Base de dados : MEDLINE
Pesquisa : A16.630 [Categoria DeCS]
Referências encontradas : 654 [refinar]
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[PMID]:28800946
[Au] Autor:Wang C; Li J; Meng Q; Wang B
[Ad] Endereço:Department of Genetic Medicine, Weill Medical College of Cornell University, 1300 York Avenue, W404, New York, NY 10065, USA.
[Ti] Título:Three Tctn proteins are functionally conserved in the regulation of neural tube patterning and Gli3 processing but not ciliogenesis and Hedgehog signaling in the mouse.
[So] Source:Dev Biol;430(1):156-165, 2017 10 01.
[Is] ISSN:1095-564X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tctn1, Tctn2, and Tctn3 are membrane proteins that localize at the transition zone of primary cilia. Tctn1 and Tctn2 mutations have been reported in both humans and mice, but Tctn3 mutations have been reported only in humans. It is also not clear whether the three Tctn proteins are functionally conserved with respect to ciliogenesis and Hedgehog (Hh) signaling. In the present study, we report that loss of Tctn3 gene function in mice results in a decrease in ciliogenesis and Hh signaling. Consistent with this, Tctn3 mutant mice exhibit holoprosencephaly and randomized heart looping and lack the floor plate in the neural tube, the phenotypes similar to those of Tctn1 and Tctn2 mutants. We also show that overexpression of Tctn3, but not Tctn1 or Tctn2, can rescue ciliogenesis in Tctn3 mutant cells. Similarly, replacement of Tctn3 with Tctn1 or Tctn2 in the Tctn3 gene locus results in reduced ciliogenesis and Hh signaling, holoprosencephaly, and randomized heart looping. Surprisingly, however, the neural tube patterning and the proteolytic processing of Gli3 (a transcription regulator for Hh signaling) into a repressor, both of which are usually impaired in ciliary gene mutants, are normal. These results suggest that Tctn1, Tctn2, and Tctn3 are functionally divergent with respect to their role in ciliogenesis and Hh signaling but conserved in neural tube patterning and Gli3 processing.
[Mh] Termos MeSH primário: Padronização Corporal
Cílios/metabolismo
Proteínas Hedgehog/metabolismo
Fatores de Transcrição Kruppel-Like/metabolismo
Proteínas de Membrana/metabolismo
Proteínas do Tecido Nervoso/metabolismo
Tubo Neural/embriologia
Tubo Neural/metabolismo
Organogênese
[Mh] Termos MeSH secundário: Animais
Padronização Corporal/genética
Sequência Conservada
Embrião de Mamíferos/metabolismo
Desenvolvimento Embrionário
Fibroblastos/metabolismo
Deleção de Genes
Inativação Gênica
Holoprosencefalia/metabolismo
Holoprosencefalia/patologia
Homozigoto
Camundongos
Organogênese/genética
Transdução de Sinais/genética
Proteína Gli3 com Dedos de Zinco
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gli3 protein, mouse); 0 (Hedgehog Proteins); 0 (Kruppel-Like Transcription Factors); 0 (Membrane Proteins); 0 (Nerve Tissue Proteins); 0 (Tctn1 protein, mouse); 0 (Tctn2 protein, mouse); 0 (Tctn3 protein, mouse); 0 (Zinc Finger Protein Gli3)
[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:170813
[St] Status:MEDLINE


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[PMID]:28778799
[Au] Autor:Prager A; Hagenlocher C; Ott T; Schambony A; Feistel K
[Ad] Endereço:University of Hohenheim, Institute of Zoology, Garbenstr. 30, 70599 Stuttgart, Germany. Electronic address: angela.prager@uni-hohenheim.de.
[Ti] Título:hmmr mediates anterior neural tube closure and morphogenesis in the frog Xenopus.
[So] Source:Dev Biol;430(1):188-201, 2017 10 01.
[Is] ISSN:1095-564X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Development of the central nervous system requires orchestration of morphogenetic processes which drive elevation and apposition of the neural folds and their fusion into a neural tube. The newly formed tube gives rise to the brain in anterior regions and continues to develop into the spinal cord posteriorly. Conspicuous differences between the anterior and posterior neural tube become visible already during neural tube closure (NTC). Planar cell polarity (PCP)-mediated convergent extension (CE) movements are restricted to the posterior neural plate, i.e. hindbrain and spinal cord, where they propagate neural fold apposition. The lack of CE in the anterior neural plate correlates with a much slower mode of neural fold apposition anteriorly. The morphogenetic processes driving anterior NTC have not been addressed in detail. Here, we report a novel role for the breast cancer susceptibility gene and microtubule (MT) binding protein Hmmr (Hyaluronan-mediated motility receptor, RHAMM) in anterior neurulation and forebrain development in Xenopus laevis. Loss of hmmr function resulted in a lack of telencephalic hemisphere separation, arising from defective roof plate formation, which in turn was caused by impaired neural tissue narrowing. hmmr regulated polarization of neural cells, a function which was dependent on the MT binding domains. hmmr cooperated with the core PCP component vangl2 in regulating cell polarity and neural morphogenesis. Disrupted cell polarization and elongation in hmmr and vangl2 morphants prevented radial intercalation (RI), a cell behavior essential for neural morphogenesis. Our results pinpoint a novel role of hmmr in anterior neural development and support the notion that RI is a major driving force for anterior neurulation and forebrain morphogenesis.
[Mh] Termos MeSH primário: Morfogênese
Tubo Neural/embriologia
Tubo Neural/metabolismo
Proteínas de Xenopus/metabolismo
Xenopus laevis/embriologia
Xenopus laevis/metabolismo
[Mh] Termos MeSH secundário: Animais
Polaridade Celular/efeitos dos fármacos
Proteínas de Membrana/metabolismo
Microtúbulos/efeitos dos fármacos
Microtúbulos/metabolismo
Microtúbulos/ultraestrutura
Modelos Biológicos
Morfolinos/farmacologia
Tubo Neural/citologia
Tubo Neural/ultraestrutura
Prosencéfalo/embriologia
Prosencéfalo/metabolismo
Ligação Proteica/efeitos dos fármacos
Domínios Proteicos
Proteínas de Xenopus/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Hmmr protein, Xenopus); 0 (Membrane Proteins); 0 (Morpholinos); 0 (Xenopus Proteins); 0 (strabismus protein, Xenopus)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170806
[St] Status:MEDLINE


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[PMID]:28688895
[Au] Autor:Hoelzl MA; Heby-Henricson K; Gerling M; Dias JM; Kuiper RV; Trünkle C; Bergström Å; Ericson J; Toftgård R; Teglund S
[Ad] Endereço:Department of Biosciences and Nutrition, Karolinska Institutet, SE-141 83 Huddinge, Sweden. Electronic address: maria.holzl@ki.se.
[Ti] Título:Differential requirement of SUFU in tissue development discovered in a hypomorphic mouse model.
[So] Source:Dev Biol;429(1):132-146, 2017 09 01.
[Is] ISSN:1095-564X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Suppressor of Fused (SUFU) is an essential negative regulator of the Hedgehog (HH) pathway and involved in GLI transcription factor regulation. Due to early embryonic lethality of Sufu mice, investigations of SUFU's role later in development are limited to conditional, tissue-specific knockout models. In this study we developed a mouse model (Sufu ) with hypomorphic features where embryos were viable up to E18.5, although with a spectrum of developmental defects of varying severity, including polydactyly, exencephaly and omphalocele. Development of certain tissues, like the skeleton, was more affected than that of others such as skin, which remained largely normal. Interestingly, no apparent changes in the dorso-ventral patterning of the neural tube at E9.0 could be seen. Thus, this model provides an opportunity to globally study SUFU's molecular function in organogenesis beyond E9.5. Molecularly, Sufu embryos displayed aberrant mRNA splicing and drastically reduced levels of Sufu wild-type mRNA and SUFU protein in all tissues. As a consequence, at E9.5 the levels of all three different GLI proteins were reduced. Interestingly, despite the reduction of GLI3 protein levels, the critical ratio of the GLI3 full-length transcriptional activator versus GLI3 truncated repressor remained unchanged compared to wild-type embryos. This suggests that the limited amount of SUFU protein present is sufficient for GLI processing but not for stabilization. Our data demonstrate that tissue development is differentially affected in response to the reduced SUFU levels, providing novel insight regarding the requirements of different levels of SUFU for proper organogenesis.
[Mh] Termos MeSH primário: Organogênese
Proteínas Repressoras/metabolismo
[Mh] Termos MeSH secundário: Alelos
Animais
Padronização Corporal/genética
Embrião de Mamíferos/metabolismo
Éxons/genética
Feminino
Regulação da Expressão Gênica no Desenvolvimento
Proteínas Hedgehog/metabolismo
Homozigoto
Masculino
Camundongos Endogâmicos BALB C
Camundongos Endogâmicos C57BL
Camundongos Nus
Modelos Animais
Tubo Neural/embriologia
Tubo Neural/metabolismo
Organogênese/genética
Mutação Puntual/genética
Sítios de Splice de RNA/genética
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Proteínas Repressoras/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Hedgehog Proteins); 0 (RNA Splice Sites); 0 (RNA, Messenger); 0 (Repressor Proteins); 0 (Sufu protein, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170710
[St] Status:MEDLINE


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[PMID]:28624345
[Au] Autor:York JR; Yuan T; Zehnder K; McCauley DW
[Ad] Endereço:Department of Biology, University of Oklahoma, 730 Van Vleet Oval, Norman, OK 73019, USA.
[Ti] Título:Lamprey neural crest migration is Snail-dependent and occurs without a differential shift in cadherin expression.
[So] Source:Dev Biol;428(1):176-187, 2017 08 01.
[Is] ISSN:1095-564X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The acquisition of neural crest cells was a key step in the origin of the vertebrate body plan. An outstanding question is how neural crest cells acquired their ability to undergo an epithelial-mesenchymal transition (EMT) and migrate extensively throughout the vertebrate embryo. We tested if differential regulation of classical cadherins-a highly conserved feature of neural crest EMT and migration in jawed vertebrates-mediates these cellular behaviors in lamprey, a basal jawless vertebrate. Lamprey has single copies of the type I and type II classical cadherins (CadIA and CadIIA). CadIIA is expressed in premigratory neural crest, and requires the transcription factor Snail for proper expression, yet CadIA is never expressed in the neural tube during neural crest development, suggesting that differential regulation of classical cadherin expression is not required to initiate neural crest migration in basal vertebrates. We hypothesize that neural crest cells evolved by retention of regulatory programs linking distinct mesenchymal and multipotency properties, and emigrated from the neural tube without differentially regulating type I/type II cadherins. Our results point to the coupling of mesenchymal state and multipotency as a key event facilitating the origin of migratory neural crest cells.
[Mh] Termos MeSH primário: Caderinas/metabolismo
Movimento Celular/fisiologia
Lampreias/embriologia
Crista Neural/embriologia
Fatores de Transcrição da Família Snail/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Caderinas/genética
Diferenciação Celular/fisiologia
Transição Epitelial-Mesenquimal/fisiologia
Regulação da Expressão Gênica no Desenvolvimento
Crista Neural/citologia
Tubo Neural/metabolismo
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cadherins); 0 (Snail Family Transcription Factors)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170619
[St] Status:MEDLINE


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[PMID]:28545845
[Au] Autor:Baumholtz AI; Simard A; Nikolopoulou E; Oosenbrug M; Collins MM; Piontek A; Krause G; Piontek J; Greene NDE; Ryan AK
[Ad] Endereço:Department of Human Genetics, McGill University, Canada; The Research Institute of the McGill University Health Centre, Montréal, Québec, Canada. Electronic address: amanda.baumholtz@mail.mcgill.ca.
[Ti] Título:Claudins are essential for cell shape changes and convergent extension movements during neural tube closure.
[So] Source:Dev Biol;428(1):25-38, 2017 08 01.
[Is] ISSN:1095-564X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During neural tube closure, regulated changes at the level of individual cells are translated into large-scale morphogenetic movements to facilitate conversion of the flat neural plate into a closed tube. Throughout this process, the integrity of the neural epithelium is maintained via cell interactions through intercellular junctions, including apical tight junctions. Members of the claudin family of tight junction proteins regulate paracellular permeability, apical-basal cell polarity and link the tight junction to the actin cytoskeleton. Here, we show that claudins are essential for neural tube closure: the simultaneous removal of Cldn3, -4 and -8 from tight junctions caused folate-resistant open neural tube defects. Their removal did not affect cell type differentiation, neural ectoderm patterning nor overall apical-basal polarity. However, apical accumulation of Vangl2, RhoA, and pMLC were reduced, and Par3 and Cdc42 were mislocalized at the apical cell surface. Our data showed that claudins act upstream of planar cell polarity and RhoA/ROCK signaling to regulate cell intercalation and actin-myosin contraction, which are required for convergent extension and apical constriction during neural tube closure, respectively.
[Mh] Termos MeSH primário: Polaridade Celular/fisiologia
Forma Celular/fisiologia
Placa Neural/embriologia
Tubo Neural/embriologia
Neurulação/fisiologia
Junções Íntimas/fisiologia
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/metabolismo
Animais
Moléculas de Adesão Celular/metabolismo
Embrião de Galinha
Claudina-3/genética
Claudina-3/metabolismo
Claudina-4/genética
Claudina-4/metabolismo
Claudinas/genética
Claudinas/metabolismo
Técnicas de Cultura Embrionária
Camundongos
Morfogênese/fisiologia
Proteínas do Tecido Nervoso/metabolismo
Defeitos do Tubo Neural/genética
Transdução de Sinais/fisiologia
Proteína cdc42 de Ligação ao GTP/metabolismo
Proteínas rho de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cdc42 protein, mouse); 0 (Cell Adhesion Molecules); 0 (Claudin-3); 0 (Claudin-4); 0 (Claudins); 0 (Cldn3 protein, mouse); 0 (Cldn4 protein, mouse); 0 (Ltap protein, mouse); 0 (Nerve Tissue Proteins); 0 (Pard3 protein, mouse); 0 (claudin 8); EC 3.6.5.2 (RhoA protein, mouse); EC 3.6.5.2 (cdc42 GTP-Binding Protein); EC 3.6.5.2 (rho GTP-Binding Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170527
[St] Status:MEDLINE


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[PMID]:28432198
[Au] Autor:Toriyama M; Toriyama M; Wallingford JB; Finnell RH
[Ad] Endereço:Department of Pediatrics, Dell Pediatric Research Institute, The University of Texas at Austin Dell Medical School, Austin, Texas, USA.
[Ti] Título:Folate-dependent methylation of septins governs ciliogenesis during neural tube closure.
[So] Source:FASEB J;31(8):3622-3635, 2017 Aug.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Periconception maternal folic acid (vitamin B ) supplementation can reduce the prevalence of neural tube defects (NTDs), although just how folates benefit the developing embryo and promote closing of the neural tube and other morphologic processes during development remains unknown. Folate contributes to a 1-carbon metabolism, which is essential for purine biosynthesis and methionine recycling and affects methylation of DNA, histones, and nonhistone proteins. Herein, we used animal models and cultured mammalian cells to demonstrate that disruption of the methylation pathway mediated by folate compromises normal neural tube closure (NTC) and ciliogenesis. We demonstrate that the embryos with NTD failed to adequately methylate septin2, a key regulator of cilium structure and function. We report that methylation of septin2 affected its GTP binding activity and formation of the septin2-6-7 complex. We propose that folic acid promotes normal NTC in some embryos by regulating the methylation of septin2, which is critical for normal cilium formation during early embryonic development.-Toriyama, M., Toriyama, M., Wallingford, J. B., Finnell, R. H. Folate-dependent methylation of septins governs ciliogenesis during neural tube closure.
[Mh] Termos MeSH primário: Cílios/fisiologia
Embrião de Mamíferos/metabolismo
Embrião não Mamífero/metabolismo
Ácido Fólico/metabolismo
Tubo Neural/fisiologia
Septinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Dactinomicina/análogos & derivados
Desenvolvimento Embrionário/fisiologia
Regulação da Expressão Gênica no Desenvolvimento/fisiologia
Células HEK293
Proteínas Hedgehog/genética
Proteínas Hedgehog/metabolismo
Seres Humanos
Metilação
Camundongos
Defeitos do Tubo Neural/etiologia
Plasmídeos
Transdução de Sinais
Xenopus/embriologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hedgehog Proteins); 0 (methylated actinomycin D); 1CC1JFE158 (Dactinomycin); 935E97BOY8 (Folic Acid); EC 3.6.1.- (Septins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170423
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201700092R


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[PMID]:28422959
[Au] Autor:Albuixech-Crespo B; López-Blanch L; Burguera D; Maeso I; Sánchez-Arrones L; Moreno-Bravo JA; Somorjai I; Pascual-Anaya J; Puelles E; Bovolenta P; Garcia-Fernàndez J; Puelles L; Irimia M; Ferran JL
[Ad] Endereço:Department of Genetics, School of Biology, and Institut de Biomedicina (IBUB), University of Barcelona, Barcelona, Spain.
[Ti] Título:Molecular regionalization of the developing amphioxus neural tube challenges major partitions of the vertebrate brain.
[So] Source:PLoS Biol;15(4):e2001573, 2017 Apr.
[Is] ISSN:1545-7885
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:All vertebrate brains develop following a common Bauplan defined by anteroposterior (AP) and dorsoventral (DV) subdivisions, characterized by largely conserved differential expression of gene markers. However, it is still unclear how this Bauplan originated during evolution. We studied the relative expression of 48 genes with key roles in vertebrate neural patterning in a representative amphioxus embryonic stage. Unlike nonchordates, amphioxus develops its central nervous system (CNS) from a neural plate that is homologous to that of vertebrates, allowing direct topological comparisons. The resulting genoarchitectonic model revealed that the amphioxus incipient neural tube is unexpectedly complex, consisting of several AP and DV molecular partitions. Strikingly, comparison with vertebrates indicates that the vertebrate thalamus, pretectum, and midbrain domains jointly correspond to a single amphioxus region, which we termed Di-Mesencephalic primordium (DiMes). This suggests that these domains have a common developmental and evolutionary origin, as supported by functional experiments manipulating secondary organizers in zebrafish and mice.
[Mh] Termos MeSH primário: Encéfalo/embriologia
Embrião não Mamífero/embriologia
Anfioxos/embriologia
Tubo Neural/embriologia
Vertebrados/embriologia
[Mh] Termos MeSH secundário: Animais
Evolução Biológica
Padronização Corporal/genética
Encéfalo/metabolismo
Embrião de Galinha
Embrião não Mamífero/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Hibridização in Situ Fluorescente
Anfioxos/metabolismo
Masculino
Camundongos Knockout
Modelos Biológicos
Modelos Genéticos
Tubo Neural/metabolismo
Vertebrados/metabolismo
Peixe-Zebra
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170522
[Lr] Data última revisão:
170522
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pbio.2001573


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[PMID]:28321127
[Au] Autor:Green SA; Uy BR; Bronner ME
[Ad] Endereço:Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, California 91125, USA.
[Ti] Título:Ancient evolutionary origin of vertebrate enteric neurons from trunk-derived neural crest.
[So] Source:Nature;544(7648):88-91, 2017 04 06.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The enteric nervous system of jawed vertebrates arises primarily from vagal neural crest cells that migrate to the foregut and subsequently colonize and innervate the entire gastrointestinal tract. Here we examine development of the enteric nervous system in the basal jawless vertebrate the sea lamprey (Petromyzon marinus) to gain insight into its evolutionary origin. Surprisingly, we find no evidence for the existence of a vagally derived enteric neural crest population in the lamprey. Rather, labelling with the lipophilic dye DiI shows that late-migrating cells, originating from the trunk neural tube and associated with nerve fibres, differentiate into neurons within the gut wall and typhlosole. We propose that these trunk-derived neural crest cells may be homologous to Schwann cell precursors, recently shown in mammalian embryos to populate post-embryonic parasympathetic ganglia, including enteric ganglia. Our results suggest that neural-crest-derived Schwann cell precursors made an important contribution to the ancient enteric nervous system of early jawless vertebrates, a role that was largely subsumed by vagal neural crest cells in early gnathostomes.
[Mh] Termos MeSH primário: Evolução Biológica
Sistema Nervoso Entérico/citologia
Sistema Nervoso Entérico/embriologia
Crista Neural/citologia
Neurônios/citologia
Petromyzon/embriologia
Tronco/embriologia
[Mh] Termos MeSH secundário: Animais
Diferenciação Celular
Linhagem da Célula
Movimento Celular
Gânglios/citologia
Gânglios/embriologia
Fibras Nervosas
Crista Neural/embriologia
Tubo Neural/citologia
Tubo Neural/embriologia
Células de Schwann/citologia
Nervo Vago/citologia
Nervo Vago/embriologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE
[do] DOI:10.1038/nature21679


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[PMID]:28285380
[Au] Autor:Chan YY; Sandlin SK; Kurzrock EA
[Ad] Endereço:Department of Urology, University of California Davis Children's Hospital, Sacramento, CA, 95817, USA.
[Ti] Título:Urological Outcomes of Myelomeningocele and Lipomeningocele.
[So] Source:Curr Urol Rep;18(5):35, 2017 May.
[Is] ISSN:1534-6285
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PURPOSE OF REVIEW: Spina bifida is caused by incomplete neural tube closure during the first trimester. This condition may lead to bowel and bladder dysfunction as well as truncal weakness and motor anomalies. Presentations vary between myelomeningoceles and lipomeningoceles and may result in different outcomes. This review seeks to explore our current understanding of the variations in outcomes between individuals with myelomeningocele and lipomeningocele. RECENT FINDINGS: Prenatal intervention has become a standard of care for prenatal diagnoses of myelomeningocele and has been shown to reduce shunt placement and improve motor skills. However, urological benefit from early intervention remains to be seen. Early surgical repair, however, may be beneficial for patients with lipomeningocele. Literature on the urological outcomes of patients with myelomeningocele and lipomeningocele is lacking. Further research is needed to better elucidate differences in long-term urological outcomes between these two pathologies.
[Mh] Termos MeSH primário: Meningomielocele/complicações
Tubo Neural/embriologia
Doenças Urológicas/etiologia
[Mh] Termos MeSH secundário: Feminino
Seres Humanos
Sistema Nervoso/embriologia
Bexiga Urinaria Neurogênica/etiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170313
[St] Status:MEDLINE
[do] DOI:10.1007/s11934-017-0684-9


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[PMID]:28264835
[Au] Autor:Xin D; Christopher KJ; Zeng L; Kong Y; Weatherbee SD
[Ad] Endereço:Department of Genetics, Yale University, New Haven, CT 06520, USA.
[Ti] Título:IFT56 regulates vertebrate developmental patterning by maintaining IFTB complex integrity and ciliary microtubule architecture.
[So] Source:Development;144(8):1544-1553, 2017 04 15.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cilia are key regulators of animal development and depend on intraflagellar transport (IFT) proteins for their formation and function, yet the roles of individual IFT proteins remain unclear. We examined the mouse mutant and reveal novel insight into the function of IFT56, a poorly understood IFTB protein. mice have normal cilia distribution but display defective cilia structure, including abnormal positioning and number of ciliary microtubule doublets. We show that cilia are unable to accumulate Gli proteins efficiently, resulting in developmental patterning defects in Shh signaling-dependent tissues such as the limb and neural tube. Strikingly, core IFTB proteins are unable to accumulate normally within cilia, including IFT88, IFT81 and IFT27, which are crucial for key processes such as tubulin transport and Shh signaling. IFT56 is required specifically for the IFTB complex, as IFTA components and proteins that rely on IFTA function are unaffected in cilia. These studies define a distinct and novel role for IFT56 in IFTB complex integrity that is crucial for cilia structure and function and, ultimately, animal development.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Padronização Corporal
Cílios/metabolismo
Microtúbulos/metabolismo
Vertebrados/embriologia
Vertebrados/metabolismo
[Mh] Termos MeSH secundário: Animais
Axonema/metabolismo
Axonema/ultraestrutura
Cílios/ultraestrutura
Códon sem Sentido/genética
Proteínas Hedgehog/metabolismo
Camundongos
Camundongos Endogâmicos C57BL
Microtúbulos/ultraestrutura
Tubo Neural/metabolismo
Fenótipo
Polidactilia/patologia
Transdução de Sinais
Proteína GLI1 em Dedos de Zinco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Codon, Nonsense); 0 (Hedgehog Proteins); 0 (Zinc Finger Protein GLI1)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170308
[St] Status:MEDLINE
[do] DOI:10.1242/dev.143255



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