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Pesquisa : D12.776.660.650 [Categoria DeCS]
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  1 / 825 MEDLINE  
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[PMID]:29335463
[Au] Autor:Wang Q; Sun Q; Czajkowsky DM; Shao Z
[Ad] Endereço:Shanghai Center for Systems Biomedicine, Shanghai Jiao Tong University, 200240, Shanghai, China.
[Ti] Título:Sub-kb Hi-C in D. melanogaster reveals conserved characteristics of TADs between insect and mammalian cells.
[So] Source:Nat Commun;9(1):188, 2018 01 15.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Topologically associating domains (TADs) are fundamental elements of the eukaryotic genomic structure. However, recent studies suggest that the insulating complexes, CTCF/cohesin, present at TAD borders in mammals are absent from those in Drosophila melanogaster, raising the possibility that border elements are not conserved among metazoans. Using in situ Hi-C with sub-kb resolution, here we show that the D. melanogaster genome is almost completely partitioned into >4000 TADs, nearly sevenfold more than previously identified. The overwhelming majority of these TADs are demarcated by the insulator complexes, BEAF-32/CP190, or BEAF-32/Chromator, indicating that these proteins may play an analogous role in flies as that of CTCF/cohesin in mammals. Moreover, extended regions previously thought to be unstructured are shown to consist of small contiguous TADs, a property also observed in mammals upon re-examination. Altogether, our work demonstrates that fundamental features associated with the higher-order folding of the genome are conserved from insects to mammals.
[Mh] Termos MeSH primário: Cromatina/ultraestrutura
Mapeamento Cromossômico/métodos
Cromossomos de Insetos/ultraestrutura
Drosophila melanogaster/genética
Genoma de Inseto
Mamíferos/genética
[Mh] Termos MeSH secundário: Animais
Evolução Biológica
Fator de Ligação a CCCTC/genética
Fator de Ligação a CCCTC/metabolismo
Proteínas de Ciclo Celular/genética
Proteínas de Ciclo Celular/metabolismo
Cromatina/química
Montagem e Desmontagem da Cromatina
Proteínas Cromossômicas não Histona/genética
Proteínas Cromossômicas não Histona/metabolismo
Mapeamento Cromossômico/instrumentação
Cromossomos de Insetos/química
Proteínas de Ligação a DNA/genética
Proteínas de Ligação a DNA/metabolismo
Proteínas de Drosophila/genética
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/ultraestrutura
Proteínas do Olho/genética
Proteínas do Olho/metabolismo
Expressão Gênica
Seres Humanos
Proteínas Associadas aos Microtúbulos/genética
Proteínas Associadas aos Microtúbulos/metabolismo
Conformação Molecular
Proteínas Associadas à Matriz Nuclear/genética
Proteínas Associadas à Matriz Nuclear/metabolismo
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (BEAF-32 protein, Drosophila); 0 (CCCTC-Binding Factor); 0 (CP190 protein, Drosophila); 0 (CTCF protein, human); 0 (Cell Cycle Proteins); 0 (Chromatin); 0 (Chromosomal Proteins, Non-Histone); 0 (DNA-Binding Proteins); 0 (Drosophila Proteins); 0 (Eye Proteins); 0 (Microtubule-Associated Proteins); 0 (Nuclear Matrix-Associated Proteins); 0 (Nuclear Proteins); 0 (chromator protein, Drosophila); 0 (cohesins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180117
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02526-9


  2 / 825 MEDLINE  
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[PMID]:29293652
[Au] Autor:Stockum A; Snijders AP; Maertens GN
[Ad] Endereço:Imperial College London, Department of Medicine, Division of Infectious Diseases, Norfolk Place, London, United Kingdom.
[Ti] Título:USP11 deubiquitinates RAE1 and plays a key role in bipolar spindle formation.
[So] Source:PLoS One;13(1):e0190513, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Correct segregation of the mitotic chromosomes into daughter cells is a highly regulated process critical to safeguard genome stability. During M phase the spindle assembly checkpoint (SAC) ensures that all kinetochores are correctly attached before its inactivation allows progression into anaphase. Upon SAC inactivation, the anaphase promoting complex/cyclosome (APC/C) E3 ligase ubiquitinates and targets cyclin B and securin for proteasomal degradation. Here, we describe the identification of Ribonucleic Acid Export protein 1 (RAE1), a protein previously shown to be involved in SAC regulation and bipolar spindle formation, as a novel substrate of the deubiquitinating enzyme (DUB) Ubiquitin Specific Protease 11 (USP11). Lentiviral knock-down of USP11 or RAE1 in U2OS cells drastically reduces cell proliferation and increases multipolar spindle formation. We show that USP11 is associated with the mitotic spindle, does not regulate SAC inactivation, but controls ubiquitination of RAE1 at the mitotic spindle, hereby functionally modulating its interaction with Nuclear Mitotic Apparatus protein (NuMA).
[Mh] Termos MeSH primário: Proteínas Associadas à Matriz Nuclear/metabolismo
Proteínas de Transporte Nucleocitoplasmático/metabolismo
Fuso Acromático
Tioléster Hidrolases/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Proliferação Celular
Técnicas de Silenciamento de Genes
Células HEK293
Seres Humanos
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Ligação Proteica
Especificidade por Substrato
Tioléster Hidrolases/genética
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Intracellular Signaling Peptides and Proteins); 0 (Nuclear Matrix-Associated Proteins); 0 (Nucleocytoplasmic Transport Proteins); 0 (RAE1 protein, human); 0 (SPRY3 protein, human); EC 3.1.2.- (Thiolester Hydrolases); EC 3.1.2.15 (USP11 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:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190513


  3 / 825 MEDLINE  
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[PMID]:29309627
[Au] Autor:Kharade SS; Parekh VI; Agarwal SK
[Ad] Endereço:Metabolic Diseases Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland.
[Ti] Título:Functional Defects From Endocrine Disease-Associated Mutations in HLXB9 and Its Interacting Partner, NONO.
[So] Source:Endocrinology;159(2):1199-1212, 2018 02 01.
[Is] ISSN:1945-7170
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The insulin-secreting pancreatic neuroendocrine tumors, insulinomas, characterized by increased pancreatic islet ß-cell proliferation, express the phosphorylated isoform of the ß-cell differentiation factor HLXB9 that interacts with NONO/p54NRB, a survival factor. Interestingly, two different homozygous germline mutations in HLXB9, p.F248L and p.F272L, were reported in neonatal diabetes, a condition with functional ß-cell deficiency. Also, two somatic heterozygous NONO mutations were found in endocrine-related tumors, p.H146R (parathyroid) and p.R293H (small intestine neuroendocrine tumor). However, the biological consequence of the mutations, and the role of HLXB9-NONO interaction in normal or abnormal ß cells, is not known. Expression, localization, and functional analysis of the clinically relevant HLXB9 and NONO mutants showed that HLXB9/p.F248L mutant localized in the nucleus but lacked phosphorylation, and NONO/p.R293H mutant was structurally impaired. The HLXB9 and NONO mutants retained the ability to interact, and overexpression of wild-type or mutant HXLB9 in MIN6 cells suppressed cell proliferation. To further understand the biological consequence of the HLXB9-NONO interaction, we mapped the NONO-interacting region in HLXB9. An 80-amino acid conserved region of HLXB9 could compete with full-length HLXB9 to interact with NONO; however, in functional assays, nuclear expression of this HLXB9-conserved region in MIN6 cells did not interfere with cell proliferation. Overall, our results highlight the importance of HLXB9 in conditions of ß-cell excess (insulinomas) and in conditions of ß-cell loss or dysfunction (diabetes). Our studies implicate therapeutic strategies for either reducing ß-cell proliferation in insulinomas or alleviating normal ß-cell deficiency in diabetes through the modulation of HLXB9 phosphorylation.
[Mh] Termos MeSH primário: Doenças do Sistema Endócrino/genética
Proteínas de Homeodomínio/genética
Proteínas de Homeodomínio/metabolismo
Proteínas Associadas à Matriz Nuclear/genética
Proteínas Associadas à Matriz Nuclear/metabolismo
Fatores de Transcrição de Octâmero/genética
Fatores de Transcrição de Octâmero/metabolismo
Proteínas de Ligação a RNA/genética
Proteínas de Ligação a RNA/metabolismo
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Diabetes Mellitus/genética
Doenças do Sistema Endócrino/metabolismo
Mutação em Linhagem Germinativa
Seres Humanos
Recém-Nascido
Células Secretoras de Insulina/metabolismo
Células Secretoras de Insulina/patologia
Camundongos
Camundongos Transgênicos
Mutação
Ligação Proteica
Proteínas Proto-Oncogênicas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL
[Nm] Nome de substância:
0 (Homeodomain Proteins); 0 (MNX1 protein, human); 0 (Men1 protein, mouse); 0 (NONO protein, human); 0 (Nuclear Matrix-Associated Proteins); 0 (Octamer Transcription Factors); 0 (Proto-Oncogene Proteins); 0 (RNA-Binding Proteins); 0 (Transcription Factors)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE
[do] DOI:10.1210/en.2017-03155


  4 / 825 MEDLINE  
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[PMID]:28744001
[Au] Autor:Li S; Koe CT; Tay ST; Tan ALK; Zhang S; Zhang Y; Tan P; Sung WK; Wang H
[Ad] Endereço:Neuroscience & Behavioural Disorders Program, Duke-NUS Medical School, 8 College Road, Singapore, 169857, Singapore.
[Ti] Título:An intrinsic mechanism controls reactivation of neural stem cells by spindle matrix proteins.
[So] Source:Nat Commun;8(1):122, 2017 07 25.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The switch between quiescence and proliferation is central for neurogenesis and its alteration is linked to neurodevelopmental disorders such as microcephaly. However, intrinsic mechanisms that reactivate Drosophila larval neural stem cells (NSCs) to exit from quiescence are not well established. Here we show that the spindle matrix complex containing Chromator (Chro) functions as a key intrinsic regulator of NSC reactivation downstream of extrinsic insulin/insulin-like growth factor signalling. Chro also prevents NSCs from ire-entering quiescence at later stages. NSC-specific in vivo profiling has dentified many downstream targets of Chro, including a temporal transcription factor Grainy head (Grh) and a neural stem cell quiescence-inducing factor Prospero (Pros). We show that spindle matrix proteins promote the expression of Grh and repress that of Pros in NSCs to govern their reactivation. Our data demonstrate that nuclear Chro critically regulates gene expression in NSCs at the transition from quiescence to proliferation.The spindle matrix proteins, including Chro, are known to regulate mitotic spindle assembly in the cytoplasm. Here the authors show that in Drosophila larval brain, Chro promotes neural stem cell (NSC) reactivation and prevents activated NSCs from entering quiescence, and that Chro carries out such a role by regulating the expression of key transcription factors in the nucleus.
[Mh] Termos MeSH primário: Proteínas de Drosophila/genética
Células-Tronco Neurais/metabolismo
Proteínas Associadas à Matriz Nuclear/genética
Fosfoproteínas/genética
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Western Blotting
Proteínas de Ligação a DNA/genética
Proteínas de Ligação a DNA/metabolismo
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/citologia
Drosophila melanogaster/genética
Drosophila melanogaster/metabolismo
Perfilação da Expressão Gênica/métodos
Larva/citologia
Larva/genética
Larva/metabolismo
Microscopia Confocal
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
Proteínas Associadas à Matriz Nuclear/metabolismo
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Fosfoproteínas/metabolismo
Interferência de RNA
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Drosophila Proteins); 0 (EAST protein, Drosophila); 0 (Nerve Tissue Proteins); 0 (Nuclear Matrix-Associated Proteins); 0 (Nuclear Proteins); 0 (Phosphoproteins); 0 (Transcription Factors); 0 (chromator protein, Drosophila); 0 (grh protein, Drosophila); 0 (megator protein, Drosophila); 0 (pros protein, Drosophila)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-00172-9


  5 / 825 MEDLINE  
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[PMID]:28977530
[Au] Autor:Banerjee A; Vest KE; Pavlath GK; Corbett AH
[Ad] Endereço:Department of Biology, Emory University, Atlanta, GA 30322, USA.
[Ti] Título:Nuclear poly(A) binding protein 1 (PABPN1) and Matrin3 interact in muscle cells and regulate RNA processing.
[So] Source:Nucleic Acids Res;45(18):10706-10725, 2017 Oct 13.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The polyadenylate binding protein 1 (PABPN1) is a ubiquitously expressed RNA binding protein vital for multiple steps in RNA metabolism. Although PABPN1 plays a critical role in the regulation of RNA processing, mutation of the gene encoding this ubiquitously expressed RNA binding protein causes a specific form of muscular dystrophy termed oculopharyngeal muscular dystrophy (OPMD). Despite the tissue-specific pathology that occurs in this disease, only recently have studies of PABPN1 begun to explore the role of this protein in skeletal muscle. We have used co-immunoprecipitation and mass spectrometry to identify proteins that interact with PABPN1 in mouse skeletal muscles. Among the interacting proteins we identified Matrin 3 (MATR3) as a novel protein interactor of PABPN1. The MATR3 gene is mutated in a form of distal myopathy and amyotrophic lateral sclerosis (ALS). We demonstrate, that like PABPN1, MATR3 is critical for myogenesis. Furthermore, MATR3 controls critical aspects of RNA processing including alternative polyadenylation and intron retention. We provide evidence that MATR3 also binds and regulates the levels of long non-coding RNA (lncRNA) Neat1 and together with PABPN1 is required for normal paraspeckle function. We demonstrate that PABPN1 and MATR3 are required for paraspeckles, as well as for adenosine to inosine (A to I) RNA editing of Ctn RNA in muscle cells. We provide a functional link between PABPN1 and MATR3 through regulation of a common lncRNA target with downstream impact on paraspeckle morphology and function. We extend our analysis to a mouse model of OPMD and demonstrate altered paraspeckle morphology in the presence of endogenous levels of alanine-expanded PABPN1. In this study, we report protein-binding partners of PABPN1, which could provide insight into novel functions of PABPN1 in skeletal muscle and identify proteins that could be sequestered with alanine-expanded PABPN1 in the nuclear aggregates found in OPMD.
[Mh] Termos MeSH primário: Músculo Esquelético/metabolismo
Proteínas Associadas à Matriz Nuclear/metabolismo
Proteína I de Ligação a Poli(A)/metabolismo
Processamento Pós-Transcricional do RNA
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Seres Humanos
Camundongos Endogâmicos C57BL
Desenvolvimento Muscular
Proteína I de Ligação a Poli(A)/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nuclear Matrix-Associated Proteins); 0 (PABPN1 protein, human); 0 (PABPN1 protein, mouse); 0 (Poly(A)-Binding Protein I); 0 (RNA-Binding Proteins); 0 (matrin-3 protein, mouse)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171005
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx786


  6 / 825 MEDLINE  
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[PMID]:28867566
[Au] Autor:Jung YD; Lee HE; Jo A; Hiroo I; Cha HJ; Kim HS
[Ad] Endereço:Biotherapeutics Translational Research Center, Korea Research Institute of Bioscience & Biotechnology, Daejeon 34141, Republic of Korea.
[Ti] Título:Activity analysis of LTR12C as an effective regulatory element of the RAE1 gene.
[So] Source:Gene;634:22-28, 2017 Nov 15.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Ribonucleic acid export 1 (RAE1) plays an important role in the export of mature mRNAs from the nucleus to the cytoplasm. Long terminal repeats (LTRs) became integrated into the human genome during primate evolution. One such repeat element, LTR12C, lies within a predicted regulatory region located upstream of the RAE1 gene. We examined the transcriptional activity of LTR12C by using the luciferase assay, and showed that the tandem repeat region (TRR) located within LTR12C was required for its regulatory function. A bioinformatics analysis revealed that the LTR12C element had multiple transcription factor binding sites specific for nuclear transcription factor Y (NF-Y), and the promoter activity of LTR12C was significantly decreased after NF-Y knockdown. Additionally, we discovered novel data indicating that LTR12C was initially inserted into the gorilla genome. Taken together, our results reveal that the TRR of LTR12C has powerful regulatory activity due to its NF-Y binding sites, and the integration of the LTR12C element into the primate genome during evolution may have affected RAE1 transcription.
[Mh] Termos MeSH primário: Fator de Ligação a CCAAT/metabolismo
Gorilla gorilla/genética
Proteínas Associadas à Matriz Nuclear/metabolismo
Proteínas de Transporte Nucleocitoplasmático/metabolismo
Sequências Repetidas Terminais
[Mh] Termos MeSH secundário: Células A549
Animais
Sítios de Ligação
Linhagem Celular
Evolução Molecular
Regulação da Expressão Gênica
Células HCT116
Células HEK293
Células Hep G2
Seres Humanos
Regiões Promotoras Genéticas
Sequências de Repetição em Tandem
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CCAAT-Binding Factor); 0 (Nuclear Matrix-Associated Proteins); 0 (Nucleocytoplasmic Transport Proteins); 0 (RAE1 protein, human); 0 (Transcription Factors); 0 (nuclear factor Y)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170905
[St] Status:MEDLINE


  7 / 825 MEDLINE  
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[PMID]:28846091
[Au] Autor:Jiang L; Shao C; Wu QJ; Chen G; Zhou J; Yang B; Li H; Gou LT; Zhang Y; Wang Y; Yeo GW; Zhou Y; Fu XD
[Ad] Endereço:State Key Laboratory of Virology and Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan, China.
[Ti] Título:NEAT1 scaffolds RNA-binding proteins and the Microprocessor to globally enhance pri-miRNA processing.
[So] Source:Nat Struct Mol Biol;24(10):816-824, 2017 Oct.
[Is] ISSN:1545-9985
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:MicroRNA (miRNA) biogenesis is known to be modulated by a variety of RNA-binding proteins (RBPs), but in most cases, individual RBPs appear to influence the processing of a small subset of target miRNAs. Here, we report that the RNA-binding NONO-PSF heterodimer binds a large number of expressed pri-miRNAs in HeLa cells to globally enhance pri-miRNA processing by the Drosha-DGCR8 Microprocessor. NONO and PSF are key components of paraspeckles organized by the long noncoding RNA (lncRNA) NEAT1. We further demonstrate that NEAT1 also has a profound effect on global pri-miRNA processing. Mechanistic dissection reveals that NEAT1 broadly interacts with the NONO-PSF heterodimer as well as many other RBPs and that multiple RNA segments in NEAT1, including a 'pseudo pri-miRNA' near its 3' end, help attract the Microprocessor. These findings suggest a 'bird nest' model in which an lncRNA orchestrates efficient processing of potentially an entire class of small noncoding RNAs in the nucleus.
[Mh] Termos MeSH primário: MicroRNAs/metabolismo
Proteínas Associadas à Matriz Nuclear/metabolismo
Fatores de Transcrição de Octâmero/metabolismo
Fator de Processamento Associado a PTB/metabolismo
Processamento Pós-Transcricional do RNA
RNA Longo não Codificante/metabolismo
Proteínas de Ligação a RNA/metabolismo
Ribonuclease III/metabolismo
[Mh] Termos MeSH secundário: Células HeLa
Seres Humanos
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DGCR8 protein, human); 0 (MicroRNAs); 0 (NEAT1 long non-coding RNA, human); 0 (NONO protein, human); 0 (Nuclear Matrix-Associated Proteins); 0 (Octamer Transcription Factors); 0 (PTB-Associated Splicing Factor); 0 (RNA, Long Noncoding); 0 (RNA-Binding Proteins); EC 3.1.26.3 (DROSHA protein, human); EC 3.1.26.3 (Ribonuclease III)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170829
[St] Status:MEDLINE
[do] DOI:10.1038/nsmb.3455


  8 / 825 MEDLINE  
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[PMID]:28739693
[Au] Autor:Konagai A; Yoshimura K; Hazama S; Yamamoto N; Aoki K; Ueno T; Fujioka M; Iijima H; Kato M; Uchida M; Wada T; Inoue M; Asao T; Fuse M; Wada S; Kuramasu A; Kamei R; Takeda S; Yamamoto S; Yoshino S; Oka M; Nagano H
[Ad] Endereço:Department of Gastroenterological, Breast and Endocrine Surgery, Yamaguchi University Graduate School of Medicine, Yamaguchi, Japan.
[Ti] Título:Correlation Between NKG2DL Expression and Antitumor Effect of Protein-bound Polysaccharide-K in Tumor-bearing Mouse Models.
[So] Source:Anticancer Res;37(8):4093-4101, 2017 08.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: We investigated the relationship between the expression of natural killer group 2, member D ligands (NKG2DLs) and the antitumor effects of protein-bound polysaccharide-K (PSK). MATERIALS AND METHODS: PSK was administered to evaluate its effectiveness against tumor growth. The expression of Rae-1 and H60 were analyzed in multiple cell lines. RESULTS: PSK showed the highest antitumor effects in mice implanted with cells expressing neither Rae-1 nor H60. PSK had little antitumor effect in mice implanted with cells expressing both Rae-1 and H60. A correlation between the expression of NKG2DLs and the antitumor effect of PSK was observed. After PSK administration, INF-γ production in CD8 T cells increased in mice with cells expressing neither Rae-1 nor H60, but did not change in mice implanted with cells expressing both Rae-1 and H60. CONCLUSION: We demonstrated that the expression of NKG2DLs affects tumor immunity and the efficacy of immuno therapy in tumor-bearing mouse model.
[Mh] Termos MeSH primário: Proteínas Fúngicas/administração & dosagem
Antígenos de Histocompatibilidade Menor/genética
Subfamília K de Receptores Semelhantes a Lectina de Células NK/genética
Neoplasias/tratamento farmacológico
Proteínas Associadas à Matriz Nuclear/genética
Proteínas de Transporte Nucleocitoplasmático/genética
Polissacarídeos/administração & dosagem
[Mh] Termos MeSH secundário: Animais
Linfócitos T CD8-Positivos/efeitos dos fármacos
Linhagem Celular Tumoral
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Ligantes
Camundongos
Antígenos de Histocompatibilidade Menor/biossíntese
Subfamília K de Receptores Semelhantes a Lectina de Células NK/biossíntese
Neoplasias/genética
Neoplasias/patologia
Proteínas Associadas à Matriz Nuclear/biossíntese
Proteínas de Transporte Nucleocitoplasmático/biossíntese
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (KLRK1 protein, human); 0 (Ligands); 0 (Minor Histocompatibility Antigens); 0 (NK Cell Lectin-Like Receptor Subfamily K); 0 (Nuclear Matrix-Associated Proteins); 0 (Nucleocytoplasmic Transport Proteins); 0 (Polysaccharides); 0 (RAE1 protein, human); 0 (minor H antigen H60); 0 (protein-bound polysaccharide K, Basidiomycetes)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE


  9 / 825 MEDLINE  
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[PMID]:28712728
[Au] Autor:Morchikh M; Cribier A; Raffel R; Amraoui S; Cau J; Severac D; Dubois E; Schwartz O; Bennasser Y; Benkirane M
[Ad] Endereço:Institut de Génétique Humaine, Laboratoire de Virologie Moléculaire, Université de Montpellier, CNRS UMR9002, 34000 Montpellier, France. Electronic address: mehdi.morchikh@igh.cnrs.fr.
[Ti] Título:HEXIM1 and NEAT1 Long Non-coding RNA Form a Multi-subunit Complex that Regulates DNA-Mediated Innate Immune Response.
[So] Source:Mol Cell;67(3):387-399.e5, 2017 Aug 03.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The DNA-mediated innate immune response underpins anti-microbial defenses and certain autoimmune diseases. Here we used immunoprecipitation, mass spectrometry, and RNA sequencing to identify a ribonuclear complex built around HEXIM1 and the long non-coding RNA NEAT1 that we dubbed the HEXIM1-DNA-PK-paraspeckle components-ribonucleoprotein complex (HDP-RNP). The HDP-RNP contains DNA-PK subunits (DNAPKc, Ku70, and Ku80) and paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATRIN3). We show that binding of HEXIM1 to NEAT1 is required for its assembly. We further demonstrate that the HDP-RNP is required for the innate immune response to foreign DNA, through the cGAS-STING-IRF3 pathway. The HDP-RNP interacts with cGAS and its partner PQBP1, and their interaction is remodeled by foreign DNA. Remodeling leads to the release of paraspeckle proteins, recruitment of STING, and activation of DNAPKc and IRF3. Our study establishes the HDP-RNP as a key nuclear regulator of DNA-mediated activation of innate immune response through the cGAS-STING pathway.
[Mh] Termos MeSH primário: DNA/imunologia
Herpesvirus Humano 8/imunologia
Imunidade Inata
RNA Longo não Codificante/imunologia
Proteínas de Ligação a RNA/imunologia
[Mh] Termos MeSH secundário: Proteínas de Ligação ao Cálcio/genética
Proteínas de Ligação ao Cálcio/imunologia
Proteínas de Ligação ao Cálcio/metabolismo
DNA/genética
DNA/metabolismo
Células HEK293
Células HeLa
Interações Hospedeiro-Patógeno
Células Endoteliais da Veia Umbilical Humana/imunologia
Células Endoteliais da Veia Umbilical Humana/metabolismo
Células Endoteliais da Veia Umbilical Humana/virologia
Seres Humanos
Fator Regulador 3 de Interferon/genética
Fator Regulador 3 de Interferon/imunologia
Fator Regulador 3 de Interferon/metabolismo
Peptídeos e Proteínas de Sinalização Intracelular/genética
Peptídeos e Proteínas de Sinalização Intracelular/imunologia
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Autoantígeno Ku/genética
Autoantígeno Ku/imunologia
Autoantígeno Ku/metabolismo
Proteínas de Membrana/genética
Proteínas de Membrana/imunologia
Proteínas de Membrana/metabolismo
Complexos Multiproteicos
Proteínas Associadas à Matriz Nuclear/genética
Proteínas Associadas à Matriz Nuclear/imunologia
Proteínas Associadas à Matriz Nuclear/metabolismo
Proteínas Nucleares/genética
Proteínas Nucleares/imunologia
Proteínas Nucleares/metabolismo
Nucleotidiltransferases/genética
Nucleotidiltransferases/imunologia
Nucleotidiltransferases/metabolismo
Fatores de Transcrição de Octâmero/genética
Fatores de Transcrição de Octâmero/imunologia
Fatores de Transcrição de Octâmero/metabolismo
Fator de Processamento Associado a PTB/genética
Fator de Processamento Associado a PTB/imunologia
Fator de Processamento Associado a PTB/metabolismo
Ligação Proteica
Interferência de RNA
RNA Longo não Codificante/genética
RNA Longo não Codificante/metabolismo
Proteínas de Ligação a RNA/genética
Proteínas de Ligação a RNA/metabolismo
Transdução de Sinais
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CIB1 protein, human); 0 (Calcium-Binding Proteins); 0 (HEXIM1 protein, human); 0 (IRF3 protein, human); 0 (Interferon Regulatory Factor-3); 0 (Intracellular Signaling Peptides and Proteins); 0 (MATR3 protein, human); 0 (MPYS protein, human); 0 (Membrane Proteins); 0 (Multiprotein Complexes); 0 (NEAT1 long non-coding RNA, human); 0 (NONO protein, human); 0 (Nuclear Matrix-Associated Proteins); 0 (Nuclear Proteins); 0 (Octamer Transcription Factors); 0 (PSPC1 protein, human); 0 (PTB-Associated Splicing Factor); 0 (RBM14 protein, human); 0 (RNA, Long Noncoding); 0 (RNA-Binding Proteins); 9007-49-2 (DNA); EC 2.7.7.- (MB21D1 protein, human); EC 2.7.7.- (Nucleotidyltransferases); EC 3.6.4.12 (XRCC5 protein, human); EC 3.6.4.12 (Xrcc6 protein, human); EC 4.2.99.- (Ku Autoantigen)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE


  10 / 825 MEDLINE  
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[PMID]:28637206
[Au] Autor:Shao Y; Hernandez-Buquer S; Childress P; Stayrook KR; Alvarez MB; Davis H; Plotkin LI; He Y; Condon KW; Burr DB; Warden SJ; Robling AG; Yang FC; Wek RC; Allen MR; Bidwell JP
[Ad] Endereço:Department of Medical and Molecular Genetics, Indiana University School of Medicine, Indianapolis, Indiana 46202.
[Ti] Título:Improving Combination Osteoporosis Therapy in a Preclinical Model of Heightened Osteoanabolism.
[So] Source:Endocrinology;158(9):2722-2740, 2017 Sep 01.
[Is] ISSN:1945-7170
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Combining anticatabolic agents with parathyroid hormone (PTH) to enhance bone mass has yielded mixed results in osteoporosis patients. Toward the goal of enhancing the efficacy of these regimens, we tested their utility in combination with loss of the transcription factor Nmp4 because disabling this gene amplifies PTH-induced increases in trabecular bone in mice by boosting osteoblast secretory activity. We addressed whether combining a sustained anabolic response with an anticatabolic results in superior bone acquisition compared with PTH monotherapy. Additionally, we inquired whether Nmp4 interferes with anticatabolic efficacy. Wild-type and Nmp4-/- mice were ovariectomized at 12 weeks of age, followed by therapy regimens, administered from 16 to 24 weeks, and included individually or combined PTH, alendronate (ALN), zoledronate (ZOL), and raloxifene (RAL). Anabolic therapeutic efficacy generally corresponded with PTH + RAL = PTH + ZOL > PTH + ALN = PTH > vehicle control. Loss of Nmp4 enhanced femoral trabecular bone increases under PTH + RAL and PTH + ZOL. RAL and ZOL promoted bone restoration, but unexpectedly, loss of Nmp4 boosted RAL-induced increases in femoral trabecular bone. The combination of PTH, RAL, and loss of Nmp4 significantly increased bone marrow osteoprogenitor number, but did not affect adipogenesis or osteoclastogenesis. RAL, but not ZOL, increased osteoprogenitors in both genotypes. Nmp4 status did not influence bone serum marker responses to treatments, but Nmp4-/- mice as a group showed elevated levels of the bone formation marker osteocalcin. We conclude that the heightened osteoanabolism of the Nmp4-/- skeleton enhances the effectiveness of diverse osteoporosis treatments, in part by increasing hyperanabolic osteoprogenitors. Nmp4 provides a promising target pathway for identifying barriers to pharmacologically induced bone formation.
[Mh] Termos MeSH primário: Osso e Ossos/efeitos dos fármacos
Osso e Ossos/metabolismo
Difosfonatos/administração & dosagem
Imidazóis/administração & dosagem
Osteoporose/tratamento farmacológico
Hormônio Paratireóideo/administração & dosagem
Cloridrato de Raloxifeno/administração & dosagem
[Mh] Termos MeSH secundário: Animais
Reabsorção Óssea/tratamento farmacológico
Reabsorção Óssea/genética
Reabsorção Óssea/metabolismo
Modelos Animais de Doenças
Avaliação Pré-Clínica de Medicamentos
Quimioterapia Combinada
Feminino
Camundongos
Camundongos Knockout
Proteínas Associadas à Matriz Nuclear/genética
Osteoporose/genética
Osteoporose/patologia
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Diphosphonates); 0 (Imidazoles); 0 (Nuclear Matrix-Associated Proteins); 0 (Parathyroid Hormone); 0 (Transcription Factors); 0 (Zfp384 protein, mouse); 4F86W47BR6 (Raloxifene Hydrochloride); 6XC1PAD3KF (zoledronic acid)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171115
[Lr] Data última revisão:
171115
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170623
[St] Status:MEDLINE
[do] DOI:10.1210/en.2017-00355



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