Base de dados : MEDLINE
Pesquisa : D12.776.210.500.410 [Categoria DeCS]
Referências encontradas : 556 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 56 ir para página                         

  1 / 556 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28465353
[Au] Autor:Borlepawar A; Rangrez AY; Bernt A; Christen L; Sossalla S; Frank D; Frey N
[Ad] Endereço:From the Department of Internal Medicine III (Cardiology, Angiology, Intensive Care), University Medical Center Kiel and.
[Ti] Título:TRIM24 protein promotes and TRIM32 protein inhibits cardiomyocyte hypertrophy via regulation of dysbindin protein levels.
[So] Source:J Biol Chem;292(24):10180-10196, 2017 06 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We have previously shown that dysbindin is a potent inducer of cardiomyocyte hypertrophy via activation of Rho-dependent serum-response factor (SRF) signaling. We have now performed a yeast two-hybrid screen using dysbindin as bait against a cardiac cDNA library to identify the cardiac dysbindin interactome. Among several putative binding proteins, we identified tripartite motif-containing protein 24 (TRIM24) and confirmed this interaction by co-immunoprecipitation and co-immunostaining. Another tripartite motif (TRIM) family protein, TRIM32, has been reported earlier as an E3 ubiquitin ligase for dysbindin in skeletal muscle. Consistently, we found that TRIM32 also degraded dysbindin in neonatal rat ventricular cardiomyocytes as well. Surprisingly, however, TRIM24 did not promote dysbindin decay but rather protected dysbindin against degradation by TRIM32. Correspondingly, TRIM32 attenuated the activation of SRF signaling and hypertrophy due to dysbindin, whereas TRIM24 promoted these effects in neonatal rat ventricular cardiomyocytes. This study also implies that TRIM32 is a key regulator of cell viability and apoptosis in cardiomyocytes via simultaneous activation of p53 and caspase-3/-7 and inhibition of X-linked inhibitor of apoptosis. In conclusion, we provide here a novel mechanism of post-translational regulation of dysbindin and hypertrophy via TRIM24 and TRIM32 and show the importance of TRIM32 in cardiomyocyte apoptosis .
[Mh] Termos MeSH primário: Cardiomiopatia Dilatada/metabolismo
Cardiomiopatia Hipertrófica/metabolismo
Proteínas de Transporte/metabolismo
Proteínas Associadas à Distrofina/metabolismo
Miócitos Cardíacos/metabolismo
Fator de Resposta Sérica/metabolismo
Fatores de Transcrição/metabolismo
Proteínas com Motivo Tripartido/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
[Mh] Termos MeSH secundário: Animais
Animais Recém-Nascidos
Apoptose
Cardiomiopatia Dilatada/patologia
Cardiomiopatia Hipertrófica/patologia
Proteínas de Transporte/antagonistas & inibidores
Proteínas de Transporte/genética
Células Cultivadas
Disbindina
Proteínas Associadas à Distrofina/química
Proteínas Associadas à Distrofina/genética
Células HEK293
Seres Humanos
Miócitos Cardíacos/citologia
Miócitos Cardíacos/patologia
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Estabilidade Proteica
Proteólise
Interferência de RNA
Ratos
Ratos Wistar
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Fator de Resposta Sérica/agonistas
Fator de Resposta Sérica/antagonistas & inibidores
Fator de Resposta Sérica/genética
Transdução de Sinais
Fatores de Transcrição/antagonistas & inibidores
Fatores de Transcrição/genética
Proteínas com Motivo Tripartido/antagonistas & inibidores
Proteínas com Motivo Tripartido/genética
Ubiquitina-Proteína Ligases/antagonistas & inibidores
Ubiquitina-Proteína Ligases/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (DTNBP1 protein, human); 0 (Dysbindin); 0 (Dystrophin-Associated Proteins); 0 (Peptide Fragments); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 0 (SRF protein, human); 0 (Serum Response Factor); 0 (TRIM24 protein, human); 0 (Transcription Factors); 0 (Tripartite Motif Proteins); EC 2.3.2.27 (TRIM32 protein, human); EC 2.3.2.27 (Ubiquitin-Protein Ligases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171228
[Lr] Data última revisão:
171228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.752543


  2 / 556 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28595731
[Au] Autor:Yete S; Pradhan S; Saranath D
[Ad] Endereço:Department of Biological Sciences, Sunandan Divatia School of Science, NMIMS (deemed-to-be) University, Vile Parle, Mumbai 400056, India.
[Ti] Título:Single nucleotide polymorphisms in an Indian cohort and association of CNTN4, MMP2 and SNTB1 variants with oral cancer.
[So] Source:Cancer Genet;214-215:16-25, 2017 Aug.
[Is] ISSN:2210-7762
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Oral cancer is a high incidence cancer in India primarily due to the prevalent tobacco/areca nut chewing habits and hence a major health concern. India constitutes 26% of the global oral cancer burden. Besides the well-established risk factors, the genomic constitution of an individual plays a role in oral cancer. The aim of the current study was to analyse genomic variants represented as single nucleotide polymorphisms (SNPs), analyse their prevalence and investigate risk association of allelotypes/genotypes to oral cancers. Eleven SNPs in genes associated with biological functions were analysed in an Indian cohort (n = 1000) comprising 500 oral cancer patients and 500 long term tobacco habitués as controls, using Allelic discrimination Real-Time PCR assay with SYBR Green dye. Fisher's exact test and Odds Ratio were used for statistical analysis. Increased risk was observed for rs9849237 CC [P = 0.008; OR 1.412 (1.09-1.82)] and rs243865 CT [P = 0.004; OR 1.469 (1.13-1.90)] genotypes, whereas rs9849237 CT [P = 0.034; OR 0.755 (0.58-0.97)], rs243865 CC [P = 0.002; OR 0.669 (0.51-0.86)] and rs10090787 CC [P = 0.049; OR 0.774 (0.60-0.99)] genotypes indicated decreased risk to oral cancer. The other SNPs showed equidistribution in both groups. Our data indicated genotypes and alleles in specific SNPs rs9849237, rs243865 and rs10090787 with increased/decreased risk to oral cancer.
[Mh] Termos MeSH primário: Contactinas/genética
Proteínas Associadas à Distrofina/genética
Metaloproteinase 2 da Matriz/genética
Neoplasias Bucais/genética
Polimorfismo de Nucleotídeo Único
[Mh] Termos MeSH secundário: Estudos de Coortes
Contactinas/fisiologia
Proteínas Associadas à Distrofina/fisiologia
Predisposição Genética para Doença
Genótipo
Seres Humanos
Índia
Metaloproteinase 2 da Matriz/fisiologia
Razão de Chances
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CNTN4 protein, human); 0 (Contactins); 0 (Dystrophin-Associated Proteins); 0 (syntrophin); EC 3.4.24.24 (MMP2 protein, human); EC 3.4.24.24 (Matrix Metalloproteinase 2)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170815
[Lr] Data última revisão:
170815
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170610
[St] Status:MEDLINE


  3 / 556 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28576874
[Au] Autor:Monis WJ; Faundez V; Pazour GJ
[Ad] Endereço:Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA.
[Ti] Título:BLOC-1 is required for selective membrane protein trafficking from endosomes to primary cilia.
[So] Source:J Cell Biol;216(7):2131-2150, 2017 Jul 03.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Primary cilia perceive the extracellular environment through receptors localized in the ciliary membrane, but mechanisms directing specific proteins to this domain are poorly understood. To address this question, we knocked down proteins potentially important for ciliary membrane targeting and determined how this affects the ciliary trafficking of fibrocystin, polycystin-2, and smoothened. Our analysis showed that fibrocystin and polycystin-2 are dependent on IFT20, GMAP210, and the exocyst complex, while smoothened delivery is largely independent of these components. In addition, we found that polycystin-2, but not smoothened or fibrocystin, requires the biogenesis of lysosome-related organelles complex-1 (BLOC-1) for ciliary delivery. Consistent with the role of BLOC-1 in sorting from the endosome, we find that disrupting the recycling endosome reduces ciliary polycystin-2 and causes its accumulation in the recycling endosome. This is the first demonstration of a role for BLOC-1 in ciliary assembly and highlights the complexity of pathways taken to the cilium.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Membrana Celular/metabolismo
Endossomos/metabolismo
Lectinas/metabolismo
Canais de Cátion TRPP/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Transporte/genética
Cílios/metabolismo
Disbindina
Proteínas Associadas à Distrofina/genética
Proteínas Associadas à Distrofina/metabolismo
Seres Humanos
Lectinas/genética
Camundongos Endogâmicos C57BL
Camundongos Knockout
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Transporte Proteico
Interferência de RNA
Ratos
Receptores de Superfície Celular/metabolismo
Receptor Smoothened/metabolismo
Fatores de Tempo
Transfecção
Proteínas de Transporte Vesicular/genética
Proteínas de Transporte Vesicular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Dtnbp1 protein, mouse); 0 (Dysbindin); 0 (Dystrophin-Associated Proteins); 0 (Exo70 protein, mouse); 0 (Ift20 protein, mouse); 0 (Lectins); 0 (Nuclear Proteins); 0 (Pkhd1 protein, mouse); 0 (Pldn protein, mouse); 0 (Receptors, Cell Surface); 0 (Smo protein, mouse); 0 (Smoothened Receptor); 0 (TRIP11 protein, mouse); 0 (TRPP Cation Channels); 0 (Vesicular Transport Proteins); 0 (polycystic kidney disease 2 protein)
[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:170604
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201611138


  4 / 556 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28317021
[Au] Autor:Chen X; Ma W; Zhang S; Paluch J; Guo W; Dickman DK
[Ad] Endereço:Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089; Neuroscience Graduate Program, University of Southern California, Los Angeles, CA 90089.
[Ti] Título:The BLOC-1 Subunit Pallidin Facilitates Activity-Dependent Synaptic Vesicle Recycling.
[So] Source:eNeuro;4(1), 2017 Jan-Feb.
[Is] ISSN:2373-2822
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Membrane trafficking pathways must be exquisitely coordinated at synaptic terminals to maintain functionality, particularly during conditions of high activity. We have generated null mutations in the homolog of pallidin, a central subunit of the biogenesis of lysosome-related organelles complex-1 (BLOC-1), to determine its role in synaptic development and physiology. We find that Pallidin localizes to presynaptic microtubules and cytoskeletal structures, and that the stability of Pallidin protein is highly dependent on the BLOC-1 components Dysbindin and Blos1. We demonstrate that the rapidly recycling vesicle pool is not sustained during high synaptic activity in pallidin mutants, leading to accelerated rundown and slowed recovery. Following intense activity, we observe a loss of early endosomes and a concomitant increase in tubular endosomal structures in synapses without Pallidin. Together, our data reveal that Pallidin subserves a key role in promoting efficient synaptic vesicle recycling and re-formation through early endosomes during sustained activity.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Endocitose/fisiologia
Proteínas Associadas aos Microtúbulos/metabolismo
Transmissão Sináptica/fisiologia
Vesículas Sinápticas/metabolismo
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Drosophila
Proteínas de Drosophila/genética
Disbindina
Proteínas Associadas à Distrofina/metabolismo
Endossomos/metabolismo
Proteínas do Olho/metabolismo
Homeostase/fisiologia
Immunoblotting
Imuno-Histoquímica
Microscopia Eletrônica
Proteínas Associadas aos Microtúbulos/genética
Microtúbulos/metabolismo
Junção Neuromuscular/metabolismo
Junção Neuromuscular/ultraestrutura
Biogênese de Organelas
Técnicas de Patch-Clamp
Estabilidade Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BLOS1 protein, Drosophila); 0 (Drosophila Proteins); 0 (Dysbindin); 0 (Dystrophin-Associated Proteins); 0 (Eye Proteins); 0 (Microtubule-Associated Proteins); 0 (dysbindin protein, Drosophila); 0 (pallidin protein, Drosophila)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170321
[St] Status:MEDLINE


  5 / 556 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28259707
[Au] Autor:Bryan MM; Tolman NJ; Simon KL; Huizing M; Hufnagel RB; Brooks BP; Speransky V; Mullikin JC; Gahl WA; Malicdan MC; Gochuico BR
[Ad] Endereço:Medical Genetics Branch, National Human Genome Research Institute, National Institutes of Health, 10 Center Drive, Bethesda, MD 20892, USA.
[Ti] Título:Clinical and molecular phenotyping of a child with Hermansky-Pudlak syndrome-7, an uncommon genetic type of HPS.
[So] Source:Mol Genet Metab;120(4):378-383, 2017 Apr.
[Is] ISSN:1096-7206
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PURPOSE: Hermansky-Pudlak syndrome (HPS) is a rare inherited disorder with ten reported genetic types; each type has defects in subunits of either Adaptor Protein-3 complex or Biogenesis of Lysosome-related Organelles Complex (BLOC)-1, -2, or -3. Very few patients with BLOC-1 deficiency (HPS-7, -8, and -9 types) have been diagnosed. We report results of comprehensive clinical testing and molecular analyses of primary fibroblasts from a new case of HPS-7. RESULTS: A 6-year old Paraguayan male presented with hypopigmentation, ocular albinism, nystagmus, reduced visual acuity, and easy bruising. He also experienced delayed motor and language development as a very young child; head and chest trauma resulted in intracranial hemorrhage with subsequent right hemiparesis and lung scarring. There was no clinical evidence of immunodeficiency or colitis. Whole mount transmission electron microscopy revealed absent platelet delta granules; platelet aggregation testing was abnormal. Exome sequencing revealed a homozygous nonsense mutation in the Dystrobrevin binding protein 1 (DTNBP1) gene [NM_032122.4: c.307C>T; p.Gln103*], previously reported in a Portuguese adult. The gene encodes the dysbindin subunit of BLOC-1. Dysbindin protein expression was negligible in our patient's dermal fibroblasts, while his DTNBP1 mRNA level was similar to that of a normal control. CONCLUSIONS: Comprehensive clinical evaluation of the first pediatric case reported with HPS-7 reveals oculocutaneous albinism and platelet storage pool deficiency; his phenotype is consistent with findings in other patients with BLOC-1 disorders. This patient's markedly reduced Dysbindin protein expression in HPS-7 resulted from a mechanism other than nonsense mediated decay.
[Mh] Termos MeSH primário: Códon sem Sentido
Proteínas Associadas à Distrofina/genética
Síndrome de Hermanski-Pudlak/patologia
[Mh] Termos MeSH secundário: Criança
Disbindina
Proteínas Associadas à Distrofina/metabolismo
Exoma
Síndrome de Hermanski-Pudlak/genética
Síndrome de Hermanski-Pudlak/metabolismo
Seres Humanos
Masculino
Análise de Sequência de DNA
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon, Nonsense); 0 (DTNBP1 protein, human); 0 (Dysbindin); 0 (Dystrophin-Associated Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170306
[St] Status:MEDLINE


  6 / 556 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28234977
[Au] Autor:Die JV; Baldwin RL; Rowland LJ; Li R; Oh S; Li C; Connor EE; Ranilla MJ
[Ad] Endereço:Genetic Improvement of Fruits and Vegetables Laboratory, US Department of Agriculture, Agricultural Research Service, Beltsville, Maryland, United States of America.
[Ti] Título:Selection of internal reference genes for normalization of reverse transcription quantitative polymerase chain reaction (RT-qPCR) analysis in the rumen epithelium.
[So] Source:PLoS One;12(2):e0172674, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The rumen is lined on the luminal side by a stratified squamous epithelium that is responsible for not only absorption, but also transport, extensive short-chain fatty acid (SCFA) metabolism and protection. Butyrate has been demonstrated to initiate the differentiation of the tissue following introduction of solid feed to the weaning neonate as well as affecting the metabolism of other nutrients and absorption of nutrients in in vitro experiments. The objective of the present study was to validate expression stability of eight putative reference genes bovine rumen, considering the intrinsic heterogeneity of bovine rumen with regard to different luminal characteristics due to direct infusion of butyrate to double the intra-ruminal content of the rumen liquor. Our focus was on identifying stable reference genes which are suitable to normalize real-time RT-qPCR experiments from rumen samples collected from clinical assays, irrespective of localization within the organ and the across physiological state. The most stably expressed genes included: ACTB, UXT, DBNDD2, RPS9, DDX54 and HMBS. Their high stability values suggest these reference genes will facilitate better evaluation of variation of across an array of conditions including: localization within the rumen, differences among cattle fed an array of rations, as well as response to development in the weaning animal. Moreover, we anticipate these reference genes may be useful for expression studies in other ruminants.
[Mh] Termos MeSH primário: Butiratos/farmacologia
Epitélio/metabolismo
Absorção Gastrointestinal/genética
Genes Essenciais
Reação em Cadeia da Polimerase em Tempo Real/normas
Rúmen/metabolismo
[Mh] Termos MeSH secundário: Actinas/genética
Actinas/metabolismo
Animais
Butiratos/metabolismo
Bovinos
RNA Helicases DEAD-box/genética
RNA Helicases DEAD-box/metabolismo
Proteínas Associadas à Distrofina/genética
Proteínas Associadas à Distrofina/metabolismo
Epitélio/efeitos dos fármacos
Epitélio/crescimento & desenvolvimento
Feminino
Regulação da Expressão Gênica no Desenvolvimento
Hidroximetilbilano Sintase/genética
Hidroximetilbilano Sintase/metabolismo
Padrões de Referência
Proteínas Ribossômicas/genética
Proteínas Ribossômicas/metabolismo
Rúmen/efeitos dos fármacos
Rúmen/crescimento & desenvolvimento
Desmame
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Butyrates); 0 (Dystrophin-Associated Proteins); 0 (Ribosomal Proteins); 0 (ribosomal protein S9); EC 2.5.1.61 (Hydroxymethylbilane Synthase); EC 3.6.4.13 (DEAD-box RNA Helicases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170821
[Lr] Data última revisão:
170821
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170225
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0172674


  7 / 556 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27889377
[Au] Autor:Li N; Tang Y; Liu B; Cong W; Liu C; Xiao J
[Ad] Endereço:Department of Oral Pathology, College of Stomatology, Dalian Medical University, Dalian, Liaoning 116044, China.
[Ti] Título:Retinoid acid-induced microRNA-27b-3p impairs C2C12 myoblast proliferation and differentiation by suppressing α-dystrobrevin.
[So] Source:Exp Cell Res;350(2):301-311, 2017 Jan 15.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We previously reported that excess retinoic acid (RA) resulted in hypoplastic and derangement of myofilaments in embryonic tongue by inhibiting myogenic proliferation and differentiation through CamKIID pathway. Our further studies revealed that the expression of a series of miRNAs was altered by RA administration in embryonic tongue as well as in C2C12 cells. Thus, if excess RA impairs myogenic proliferation and differentiation through miRNAs is taken into account. In present study, miR-27b-3p was found up-regulated in RA-treated C2C12 cells as in embryonic tongue, and predicted to target the 3'UTR of α-dystrobrevin (DTNA). Luciferase reporter assays confirmed the direct interaction between miR-27b-3p and the 3'UTR of DTNA. MiR-27b-3p mimics recapitulated the RA repression on DTNA expression, C2C12 proliferation and differentiation, while the miR-27b-3p inhibitor circumvented these defects resulting from excess RA. As expected, the effects of siDTNA on C2C12 were coincided with those by RA treatment or miR-27b-3p mimics. Therefore, these findings indicated that excess RA inhibited the myoblast proliferation and differentiation by up-regulating miR-27b-3p to target DTNA, which implied a new mechanism in myogenic hypoplasia.
[Mh] Termos MeSH primário: Diferenciação Celular
Proliferação Celular
Proteínas Associadas à Distrofina/metabolismo
MicroRNAs/genética
Mioblastos/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Proteínas Associadas à Distrofina/genética
Camundongos
Desenvolvimento Muscular
Mioblastos/citologia
Mioblastos/efeitos dos fármacos
Mioblastos/fisiologia
Língua/efeitos dos fármacos
Língua/embriologia
Língua/metabolismo
Tretinoína/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dystrophin-Associated Proteins); 0 (MicroRNAs); 0 (Mirn27 microRNA, mouse); 0 (dystrobrevin); 5688UTC01R (Tretinoin)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170518
[Lr] Data última revisão:
170518
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161128
[St] Status:MEDLINE


  8 / 556 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27330059
[Au] Autor:Zhang W; Daly KM; Liang B; Zhang L; Li X; Li Y; Lin DT
[Ad] Endereço:Intramural Research Program, National Institute on Drug Abuse, National Institutes of Health, 333 Cassell Drive, Baltimore, MD 21224, USA.
[Ti] Título:BDNF rescues prefrontal dysfunction elicited by pyramidal neuron-specific DTNBP1 deletion in vivo.
[So] Source:J Mol Cell Biol;9(2):117-131, 2017 Apr 01.
[Is] ISSN:1759-4685
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dystrobrevin-binding protein 1 (Dtnbp1) is one of the earliest identified schizophrenia susceptibility genes. Reduced expression of DTNBP1 is commonly found in brain areas of schizophrenic patients. Dtnbp1-null mutant mice exhibit abnormalities in behaviors and impairments in neuronal activities. However, how diminished DTNBP1 expression contributes to clinical relevant features of schizophrenia remains to be illustrated. Here, using a conditional Dtnbp1 knockout mouse line, we identified an in vivo schizophrenia-relevant function of DTNBP1 in pyramidal neurons of the medial prefrontal cortex (mPFC). We demonstrated that DTNBP1 elimination specifically in pyramidal neurons of the mPFC impaired mouse pre-pulse inhibition (PPI) behavior and reduced perisomatic GABAergic synapses. We further revealed that loss of DTNBP1 in pyramidal neurons diminished activity-dependent secretion of brain-derived neurotrophic factor (BDNF). Finally, we showed that chronic BDNF infusion in the mPFC fully rescued both GABAergic synaptic dysfunction and PPI behavioral deficit induced by DTNBP1 elimination from pyramidal neurons. Our findings highlight brain region- and cell type-specific functions of DTNBP1 in the pathogenesis of schizophrenia, and underscore BDNF restoration as a potential therapeutic strategy for schizophrenia.
[Mh] Termos MeSH primário: Fator Neurotrófico Derivado do Encéfalo/metabolismo
Proteínas Associadas à Distrofina/metabolismo
Deleção de Genes
Córtex Pré-Frontal/fisiopatologia
Células Piramidais/metabolismo
[Mh] Termos MeSH secundário: Animais
Comportamento Animal
Dependovirus
Disbindina
Potenciais Pós-Sinápticos Excitadores
Proteínas de Fluorescência Verde/metabolismo
Potenciais Pós-Sinápticos Inibidores
Integrases/metabolismo
Masculino
Camundongos
Especificidade de Órgãos
Inibição Pré-Pulso
Ácido gama-Aminobutírico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Brain-Derived Neurotrophic Factor); 0 (Dtnbp1 protein, mouse); 0 (Dysbindin); 0 (Dystrophin-Associated Proteins); 0 (enhanced green fluorescent protein); 147336-22-9 (Green Fluorescent Proteins); 56-12-2 (gamma-Aminobutyric Acid); EC 2.7.7.- (Cre recombinase); EC 2.7.7.- (Integrases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160623
[St] Status:MEDLINE
[do] DOI:10.1093/jmcb/mjw029


  9 / 556 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27927957
[Au] Autor:Gokhale A; Hartwig C; Freeman AH; Das R; Zlatic SA; Vistein R; Burch A; Carrot G; Lewis AF; Nelms S; Dickman DK; Puthenveedu MA; Cox DN; Faundez V
[Ad] Endereço:Department of Cell Biology and agokhal@emory.edu vfaunde@emory.edu.
[Ti] Título:The Proteome of BLOC-1 Genetic Defects Identifies the Arp2/3 Actin Polymerization Complex to Function Downstream of the Schizophrenia Susceptibility Factor Dysbindin at the Synapse.
[So] Source:J Neurosci;36(49):12393-12411, 2016 Dec 07.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proteome modifications downstream of monogenic or polygenic disorders have the potential to uncover novel molecular mechanisms participating in pathogenesis and/or extragenic modification of phenotypic expression. We tested this idea by determining the proteome sensitive to genetic defects in a locus encoding dysbindin, a protein required for synapse biology and implicated in schizophrenia risk. We applied quantitative mass spectrometry to identify proteins expressed in neuronal cells the abundance of which was altered after downregulation of the schizophrenia susceptibility factor dysbindin (Bloc1s8) or two other dysbindin-interacting polypeptides, which assemble into the octameric biogenesis of lysosome-related organelles complex 1 (BLOC-1). We found 491 proteins sensitive to dysbindin and BLOC-1 loss of function. Gene ontology of these 491 proteins singled out the actin cytoskeleton and the actin polymerization factor, the Arp2/3 complex, as top statistical molecular pathways contained within the BLOC-1-sensitive proteome. Subunits of the Arp2/3 complex were downregulated by BLOC-1 loss of function, thus affecting actin dynamics in early endosomes of BLOC-1-deficient cells. Furthermore, we demonstrated that Arp2/3, dysbindin, and subunits of the BLOC-1 complex biochemically and genetically interact, modulating Drosophila melanogaster synapse morphology and homeostatic synaptic plasticity. Our results indicate that ontologically prioritized proteomics identifies novel pathways that modify synaptic phenotypes associated with neurodevelopmental disorder gene defects. SIGNIFICANCE STATEMENT: The mechanisms associated with schizophrenia are mostly unknown despite the increasing number of genetic loci identified that increase disease risk. We present an experimental strategy that impartially and comprehensively interrogates the proteome of neurons to identify effects of genetic mutations in a schizophrenia risk factor, dysbindin. We find that the expression of the actin polymerization complex Arp2/3 is reduced in dysbindin-deficient cells, thus affecting actin-dependent phenotypes in two cellular compartments where dysbindin resides, endosomes and presynapses. Our studies indicate that a central cellular structure affected by schizophrenia susceptibility loci is the actin cytoskeleton, an organelle necessary for synaptic function in the presynaptic and postsynaptic compartment.
[Mh] Termos MeSH primário: Proteína 3 Relacionada a Actina/genética
Angiopoietinas/genética
Proteínas de Transporte/genética
Proteínas Associadas à Distrofina/genética
Lectinas/genética
Esquizofrenia/genética
Sinapses
[Mh] Termos MeSH secundário: Actinas/genética
Proteínas Semelhantes a Angiopoietina
Animais
Células Cultivadas
Citoesqueleto/genética
Drosophila melanogaster
Disbindina
Feminino
Células HEK293
Seres Humanos
Camundongos
Camundongos Endogâmicos C57BL
Polimerização
Proteoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actin-Related Protein 3); 0 (Actins); 0 (Actr3 protein, mouse); 0 (Angiopoietin-like Proteins); 0 (Angiopoietins); 0 (Angptl2 protein, mouse); 0 (Carrier Proteins); 0 (Dtnbp1 protein, mouse); 0 (Dysbindin); 0 (Dystrophin-Associated Proteins); 0 (Lectins); 0 (Pldn protein, mouse); 0 (Proteome)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161209
[St] Status:MEDLINE


  10 / 556 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27798936
[Au] Autor:Bakanidze G; Brandl EJ; Hutzler C; Aurass F; Onken S; Rapp MA; Puls I
[Ad] Endereço:Department of Psychiatry and Psychotherapy, Campus Charité Mitte, Charité University Medicine, Berlin, Germany.
[Ti] Título:Association of Dystrobrevin-Binding Protein 1 Polymorphisms with Sustained Attention and Set-Shifting in Schizophrenia Patients.
[So] Source:Neuropsychobiology;74(1):41-47, 2016.
[Is] ISSN:1423-0224
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Despite extensive research in the past decades, the influence of genetics on cognitive functions in schizophrenia remains unclear. Dystrobrevin-binding protein 1 (DTNBP1) is one of the most promising candidate genes in schizophrenia. An association of DTNBP1 with cognitive dysfunction, particularly memory impairment, has been reported in a number of studies. However, the results remain inconsistent. The aim of this study was to measure the association between DTNBP1 polymorphisms and cognitive domains in a well-characterized sample. METHODS: Ninety-one clinically stable schizophrenia outpatients underwent a battery of cognitive tests. Six single nucleotide polymorphisms (SNPs) of DTNBP1 were genotyped in all participants. Statistical and multivariate analyses were performed. RESULTS: Factor analysis revealed 4 factors corresponding to distinct cognitive domains, namely sustained attention, set-shifting, executive functioning, and memory. We found a significant association of the rs909706 polymorphism with attention (p = 0.030) and a nonsignificant trend for set-shifting (p = 0.060). The other SNPs and haplotypes were not associated with cognitive function. DISCUSSION: Replication of this finding in a larger sample is needed in order to confirm the importance of this particular polymorphism in the genetics of schizophrenia, particularly the distinct cognitive domains. In conclusion, the present study supports the involvement of DTNBP1 in the regulation of cognitive processes and demonstrates association in particular with sustained attention and set-shifting in schizophrenia patients.
[Mh] Termos MeSH primário: Atenção
Transtornos Cognitivos/genética
Proteínas Associadas à Distrofina/genética
Esquizofrenia/genética
Psicologia do Esquizofrênico
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Transtornos Cognitivos/psicologia
Disbindina
Função Executiva
Análise Fatorial
Feminino
Predisposição Genética para Doença
Genótipo
Seres Humanos
Masculino
Memória
Meia-Idade
Polimorfismo de Nucleotídeo Único
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DTNBP1 protein, human); 0 (Dysbindin); 0 (Dystrophin-Associated Proteins)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161101
[St] Status:MEDLINE
[do] DOI:10.1159/000450550



página 1 de 56 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde