Base de dados : MEDLINE
Pesquisa : B01.050.150.900.649.313.992.635.505.500.550.560 [Categoria DeCS]
Referências encontradas : 190 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 19 ir para página                         

  1 / 190 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26645409
[Au] Autor:Myers KR; Liu G; Feng Y; Zheng JQ
[Ad] Endereço:Department of Cell Biology, Emory University School of Medicine, Atlanta, Georgia, 30322.
[Ti] Título:Oligodendroglial defects during quakingviable cerebellar development.
[So] Source:Dev Neurobiol;76(9):972-82, 2016 09.
[Is] ISSN:1932-846X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The selective RNA-binding protein Quaking I (QKI) has previously been implicated in RNA localization and stabilization, alternative splicing, cell proliferation, and differentiation. The spontaneously-occurring quakingviable (qkv) mutant mouse exhibits a sharply attenuated level of QKI in myelin-producing cells, including oligodendrocytes (OL) because of the loss of an OL-specific promoter. The disruption of QKI in OLs results in severe hypomyelination of the central nervous system, but the underlying cellular mechanisms remain to be fully elucidated. In this study, we used the qkv mutant mouse as a model to study myelination defects in the cerebellum. We found that oligodendroglial development and myelination are adversely affected in the cerebellum of qkv mice. Specifically, we identified an increase in the total number of oligodendroglial precursor cells in qkv cerebella, a substantial portion of which migrated into the grey matter. Furthermore, these mislocalized oligodendroglial precursor cells retained their migratory morphology late into development. Interestingly, a number of these presumptive oligodendrocyte precursors were found at the Purkinje cell layer in qkv cerebella, resembling Bergman glia. These findings indicate that QKI is involved in multiple aspects of oligodendroglial development. QKI disruption can impact the cell fate of oligodendrocyte precursor cells, their migration and differentiation, and ultimately myelination in the cerebellum. © 2015 Wiley Periodicals, Inc. Develop Neurobiol 76: 972-982, 2016.
[Mh] Termos MeSH primário: Diferenciação Celular/fisiologia
Movimento Celular/fisiologia
Doenças Cerebelares/metabolismo
Cerebelo/fisiologia
Doenças Desmielinizantes/metabolismo
Oligodendroglia/fisiologia
Proteínas de Ligação a RNA/fisiologia
[Mh] Termos MeSH secundário: Animais
Cerebelo/crescimento & desenvolvimento
Modelos Animais de Doenças
Feminino
Masculino
Camundongos
Camundongos Quaking
Camundongos Transgênicos
Células de Purkinje/fisiologia
Proteínas de Ligação a RNA/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Qk protein, mouse); 0 (RNA-Binding Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171121
[Lr] Data última revisão:
171121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151210
[St] Status:MEDLINE
[do] DOI:10.1002/dneu.22369


  2 / 190 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:24792162
[Au] Autor:Mandler MD; Ku L; Feng Y
[Ad] Endereço:Department of Pharmacology, Emory University, Atlanta, GA 30329, USA.
[Ti] Título:A cytoplasmic quaking I isoform regulates the hnRNP F/H-dependent alternative splicing pathway in myelinating glia.
[So] Source:Nucleic Acids Res;42(11):7319-29, 2014 Jun.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The selective RNA-binding protein quaking I (QKI) plays important roles in controlling alternative splicing (AS). Three QKI isoforms are broadly expressed, which display distinct nuclear-cytoplasmic distribution. However, molecular mechanisms by which QKI isoforms control AS, especially in distinct cell types, still remain elusive. The quakingviable (qk(v)) mutant mice carry deficiencies of all QKI isoforms in oligodendrocytes (OLs) and Schwann cells (SWCs), the myelinating glia of central and peripheral nervous system (CNS and PNS), respectively, resulting in severe dysregulation of AS. We found that the cytoplasmic isoform QKI-6 regulates AS of polyguanine (G-run)-containing transcripts in OLs and rescues aberrant AS in the qk(v) mutant by repressing expression of two canonical splicing factors, heterologous nuclear ribonucleoproteins (hnRNPs) F and H. Moreover, we identified a broad spectrum of in vivo functional hnRNP F/H targets in OLs that contain conserved exons flanked by G-runs, many of which are dysregulated in the qk(v) mutant. Interestingly, AS targets of the QKI-6-hnRNP F/H pathway in OLs are differentially affected in SWCs, suggesting that additional cell-type-specific factors modulate AS during CNS and PNS myelination. Together, our studies provide the first evidence that cytoplasmic QKI-6 acts upstream of hnRNP F/H, which forms a novel pathway to control AS in myelinating glia.
[Mh] Termos MeSH primário: Processamento Alternativo
Ribonucleoproteínas Nucleares Heterogêneas Grupo F-H/metabolismo
Neuroglia/metabolismo
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Citoplasma/metabolismo
Éxons
Camundongos
Camundongos Quaking
Camundongos Transgênicos
Bainha de Mielina/fisiologia
Oligodendroglia/metabolismo
Isoformas de Proteínas/metabolismo
Precursores de RNA/metabolismo
RNA Mensageiro/metabolismo
Células de Schwann/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Heterogeneous-Nuclear Ribonucleoprotein Group F-H); 0 (Protein Isoforms); 0 (Qk protein, mouse); 0 (RNA Precursors); 0 (RNA, Messenger); 0 (RNA-Binding Proteins)
[Em] Mês de entrada:1408
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140506
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gku353


  3 / 190 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:23963726
[Au] Autor:van der Veer EP; de Bruin RG; Kraaijeveld AO; de Vries MR; Bot I; Pera T; Segers FM; Trompet S; van Gils JM; Roeten MK; Beckers CM; van Santbrink PJ; Janssen A; van Solingen C; Swildens J; de Boer HC; Peters EA; Bijkerk R; Rousch M; Doop M; Kuiper J; Schalij MJ; van der Wal AC; Richard S; van Berkel TJ; Pickering JG; Hiemstra PS; Goumans MJ; Rabelink TJ; de Vries AA; Quax PH; Jukema JW; Biessen EA; van Zonneveld AJ
[Ad] Endereço:From the Einthoven Laboratory of Experimental Vascular Medicine.
[Ti] Título:Quaking, an RNA-binding protein, is a critical regulator of vascular smooth muscle cell phenotype.
[So] Source:Circ Res;113(9):1065-75, 2013 Oct 12.
[Is] ISSN:1524-4571
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RATIONALE: RNA-binding proteins are critical post-transcriptional regulators of RNA and can influence pre-mRNA splicing, RNA localization, and stability. The RNA-binding protein Quaking (QKI) is essential for embryonic blood vessel development. However, the role of QKI in the adult vasculature, and in particular in vascular smooth muscle cells (VSMCs), is currently unknown. OBJECTIVE: We sought to determine the role of QKI in regulating adult VSMC function and plasticity. METHODS AND RESULTS: We identified that QKI is highly expressed by neointimal VSMCs of human coronary restenotic lesions, but not in healthy vessels. In a mouse model of vascular injury, we observed reduced neointima hyperplasia in Quaking viable mice, which have decreased QKI expression. Concordantly, abrogation of QKI attenuated fibroproliferative properties of VSMCs, while potently inducing contractile apparatus protein expression, rendering noncontractile VSMCs with the capacity to contract. We identified that QKI localizes to the spliceosome, where it interacts with the myocardin pre-mRNA and regulates the splicing of alternative exon 2a. This post-transcriptional event impacts the Myocd_v3/Myocd_v1 mRNA balance and can be modulated by mutating the quaking response element in exon 2a of myocardin. Furthermore, we identified that arterial damage triggers myocardin alternative splicing and is tightly coupled with changes in the expression levels of distinct QKI isoforms. CONCLUSIONS: We propose that QKI is a central regulator of VSMC phenotypic plasticity and that intervention in QKI activity can ameliorate pathogenic, fibroproliferative responses to vascular injury.
[Mh] Termos MeSH primário: Proliferação Celular
Músculo Liso Vascular/metabolismo
Miócitos de Músculo Liso/metabolismo
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Processamento Alternativo
Animais
Lesões das Artérias Carótidas/metabolismo
Artéria Carótida Primitiva/metabolismo
Artéria Carótida Primitiva/patologia
Movimento Celular
Reestenose Coronária/metabolismo
Reestenose Coronária/patologia
Vasos Coronários/metabolismo
Vasos Coronários/patologia
Modelos Animais de Doenças
Matriz Extracelular/metabolismo
Feminino
Regulação da Expressão Gênica
Células HEK293
Seres Humanos
Hiperplasia
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Quaking
Músculo Liso Vascular/patologia
Miócitos de Músculo Liso/patologia
Neointima
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Fenótipo
Interferência de RNA
Proteínas de Ligação a RNA/genética
Transativadores/genética
Transativadores/metabolismo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Nuclear Proteins); 0 (QKI protein, human); 0 (Qk protein, mouse); 0 (RNA-Binding Proteins); 0 (Trans-Activators); 0 (myocardin)
[Em] Mês de entrada:1312
[Cu] Atualização por classe:131011
[Lr] Data última revisão:
131011
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130822
[St] Status:MEDLINE
[do] DOI:10.1161/CIRCRESAHA.113.301302


  4 / 190 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:23224912
[Au] Autor:Rosenbluth J; Bobrowski-Khoury N
[Ad] Endereço:Department of Physiology and Neuroscience, New York University School of Medicine, New York, New York 10016, USA. rosenj03@med.nyu.edu
[Ti] Título:Structural bases for central nervous system malfunction in the quaking mouse: dysmyelination in a potential model of schizophrenia.
[So] Source:J Neurosci Res;91(3):374-81, 2013 Mar.
[Is] ISSN:1097-4547
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The dysmyelinating mouse mutant quaking (qk) is thought to be a model of schizophrenia based on diminution of CNS myelin (Andreone et al., 2007) and downregulation of the Qk gene (Haroutunian et al., 2006) in the brains of schizophrenic patients. The purpose of this study was to identify specific structural defects in the qk mouse CNS that could compromise physiologic function and that in humans might account for some of the cognitive defects characteristic of schizophrenia. Ultrastructural analysis of qk mouse CNS myelinated fibers shows abnormalities in nodal, internodal, and paranodal regions, including marked variation in myelin thickness among neighboring fibers, spotty disruption of paranodal junctions, abnormal distribution of nodal and paranodal ion channel complexes, generalized thinning and incompactness of myelin, and on many axonal profiles complete absence of myelin. These structural defects are likely to cause abnormalities in conduction velocity, synchrony of activation, temporal ordering of signals, and other physiological parameters. We conclude that the structural abnormalities described are likely to be responsible for significant functional impairment both in the qk mouse CNS and in the human CNS with comparable myelin pathology.
[Mh] Termos MeSH primário: Doenças Desmielinizantes/patologia
Modelos Animais de Doenças
Esquizofrenia/patologia
Medula Espinal/patologia
[Mh] Termos MeSH secundário: Animais
Doenças do Sistema Nervoso Central/genética
Doenças do Sistema Nervoso Central/patologia
Doenças Desmielinizantes/genética
Camundongos
Camundongos Quaking
Esquizofrenia/genética
Medula Espinal/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1310
[Cu] Atualização por classe:130117
[Lr] Data última revisão:
130117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121211
[St] Status:MEDLINE
[do] DOI:10.1002/jnr.23167


  5 / 190 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:21948283
[Au] Autor:Zhu H; Zhao L; Wang E; Dimova N; Liu G; Feng Y; Cambi F
[Ad] Endereço:Department of Neurology, University of Kentucky, Lexington, Kentucky, USA.
[Ti] Título:The QKI-PLP pathway controls SIRT2 abundance in CNS myelin.
[So] Source:Glia;60(1):69-82, 2012 Jan.
[Is] ISSN:1098-1136
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sirtuin 2 (SIRT2), a nicotinamide adenine dinucleotide (NAD)-dependent deacetylase expressed by oligodendrocytes (OLs), the myelin-producing cells of the central nervous system (CNS), is markedly up-regulated during active myelination (Li et al. (2007) J Neurosci 27:2606-2616; Southwood et al. (2007) Neurochem Res 32:187-195; Werner et al. (2007) J Neurosci 27:7717-7730). SIRT2 is a component of the myelin proteome and is severely reduced in the Plp1 knockout mouse brain, in which both proteolipid protein (PLP) and DM20 are absent (Werner et al. (2007) J Neurosci 27:7717-7730). The mechanisms that regulate SIRT2 expression in OLs and myelin remain to be investigated. We report for the first time that the expression of SIRT2 is regulated by the QKI-dependent pathway and this effect is mediated through selective regulation of PLP. In the homozygous quakingviable (qk(v) /qk(v) ) mutant mouse that harbors QKI deficiency in OLs (Bockbrader and Feng (2008) Future Neurol 3:655-668; Ebersole et al. (1996) Nat Genet 12:260-265; Hardy et al. (1996) J Neurosci 16:7941-7949), PLP, but not DM20 mRNA, was selectively down-regulated and SIRT2 protein was severely reduced whereas SIRT2 mRNA expression was unaffected. Expression of the cytoplasmic isoform QKI6 in OLs (Zhao et al. (2006) J Neurosci 26:11278-11286) rescued SIRT2 expression in the qk(v) /qk(v) mutant concomitantly with restoration of PLP expression. Moreover, SIRT2 protein is diminished in myelin tracts and compact myelin of the PLP-ISEdel mutant brain, in which PLP protein but not DM20 is selectively reduced (Wang et al. (2008) Exp Neurol 214:322-330). In contrast, SIRT2 expression and its cellular function in regulating process complexity are not affected by the absence of PLP in PLP-ISEdel non-myelinating OLs. Collectively, our results indicate that the abundance of SIRT2 in myelin is dependent on PLP, but not DM20.
[Mh] Termos MeSH primário: Encéfalo/citologia
Proteína Proteolipídica de Mielina/metabolismo
Bainha de Mielina/metabolismo
Oligodendroglia/metabolismo
Proteínas de Ligação a RNA/metabolismo
Transdução de Sinais/fisiologia
Sirtuína 2/metabolismo
[Mh] Termos MeSH secundário: Fatores Etários
Animais
Animais Recém-Nascidos
Diferenciação Celular
Citometria de Fluxo
Regulação da Expressão Gênica no Desenvolvimento
Proteínas de Fluorescência Verde
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Quaking
Camundongos Transgênicos
Mutação
Proteína Proteolipídica de Mielina/genética
RNA Mensageiro
Proteínas de Ligação a RNA/genética
Receptores do Fator Natriurético Atrial/genética
Transdução de Sinais/genética
Sirtuína 2/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Myelin Proteolipid Protein); 0 (Plp1 protein, mouse); 0 (Qk protein, mouse); 0 (RNA, Messenger); 0 (RNA-Binding Proteins); 0 (enhanced green fluorescent protein); 147336-22-9 (Green Fluorescent Proteins); EC 3.5.1.- (Sirt2 protein, mouse); EC 3.5.1.- (Sirtuin 2); EC 4.6.1.2 (Receptors, Atrial Natriuretic Factor); EC 4.6.1.2 (atrial natriuretic factor receptor C)
[Em] Mês de entrada:1203
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110928
[St] Status:MEDLINE
[do] DOI:10.1002/glia.21248


  6 / 190 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:22355603
[Au] Autor:Gavino C; Richard S
[Ad] Endereço:Terry Fox Molecular Oncology Group and the Bloomfield Center for Research on Aging, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital, and Departments of Oncology and Medicine, McGill University , Montréal, Québec, Canada, H3T 1E2.
[Ti] Título:Loss of p53 in quaking viable mice leads to Purkinje cell defects and reduced survival.
[So] Source:Sci Rep;1:84, 2011.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The qk(v) mutation is a one megabase deletion resulting in abnormal expression of the qkI gene. qk(v) mice exhibit hypomyelination of the central nervous system and display rapid tremors and seizures as adults. The qkI locus on 6q26-27 has also been implicated as a candidate tumor suppressor gene as the qkI locus maps to a region of genetic instability in Glioblastoma Multiforme (GBM), an aggressive brain tumor of astrocytic lineage. As GBM frequently harbors mutations affecting p53, we crossbred qk(v) and p53 mutant mice to examine whether qk(v) mice on a p53(-/-) background have an increased incidence of GBM. qk(v) (/v); p53(-/-) mice had a reduced survival rate compared to p53(-/-) littermates, and the cause of death of the majority of the mice remains unknown. In addition, immunohistochemistry revealed Purkinje cell degeneration in the cerebellum. These results suggest that p53 and qkI are genetically linked for neuronal maintenance and survival.
[Mh] Termos MeSH primário: Células de Purkinje/patologia
Proteína Supressora de Tumor p53/fisiologia
[Mh] Termos MeSH secundário: Animais
Sequência de Bases
Neoplasias Encefálicas/patologia
Primers do DNA
Instabilidade Genômica
Glioblastoma/patologia
Imuno-Histoquímica
Camundongos
Camundongos Knockout
Camundongos Quaking
Mutação
Reação em Cadeia da Polimerase
Análise de Sobrevida
Proteína Supressora de Tumor p53/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA Primers); 0 (Tumor Suppressor Protein p53)
[Em] Mês de entrada:1308
[Cu] Atualização por classe:150225
[Lr] Data última revisão:
150225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120223
[St] Status:MEDLINE
[do] DOI:10.1038/srep00084


  7 / 190 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:21447392
[Au] Autor:Gavino C; Richard S
[Ad] Endereço:Terry Fox Molecular Oncology Group and the Bloomfield Center for Research on Aging, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital, McGill University, Montréal, Québec H3T1E2, Canada.
[Ti] Título:Patched1 haploinsufficiency impairs ependymal cilia function of the quaking viable mice, leading to fatal hydrocephalus.
[So] Source:Mol Cell Neurosci;47(2):100-7, 2011 Jun.
[Is] ISSN:1095-9327
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The quaking viable (qk(v)) mice harbor an autosomal recessive mutation that deletes the parkin co-regulated gene (pacrg) and parkin (park2) genes, and alters the expression of the quaking (qkI) gene. qk(v) mice have been well-studied for their dysmyelination phenotype caused by the altered expression of the qkI gene. The qk(v) mice exhibit sterility in males and develop acquired mild hydrocephalus due to the lack of PACRG expression. To identify genetic interactors of the pacrg-parkin-qkI locus, we crossbred the qk(v) mice with various mouse strains including the patched1 (ptch1)-deficient mice. The ptch1 heterozygous mice exhibit increased Sonic Hedgehog (Shh) signaling and are prone to several malignancies including tumorigenesis. In the present study, we show that the qk(v/v); ptch1⁺/⁻ mice are distinguished by a dome-shaped skull at 4 to 6weeks of age and exhibit dilation of the lateral and third ventricles leading to fatal acquired hydrocephalus by ~5months of age, unlike their littermate controls that did not develop the condition. The qk(v/v); ptch1⁺/⁻ mice contained normal ciliated ependymal cells lining the ventricles of the brain, but these cells were functionally compromised with a severe cilial mediated flow defect. Our findings suggest that the ptch1 and the pacrg-parkin-qkI loci genetically interact to regulate cilia function of the ependymal cells.
[Mh] Termos MeSH primário: Cílios/metabolismo
Epêndima/citologia
Haploinsuficiência
Hidrocefalia/genética
Hidrocefalia/mortalidade
Camundongos Quaking
Receptores de Superfície Celular/genética
[Mh] Termos MeSH secundário: Animais
Ventrículos Cerebrais/anatomia & histologia
Cílios/patologia
Epêndima/metabolismo
Hidrocefalia/patologia
Masculino
Camundongos
Camundongos Knockout
Receptores Patched
Receptor Patched-1
Receptores de Superfície Celular/deficiência
Taxa de Sobrevida
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Patched Receptors); 0 (Patched-1 Receptor); 0 (Ptch1 protein, mouse); 0 (Receptors, Cell Surface)
[Em] Mês de entrada:1110
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110331
[St] Status:MEDLINE
[do] DOI:10.1016/j.mcn.2011.03.004


  8 / 190 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:20106870
[Au] Autor:Wilson GR; Wang HX; Egan GF; Robinson PJ; Delatycki MB; O'Bryan MK; Lockhart PJ
[Ad] Endereço:Bruce Lefroy Centre for Genetic Health Research, Murdoch Childrens Research Institute, Parkville 3052, Australia.
[Ti] Título:Deletion of the Parkin co-regulated gene causes defects in ependymal ciliary motility and hydrocephalus in the quakingviable mutant mouse.
[So] Source:Hum Mol Genet;19(8):1593-602, 2010 Apr 15.
[Is] ISSN:1460-2083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The quakingviable mouse (qkv) is a spontaneous recessive mouse mutant with a deletion of approximately 1.1 Mb in the proximal region of chromosome 17. The deletion affects the expression of three genes; quaking (Qk), Parkin-coregulated gene (Pacrg) and parkin (Park2). The resulting phenotype, which includes dysmyelination of the central nervous system and male sterility, is due to reduced expression of Qk and a complete lack of Pacrg expression, respectively. Pacrg is required for correct development of the spermatozoan flagella, a specialized type of motile cilia. In vertebrates, motile cilia are required for multiple functions related to cellular movement or movement of media over a stationary cell surface. To investigate the potential role of PACRG in motile cilia we analysed qkv mutant mice for evidence of cilial dysfunction. Histological and magnetic resonance imaging analyses demonstrated that qkv mutant mice were affected by acquired, communicating hydrocephalus (HC). Structural analysis of ependymal cilia demonstrated that the 9 + 2 arrangement of axonemal microtubules was intact and that both the density of ciliated cells and cilia length was similar to wild-type littermates. Cilia function studies showed a reduction in ependymal cilial beat frequency and cilial mediated flow in qkv mutant mice compared with wild-type littermate controls. Moreover, transgenic expression of Pacrg was necessary and sufficient to correct this deficit and rescue the HC phenotype in the qkv mutant. This study provides novel in vivo evidence that Pacrg is required for motile cilia function and may be involved in the pathogenesis of human ciliopathies, such as HC, asthenospermia and primary ciliary dyskinesia.
[Mh] Termos MeSH primário: Cílios/fisiologia
Epêndima/metabolismo
Deleção de Genes
Hidrocefalia/genética
Proteínas/genética
[Mh] Termos MeSH secundário: Animais
Cílios/genética
Modelos Animais de Doenças
Feminino
Seres Humanos
Hidrocefalia/metabolismo
Hidrocefalia/fisiopatologia
Masculino
Camundongos
Camundongos Quaking
Proteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Pacrg protein, mouse); 0 (Proteins)
[Em] Mês de entrada:1009
[Cu] Atualização por classe:100329
[Lr] Data última revisão:
100329
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100129
[St] Status:MEDLINE
[do] DOI:10.1093/hmg/ddq031


  9 / 190 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:19226531
[Au] Autor:Burguet J; Andrey P; Rampin O; Maurin Y
[Ad] Endereço:Equipe Analyse & modélisation en imagerie biologique, Nopa, Umr 1197 Inra-Université Paris 11, bât 325, Jouy-en-Josas 78352, France. Jasmine.Burguet@jouy.inra.fr
[Ti] Título:Three-dimensional statistical modeling of neuronal populations: illustration with spatial localization of supernumerary neurons in the locus coeruleus of quaking mutant mice.
[So] Source:J Comp Neurol;513(5):483-95, 2009 Apr 10.
[Is] ISSN:1096-9861
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:An algorithm for the three-dimensional statistical representation of neuronal populations was designed and implemented. Using this algorithm a series of 3D models, calculated from repeated histological experiments, can be combined to provide a synthetic vision of a population of neurons taking into account biological and experimental variability. Based on the point process theory, our algorithm allows computation of neuronal density maps from which isodensity surfaces can be readily extracted and visualized as surface models revealing the statistical organization of the neuronal population under study. This algorithm was applied to the spatial distribution of locus coeruleus (LC) neurons of 30- and 90-day-old control and quaking mice. By combining 12 3D models of the LC, a region of the nucleus in which a subpopulation of neurons loses its noradrenergic phenotype between 30 and 90 days postnatally was demonstrated in control mice but not in quaking mice, leading to the hyperplasia previously reported in adult mutants. Altogether, this algorithm allows computation of 3D statistical and graphical models of neuronal populations, providing a contribution to quantitative 3D neuroanatomical modeling.
[Mh] Termos MeSH primário: Algoritmos
Imagem Tridimensional/métodos
Locus Cerúleo/anatomia & histologia
Neurônios/metabolismo
Tirosina 3-Mono-Oxigenase/metabolismo
[Mh] Termos MeSH secundário: Fatores Etários
Animais
Contagem de Células
Locus Cerúleo/citologia
Locus Cerúleo/enzimologia
Camundongos
Camundongos Quaking
Modelos Estatísticos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 1.14.16.2 (Tyrosine 3-Monooxygenase)
[Em] Mês de entrada:0904
[Cu] Atualização por classe:090225
[Lr] Data última revisão:
090225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090220
[St] Status:MEDLINE
[do] DOI:10.1002/cne.21954


  10 / 190 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:18590840
[Au] Autor:Zearfoss NR; Farley BM; Ryder SP
[Ad] Endereço:Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, LRB-906, Worcester, MA, 01605, USA.
[Ti] Título:Post-transcriptional regulation of myelin formation.
[So] Source:Biochim Biophys Acta;1779(8):486-94, 2008 Aug.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Myelin is a specialized structure of the nervous system that both enhances electrical conductance and protects neurons from degeneration. In the central nervous system, extensively polarized oligodendrocytes form myelin by wrapping cellular processes in a spiral pattern around neuronal axons. Myelin formation requires the oligodendrocyte to regulate gene expression in response to changes in its extracellular environment. Because these changes occur at a distance from the cell body, post-transcriptional control of gene expression allows the cell to fine-tune its response. Here, we review the RNA-binding proteins that control myelin formation in the brain, highlighting the molecular mechanisms by which they control gene expression and drawing parallels from studies in other cell types.
[Mh] Termos MeSH primário: Encéfalo/metabolismo
Regulação da Expressão Gênica/fisiologia
Bainha de Mielina/metabolismo
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Animais
Axônios/metabolismo
Proteína do X Frágil de Retardo Mental/genética
Proteína do X Frágil de Retardo Mental/metabolismo
Camundongos
Camundongos Quaking
Oligodendroglia/metabolismo
Proteínas de Ligação a RNA/genética
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Qk protein, mouse); 0 (RNA-Binding Proteins); 139135-51-6 (Fragile X Mental Retardation Protein)
[Em] Mês de entrada:0810
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:080702
[St] Status:MEDLINE
[do] DOI:10.1016/j.bbagrm.2008.06.003



página 1 de 19 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