We used cell proliferation and colony formation assays to measure proliferation. Then, flow cytometry was used to analyze cell cycle progression. The expression of Fstl1, p-Smad1/5/8 and p21 in GBM tissue sections was evaluated using immunohistochemical staining. Furthermore, we used coimmunoprecipitation (Co-IP) and immunoprecipitation to validate the relationship between Fstl1, BMP4 and BMPR2. Finally, we used orthotopic xenograft studies to measure the growth of tumors in vivo. RESULTS: We found that follistatin-like 1 (Fstl1) was upregulated in high-grade glioma specimens and that its levels correlated with poor prognosis. Fstl1 upregulation increased cell proliferation, colony formation and cell cycle progression, while its knockdown inhibited these processes. Moreover, Fstl1 interacted with bone morphogenetic protein (BMP) 4, but not BMP receptor (BMPR) 2, and competitively inhibited their association. Furthermore, Fstl1 overexpression suppressed the activation of the BMP4/Smad1/5/8 signaling pathway, while BMP4 overexpression reversed this effect. CONCLUSION: Our study demonstrated that Fstl1 promoted glioma growth through the BMP4/Smad1/5/8 signaling pathway, and these findings suggest potential new glioblastoma treatment strategies.
[Mh] Termos MeSH primário: Proteína Morfogenética Óssea 4/metabolismo
Neoplasias Encefálicas/patologia
Proteínas Relacionadas à Folistatina/metabolismo
Glioma/patologia
Proteína Smad1/metabolismo
Proteína Smad5/metabolismo
Proteína Smad8/metabolismo
[Mh] Termos MeSH secundário: Animais
Receptores de Proteínas Morfogenéticas Ósseas Tipo II/metabolismo
Neoplasias Encefálicas/metabolismo
Neoplasias Encefálicas/mortalidade
Linhagem Celular Tumoral
Proteínas Relacionadas à Folistatina/antagonistas & inibidores
Proteínas Relacionadas à Folistatina/genética
Glioma/metabolismo
Glioma/mortalidade
Seres Humanos
Imunoprecipitação
Estimativa de Kaplan-Meier
Camundongos
Fosforilação
Ligação Proteica
Interferência de RNA
RNA Interferente Pequeno/metabolismo
Pontos de Checagem da Fase S do Ciclo Celular
Transdução de Sinais
Transplante Heterólogo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bone Morphogenetic Protein 4); 0 (Follistatin-Related Proteins); 0 (RNA, Small Interfering); 0 (Smad1 Protein); 0 (Smad5 Protein); 0 (Smad8 Protein); 158709-61-6 (FSTL1 protein, human); EC 2.7.11.30 (Bone Morphogenetic Protein Receptors, Type II)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE
[do] DOI:10.1159/000485759


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[PMID]:29176328
[Au] Autor:Xie Y; Liu S; Hu S; Wei Y
[Ti] Título:Cardiomyopathy-Associated Gene 1-Sensitive PKC-Dependent Connexin 43 Expression and Phosphorylation in Left Ventricular Noncompaction Cardiomyopathy.
[So] Source:Cell Physiol Biochem;44(2):828-842, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: Cardiomyopathy-associated gene 1 (CMYA1) plays an important role in embryonic cardiac development, postnatal cardiac remodeling and myocardial injury repair. Abnormal CMYA1 expression may be involved in cardiac dysplasia and primary cardiomyopathy. Our study aims to establish the relationship between CMYA1 and Left ventricular noncompaction cardiomyopathy (LVNC) pathogenesis. METHODS: We explored the effects of CMYA1 on connexins (Cx), which contribute to gap junction intercellular communication (GJIC), and the underlying signaling pathway in human normal tissues, LVNC myocardial tissues and HL1 cells by means of western blotting, RT-qPCR, immunohistochemistry, immunofluorescence, co-immunoprecipitation and scrape loading-dye transfer. RESULTS: CMYA1 expression was inversely associated with Cx43 and Cx40 expression, as determined by gap junction PCR array analysis. An increased expression and disordered distribution of CMYA1 at the intercalated discs in LVNC myocardial tissue was also observed. CMYA1 and Cx43 are co-expressed and interact in myocardial cells. CMYA1 expression was positively correlated with p-Cx43 (S368) via the Protein kinase C (PKC) signaling pathway in myocardial tissue and HL1 cells. The diffusion distance of Lucifer Yellow in the HL1 cells in which CMYA1 was over-expressed or knocked down was significantly less or more than that of the control group, respectively. CONCLUSION: Abnormal CMYA1 expression affects the expression and phosphorylation of Cx43 through the PKC signaling pathway, which is involved in the regulation of GJIC. CMYA1 participates in the molecular mechanism of LVNC pathogenesis.
[Mh] Termos MeSH primário: Conexina 43/metabolismo
Proteínas de Ligação a DNA/metabolismo
Proteínas Nucleares/metabolismo
Proteína Quinase C/metabolismo
[Mh] Termos MeSH secundário: Cardiomiopatias/metabolismo
Cardiomiopatias/patologia
Comunicação Celular
Linhagem Celular
Conexina 43/genética
Conexinas/genética
Conexinas/metabolismo
Proteínas de Ligação a DNA/antagonistas & inibidores
Proteínas de Ligação a DNA/genética
Junções Comunicantes/metabolismo
Ventrículos do Coração/fisiopatologia
Seres Humanos
Imuno-Histoquímica
Imunoprecipitação
Microscopia de Fluorescência
Miocárdio/metabolismo
Miocárdio/patologia
Proteínas Nucleares/antagonistas & inibidores
Proteínas Nucleares/genética
Fosforilação
Ligação Proteica
Interferência de RNA
RNA Interferente Pequeno/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Connexin 43); 0 (Connexins); 0 (DNA-Binding Proteins); 0 (Nuclear Proteins); 0 (RNA, Small Interfering); 0 (XIRP1 protein, human); 0 (connexin 40); EC 2.7.11.13 (Protein Kinase C)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1159/000485348



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