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Pesquisa : D03.383.533.640.562 [Categoria DeCS]
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  1 / 907 MEDLINE  
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[PMID]:29214789
[Au] Autor:Kim CW; Han JH; Wu L; Choi JY
[Ad] Endereço:Department of Otorhinolaryngology, Hallym University College of Medicine, Seoul, Korea.
[Ti] Título:microRNA-183 is Essential for Hair Cell Regeneration after Neomycin Injury in Zebrafish.
[So] Source:Yonsei Med J;59(1):141-147, 2018 Jan.
[Is] ISSN:1976-2437
[Cp] País de publicação:Korea (South)
[La] Idioma:eng
[Ab] Resumo:PURPOSE: microRNAs (miRNAs) are non-coding RNAs composed of 20 to 22 nucleotides that regulate development and differentiation in various organs by silencing specific RNAs and regulating gene expression. In the present study, we show that the microRNA (miR)-183 cluster is upregulated during hair cell regeneration and that its inhibition reduces hair cell regeneration following neomycin-induced ototoxicity in zebrafish. MATERIALS AND METHODS: miRNA expression patterns after neomycin exposure were analyzed using microarray chips. Quantitative polymerase chain reaction was performed to validate miR-183 cluster expression patterns following neomycin exposure (500 µM for 2 h). After injection of an antisense morpholino (MO) to miR-183 (MO-183) immediately after fertilization, hair cell regeneration after neomycin exposure in neuromast cells was evaluated by fluorescent staining (YO-PRO1). The MO-183 effect also was assessed in transgenic zebrafish larvae expressing green fluorescent protein (GFP) in inner ear hair cells. RESULTS: Microarray analysis clearly showed that the miR-183 cluster (miR-96, miR-182, and miR-183) was upregulated after neomycin treatment. We also confirmed upregulated expression of the miR-183 cluster during hair cell regeneration after neomycin-induced ototoxicity. miR-183 inhibition using MO-183 reduced hair cell regeneration in both wild-type and GFP transgenic zebrafish larvae. CONCLUSION: Our work demonstrates that the miR-183 cluster is essential for the regeneration of hair cells following ototoxic injury in zebrafish larvae. Therefore, regulation of the miR-183 cluster can be a novel target for stimulation of hair cell regeneration.
[Mh] Termos MeSH primário: Células Ciliadas Auditivas/fisiologia
MicroRNAs/metabolismo
Regeneração/genética
Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Contagem de Células
Perfilação da Expressão Gênica
Regulação da Expressão Gênica/efeitos dos fármacos
Técnicas de Silenciamento de Genes
Proteínas de Fluorescência Verde/metabolismo
Células Ciliadas Auditivas/efeitos dos fármacos
Larva/efeitos dos fármacos
Larva/genética
MicroRNAs/genética
Morfolinos/farmacologia
Neomicina/toxicidade
Regeneração/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MIRN183 microRNA, zebrafish); 0 (MicroRNAs); 0 (Morpholinos); 1404-04-2 (Neomycin); 147336-22-9 (Green Fluorescent Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171208
[St] Status:MEDLINE
[do] DOI:10.3349/ymj.2018.59.1.141


  2 / 907 MEDLINE  
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[PMID]:29331378
[Au] Autor:Paone C; Rudeck S; Etard C; Strähle U; Rottbauer W; Just S
[Ad] Endereço:Molecular Cardiology, Department of Inner Medicine II, University of Ulm, Ulm, Germany.
[Ti] Título:Loss of zebrafish Smyd1a interferes with myofibrillar integrity without triggering the misfolded myosin response.
[So] Source:Biochem Biophys Res Commun;496(2):339-345, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sarcomeric protein turnover needs to be tightly balanced to assure proper assembly and renewal of sarcomeric units within muscle tissues. The mechanisms regulating these fundamental processes are only poorly understood, but of great clinical importance since many cardiac and skeletal muscle diseases are associated with defective sarcomeric organization. The SET- and MYND domain containing protein 1b (Smyd1b) is known to play a crucial role in myofibrillogenesis by functionally interacting with the myosin chaperones Unc45b and Hsp90α1. In zebrafish, Smyd1b, Unc45b and Hsp90α1 are part of the misfolded myosin response (MMR), a regulatory transcriptional response that is activated by disturbed myosin homeostasis. Genome duplication in zebrafish led to a second smyd1 gene, termed smyd1a. Morpholino- and CRISPR/Cas9-mediated knockdown of smyd1a led to significant perturbations in sarcomere structure resulting in decreased cardiac as well as skeletal muscle function. Similar to Smyd1b, we found Smyd1a to localize to the sarcomeric M-band in skeletal and cardiac muscles. Overexpression of smyd1a efficiently compensated for the loss of Smyd1b in flatline (fla) mutant zebrafish embryos, rescued the myopathic phenotype and suppressed the MMR in Smyd1b-deficient embryos, suggesting overlapping functions of both Smyd1 paralogs. Interestingly, Smyd1a is not transcriptionally activated in Smyd1b-deficient fla mutants, demonstrating lack of genetic compensation despite the functional redundancy of both zebrafish Smyd1 paralogs.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica no Desenvolvimento
Histona-Lisina N-Metiltransferase/genética
Músculo Esquelético/metabolismo
Miócitos Cardíacos/metabolismo
Miosinas/genética
Sarcômeros/metabolismo
Proteínas de Peixe-Zebra/genética
Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Sistemas CRISPR-Cas
Embrião não Mamífero
Duplicação Gênica
Edição de Genes
Genes Reporter
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Proteínas de Choque Térmico HSP90/genética
Proteínas de Choque Térmico HSP90/metabolismo
Histona-Lisina N-Metiltransferase/antagonistas & inibidores
Histona-Lisina N-Metiltransferase/deficiência
Seres Humanos
Chaperonas Moleculares/genética
Chaperonas Moleculares/metabolismo
Morfolinos/genética
Morfolinos/metabolismo
Músculo Esquelético/patologia
Miócitos Cardíacos/patologia
Miosinas/metabolismo
Dobramento de Proteína
Isoformas de Proteínas/deficiência
Isoformas de Proteínas/genética
Sarcômeros/patologia
Peixe-Zebra/crescimento & desenvolvimento
Peixe-Zebra/metabolismo
Proteínas de Peixe-Zebra/antagonistas & inibidores
Proteínas de Peixe-Zebra/deficiência
Proteínas de Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (HSP90 Heat-Shock Proteins); 0 (Molecular Chaperones); 0 (Morpholinos); 0 (Protein Isoforms); 0 (Unc45b protein, zebrafish); 0 (Zebrafish Proteins); 147336-22-9 (Green Fluorescent Proteins); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase); EC 2.1.1.43 (SmyD1 protein, zebrafish); EC 3.6.4.1 (Myosins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180115
[St] Status:MEDLINE


  3 / 907 MEDLINE  
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[PMID]:29178643
[Au] Autor:Yuan Q; Zhao M; Tandon B; Maili L; Liu X; Zhang A; Baugh EH; Tran T; Silva RM; Hecht JT; Swindell EC; Wagner DS; Letra A
[Ad] Endereço:Department of Pediatrics, University of Texas Health Science Center at Houston Medical School, Houston, Texas.
[Ti] Título:Role of WNT10A in failure of tooth development in humans and zebrafish.
[So] Source:Mol Genet Genomic Med;5(6):730-741, 2017 11.
[Is] ISSN:2324-9269
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Oligodontia is a severe form of tooth agenesis characterized by the absence of six or more permanent teeth. Oligodontia has complex etiology and variations in numerous genes have been suggested as causal for the condition. METHODS: We applied whole-exome sequencing (WES) to identify the cause of oligodontia in a 9-year-old girl missing 11 permanent teeth. Protein modeling and functional analysis in zebrafish were also performed to understand the impact of identified variants on the phenotype. RESULTS: We identified a novel compound heterozygous missense mutation in WNT10A (c.637G>A:p.Gly213Ser and c.1070C>T:p.Thr357Ile) as the likely cause of autosomal recessive oligodontia in the child. Affected residues are located in conserved regions and variants are predicted to be highly deleterious for potentially destabilizing the protein fold and inhibiting normal protein function. Functional studies in zebrafish embryos showed that wnt10a is expressed in the craniofacies at critical time points for tooth development, and that perturbations of wnt10a expression impaired normal tooth development and arrested tooth development at 5 days postfertilization (dpf). Furthermore, mRNA expression levels of additional tooth development genes were directly correlated with wnt10a expression; expression of msx1, dlx2b, eda, and axin2 was decreased upon wnt10a knockdown, and increased upon wnt10a overexpression. CONCLUSIONS: Our results reveal a novel compound heterozygous variant in WNT10A as pathogenic for oligodontia, and demonstrate that perturbations of wnt10a expression in zebrafish may directly and/or indirectly affect tooth development recapitulating the agenesis phenotype observed in humans.
[Mh] Termos MeSH primário: Anodontia/genética
Dente/crescimento & desenvolvimento
Proteínas Wnt/genética
Proteínas de Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Animais Geneticamente Modificados/genética
Anodontia/diagnóstico
Sequência de Bases
Criança
Dentição Permanente
Embrião não Mamífero/metabolismo
Feminino
Heterozigoto
Seres Humanos
Modelos Animais
Morfolinos/genética
Morfolinos/metabolismo
Fenótipo
Estrutura Terciária de Proteína
Dente/patologia
Sequenciamento Completo do Exoma
Proteínas Wnt/química
Proteínas Wnt/metabolismo
Peixe-Zebra/genética
Proteínas de Peixe-Zebra/antagonistas & inibidores
Proteínas de Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Morpholinos); 0 (WNT10A protein, human); 0 (Wnt Proteins); 0 (Zebrafish Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1002/mgg3.332


  4 / 907 MEDLINE  
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[PMID]:28934490
[Au] Autor:Joris M; Schloesser M; Baurain D; Hanikenne M; Muller M; Motte P
[Ad] Endereço:Laboratory of Functional Genomics and Plant Molecular Imaging, InBioS, PhytoSystems and Centre for Assistance in Technology of Microscopy (CAREm), University of Liège, 4000 Liège, Belgium.
[Ti] Título:Number of inadvertent RNA targets for morpholino knockdown in Danio rerio is largely underestimated: evidence from the study of Ser/Arg-rich splicing factors.
[So] Source:Nucleic Acids Res;45(16):9547-9557, 2017 Sep 19.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Although the involvement of Ser/Arg-rich (SR) proteins in RNA metabolism is well documented, their role in vertebrate development remains elusive. We, therefore, elected to take advantage of the zebrafish model organism to study the SR genes' functions using the splicing morpholino (sMO) microinjection and the programmable site-specific nucleases. Consistent with previous research, we revealed discrepancies between the mutant and morphant phenotypes and we show that these inconsistencies may result from a large number of unsuspected inadvertent morpholino RNA targets. While microinjection of MOs directed against srsf5a (sMOsrsf5a) led to developmental defects, the corresponding homozygous mutants did not display any phenotypic traits. Furthermore, microinjection of sMOsrsf5a into srsf5a-/- led to the previously observed morphant phenotype. Similar findings were observed for other SR genes. sMOsrsf5a alternative target genes were identified using deep mRNA sequencing. We uncovered that only 11 consecutive bases complementary to sMOsrsf5a are sufficient for binding and subsequent blocking of splice sites. In addition, we observed that sMOsrsf5a secondary targets can be reduced by increasing embryos growth temperature after microinjection. Our data contribute to the debate about MO specificity, efficacy and the number of unknown targeted sequences.
[Mh] Termos MeSH primário: Morfolinos/farmacologia
Fatores de Processamento de Serina-Arginina/genética
Proteínas de Peixe-Zebra/genética
Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Animais
Embrião não Mamífero
Técnicas de Silenciamento de Genes
Microinjeções
Sítios de Splice de RNA
Fatores de Processamento de Serina-Arginina/metabolismo
Peixe-Zebra/embriologia
Proteínas de Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Morpholinos); 0 (RNA Splice Sites); 0 (Zebrafish Proteins); 170974-22-8 (Serine-Arginine Splicing Factors)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170922
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx638


  5 / 907 MEDLINE  
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[PMID]:28823919
[Au] Autor:Kobayashi D; Asano-Hoshino A; Nakakura T; Nishimaki T; Ansai S; Kinoshita M; Ogawa M; Hagiwara H; Yokoyama T
[Ad] Endereço:Department of Anatomy and Developmental Biology, Graduate School of Medical Science, Kyoto Prefectural University of Medicine, Kyoto, Japan. Electronic address: kdaisuke@koto.kpu-m.ac.jp.
[Ti] Título:Loss of zinc finger MYND-type containing 10 (zmynd10) affects cilia integrity and axonemal localization of dynein arms, resulting in ciliary dysmotility, polycystic kidney and scoliosis in medaka (Oryzias latipes).
[So] Source:Dev Biol;430(1):69-79, 2017 10 01.
[Is] ISSN:1095-564X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cilia and flagella are hair-like organelles that project from the cell surface and play important roles in motility and sensory perception. Motility defects in cilia and flagella lead to primary ciliary dyskinesia (PCD), a rare human disease. Recently zinc finger MYND-type containing 10 (ZMYND10) was identified in humans as a PCD-associated gene. In this study, we use medaka fish as a model to characterize the precise functions of zmynd10. In medaka, zmynd10 is exclusively expressed in cells with motile cilia. Embryos with zmynd10 Morpholino knockdown exhibited a left-right (LR) defect associated with loss of motility in Kupffer's vesicle (KV) cilia. This immotility was caused by loss of the outer dynein arms, which is a characteristic ultrastructural phenotype in PCD. In addition, KV cilia in zmynd10 knockdown embryos had a swollen and wavy morphology. Together, these results suggest that zmynd10 is a multi-functional protein that has independent roles in axonemal localization of dynein arms and in formation and/or maintenance of cilia. The C-terminal region of zmynd10 has a MYND-type zinc finger domain (zf-MYND) that is important for its function. Our rescue experiment showed that the zmynd10-ΔC truncated protein, which lacks zf-MYND, was still partially functional, suggesting that zmynd10 has another functional domain besides zf-MYND. To analyze the later stages of development, we generated a zmynd10 knockout mutant using transcription activator-like effector nuclease (TALEN) technology. Adult mutants exhibited sperm dysmotility, scoliosis and progressive polycystic kidney.
[Mh] Termos MeSH primário: Axonema/metabolismo
Cílios/metabolismo
Dineínas/metabolismo
Oryzias/metabolismo
Doenças Renais Policísticas/metabolismo
Escoliose/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Axonema/efeitos dos fármacos
Sequência de Bases
Padronização Corporal/efeitos dos fármacos
Padronização Corporal/genética
Cílios/efeitos dos fármacos
Embrião não Mamífero/efeitos dos fármacos
Embrião não Mamífero/metabolismo
Epistasia Genética/efeitos dos fármacos
Regulação da Expressão Gênica no Desenvolvimento/efeitos dos fármacos
Masculino
Morfolinos/farmacologia
Movimento
Oryzias/embriologia
Oryzias/genética
Fenótipo
Doenças Renais Policísticas/patologia
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Escoliose/patologia
Espermatozoides/metabolismo
Proteínas Supressoras de Tumor/química
Proteínas Supressoras de Tumor/genética
Proteínas Supressoras de Tumor/metabolismo
Dedos de Zinco
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Morpholinos); 0 (RNA, Messenger); 0 (Tumor Suppressor Proteins); EC 3.6.4.2 (Dyneins)
[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:170822
[St] Status:MEDLINE


  6 / 907 MEDLINE  
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[PMID]:28808058
[Au] Autor:Seguin A; Takahashi-Makise N; Yien YY; Huston NC; Whitman JC; Musso G; Wallace JA; Bradley T; Bergonia HA; Kafina MD; Matsumoto M; Igarashi K; Phillips JD; Paw BH; Kaplan J; Ward DM
[Ad] Endereço:From the Division of Microbiology and Immunology, Department of Pathology, and.
[Ti] Título:Reductions in the mitochondrial ABC transporter Abcb10 affect the transcriptional profile of heme biosynthesis genes.
[So] Source:J Biol Chem;292(39):16284-16299, 2017 Sep 29.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:ATP-binding cassette subfamily B member 10 (Abcb10) is a mitochondrial ATP-binding cassette (ABC) transporter that complexes with mitoferrin1 and ferrochelatase to enhance heme biosynthesis in developing red blood cells. Reductions in Abcb10 levels have been shown to reduce mitoferrin1 protein levels and iron import into mitochondria, resulting in reduced heme biosynthesis. As an ABC transporter, Abcb10 binds and hydrolyzes ATP, but its transported substrate is unknown. Here, we determined that decreases in Abcb10 did not result in protoporphyrin IX accumulation in morphant-treated zebrafish embryos or in differentiated Abcb10-specific shRNA murine Friend erythroleukemia (MEL) cells in which Abcb10 was specifically silenced with shRNA. We also found that the ATPase activity of Abcb10 is necessary for hemoglobinization in MEL cells, suggesting that the substrate transported by Abcb10 is important in mediating increased heme biosynthesis during erythroid development. Inhibition of 5-aminolevulinic acid dehydratase (EC 4.2.1.24) with succinylacetone resulted in both 5-aminolevulinic acid (ALA) accumulation in control and Abcb10-specific shRNA MEL cells, demonstrating that reductions in Abcb10 do not affect ALA export from mitochondria and indicating that Abcb10 does not transport ALA. Abcb10 silencing resulted in an alteration in the heme biosynthesis transcriptional profile due to repression by the transcriptional regulator Bach1, which could be partially rescued by overexpression of Alas2 or Gata1, providing a mechanistic explanation for why Abcb10 shRNA MEL cells exhibit reduced hemoglobinization. In conclusion, our findings rule out that Abcb10 transports ALA and indicate that Abcb10's ATP-hydrolysis activity is critical for hemoglobinization and that the substrate transported by Abcb10 provides a signal that optimizes hemoglobinization.
[Mh] Termos MeSH primário: Transportadores de Cassetes de Ligação de ATP/metabolismo
Fatores de Transcrição de Zíper de Leucina Básica/metabolismo
Regulação Enzimológica da Expressão Gênica
Heme/biossíntese
Proteínas de Peixe-Zebra/metabolismo
[Mh] Termos MeSH secundário: Transportadores de Cassetes de Ligação de ATP/antagonistas & inibidores
Transportadores de Cassetes de Ligação de ATP/química
Transportadores de Cassetes de Ligação de ATP/genética
Motivos de Aminoácidos
Substituição de Aminoácidos
Animais
Fatores de Transcrição de Zíper de Leucina Básica/antagonistas & inibidores
Fatores de Transcrição de Zíper de Leucina Básica/genética
Embrião não Mamífero/enzimologia
Embrião não Mamífero/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Seres Humanos
Camundongos
Microinjeções
Morfolinos/metabolismo
Mutação
Interferência de RNA
RNA Interferente Pequeno
Peixe-Zebra
Proteínas de Peixe-Zebra/antagonistas & inibidores
Proteínas de Peixe-Zebra/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABCB10 protein, human); 0 (Abcb10 protein, zebrafish); 0 (Bach1 protein, mouse); 0 (Bach1 protein, zebrafish); 0 (Basic-Leucine Zipper Transcription Factors); 0 (Morpholinos); 0 (RNA, Small Interfering); 0 (Zebrafish Proteins); 147336-22-9 (Green Fluorescent Proteins); 42VZT0U6YR (Heme)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170816
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.797415


  7 / 907 MEDLINE  
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[PMID]:28781168
[Au] Autor:Wong HH; Lin JQ; Ströhl F; Roque CG; Cioni JM; Cagnetta R; Turner-Bridger B; Laine RF; Harris WA; Kaminski CF; Holt CE
[Ad] Endereço:Department of Physiology, Development and Neuroscience, University of Cambridge, Cambridge CB2 3DY, UK.
[Ti] Título:RNA Docking and Local Translation Regulate Site-Specific Axon Remodeling In Vivo.
[So] Source:Neuron;95(4):852-868.e8, 2017 Aug 16.
[Is] ISSN:1097-4199
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nascent proteins can be positioned rapidly at precise subcellular locations by local protein synthesis (LPS) to facilitate localized growth responses. Axon arbor architecture, a major determinant of synaptic connectivity, is shaped by localized growth responses, but it is unknown whether LPS influences these responses in vivo. Using high-resolution live imaging, we examined the spatiotemporal dynamics of RNA and LPS in retinal axons during arborization in vivo. Endogenous RNA tracking reveals that RNA granules dock at sites of branch emergence and invade stabilized branches. Live translation reporter analysis reveals that de novo ß-actin hotspots colocalize with docked RNA granules at the bases and tips of new branches. Inhibition of axonal ß-actin mRNA translation disrupts arbor dynamics primarily by reducing new branch emergence and leads to impoverished terminal arbors. The results demonstrate a requirement for LPS in building arbor complexity and suggest a key role for pre-synaptic LPS in assembling neural circuits.
[Mh] Termos MeSH primário: Axônios/fisiologia
Regulação da Expressão Gênica no Desenvolvimento/genética
RNA/metabolismo
[Mh] Termos MeSH secundário: Actinas/genética
Actinas/metabolismo
Animais
Anisomicina/farmacologia
Biotina/metabolismo
Blastômeros
Carbocianinas/metabolismo
Cicloeximida/farmacologia
Nucleotídeos de Desoxiuracil/metabolismo
Embrião não Mamífero
Regulação da Expressão Gênica no Desenvolvimento/efeitos dos fármacos
Técnicas In Vitro
Proteínas Luminescentes/genética
Proteínas Luminescentes/metabolismo
Mitocôndrias/metabolismo
Morfolinos/farmacologia
Oligonucleotídeos Antissenso/farmacologia
Técnicas de Cultura de Órgãos
Inibidores da Síntese de Proteínas/farmacologia
RNA/genética
Retina/citologia
Xenopus laevis
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3'-deoxy-5-(cyanine dye 5)uridine 5'-trisphosphate); 0 (Actins); 0 (Carbocyanines); 0 (Deoxyuracil Nucleotides); 0 (Luminescent Proteins); 0 (Morpholinos); 0 (Oligonucleotides, Antisense); 0 (Protein Synthesis Inhibitors); 63231-63-0 (RNA); 6C74YM2NGI (Anisomycin); 6SO6U10H04 (Biotin); 98600C0908 (Cycloheximide)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170902
[Lr] Data última revisão:
170902
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170808
[St] Status:MEDLINE


  8 / 907 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


  9 / 907 MEDLINE  
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[PMID]:28760346
[Au] Autor:D'Agati G; Beltre R; Sessa A; Burger A; Zhou Y; Mosimann C; White RM
[Ad] Endereço:Institute of Molecular Life Sciences, University of Zürich, Zürich, Switzerland.
[Ti] Título:A defect in the mitochondrial protein Mpv17 underlies the transparent casper zebrafish.
[So] Source:Dev Biol;430(1):11-17, 2017 10 01.
[Is] ISSN:1095-564X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The casper strain of zebrafish is widely used in studies ranging from cancer to neuroscience. casper offers the advantage of relative transparency throughout adulthood, making it particularly useful for in vivo imaging by epifluorescence, confocal, and light sheet microscopy. casper was developed by selective breeding of two previously described recessive pigment mutants: 1) nacre, which harbors an inactivating mutation of the mitfa gene, rendering the fish devoid of pigmented melanocytes; and 2) roy orbison, a mutant with a so-far unidentified genetic cause that lacks reflective iridophores. To clarify the molecular nature of the roy orbison mutation, such that it can inform studies using casper, we undertook an effort to positionally clone the roy orbison mutation. We find that roy orbison is caused by an intronic defect in the gene mpv17, encoding an inner mitochondrial membrane protein that has been implicated in the human mitochondrial DNA depletion syndrome. The roy orbison mutation is phenotypically and molecularly remarkably similar to another zebrafish iridophore mutant called transparent. Using Cas9-induced crispants and germline mutants with a disrupted mpv17 open reading frame, we show in trans-heterozygote embryos that new frameshift alleles of mpv17, roy orbison, and transparent fail to complement each other. Our work provides genetic evidence that both roy orbison and transparent affect the mpv17 locus by a similar if not identical genetic lesion. Identification of mpv17 mutants will allow for further work probing the relationship between mitochondrial function and pigmentation, which has to date received little attention.
[Mh] Termos MeSH primário: Proteínas de Membrana/genética
Proteínas Mitocondriais/genética
Mutação/genética
Proteínas de Peixe-Zebra/genética
Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Alelos
Animais
Pareamento de Bases/genética
Sequência de Bases
Sistemas CRISPR-Cas/genética
Mapeamento Cromossômico
DNA Mitocondrial/genética
Técnicas de Silenciamento de Genes
Loci Gênicos
Proteínas Mitocondriais/metabolismo
Morfolinos/farmacologia
Mutagênese/genética
Fenótipo
Pigmentação/efeitos dos fármacos
Pigmentação/genética
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Mitochondrial); 0 (Membrane Proteins); 0 (Mitochondrial Proteins); 0 (Morpholinos); 0 (Mpv17 protein, zebrafish); 0 (RNA, Messenger); 0 (Zebrafish 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:170802
[St] Status:MEDLINE


  10 / 907 MEDLINE  
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[PMID]:28692664
[Au] Autor:Williams RM; Winkfein RJ; Ginger RS; Green MR; Schnetkamp PP; Wheeler GN
[Ad] Endereço:School of Biological Sciences, University of East Anglia, Norwich, United Kingdom.
[Ti] Título:A functional approach to understanding the role of NCKX5 in Xenopus pigmentation.
[So] Source:PLoS One;12(7):e0180465, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:NCKX5 is an ion exchanger expressed mostly in pigment cells; however, the functional role for this protein in melanogenesis is not clear. A variant allele of SLC24A5, the gene encoding NCKX5, has been shown to correlate with lighter skin pigmentation in humans, indicating a key role for SLC24A5 in determining human skin colour. SLC24A5 expression has been found to be elevated in melanoma. Knockdown analyses have shown SLC24A5 to be important for pigmentation, but to date the function of this ion exchanger in melanogenesis has not been fully established. Our data suggest NCKX5 may have an alternative activity that is key to its role in the regulation of pigmentation. Here Xenopus laevis is employed as an in vivo model system to further investigate the function of NCKX5 in pigmentation. SLC24A5 is expressed in the melanophores as they differentiate from the neural crest and develop in the RPE of the eye. Morpholino knockdown and rescue experiments were designed to elucidate key residues and regions of the NCKX5 protein. Unilateral morpholino injection at the 2 cell stage resulted in a reduction of pigmentation in the eye and epidermis of one lateral side of the tadpole. Xenopus and human SLC24A5 can rescue the morpholino effects. Further rescue experiments including the use of ion exchange inactive SLC24A5 constructs raise the possibility that full ion exchanger function of NCKX5 may not be required for rescue of pigmentation.
[Mh] Termos MeSH primário: Pigmentação da Pele/genética
Trocador de Sódio e Cálcio/genética
Proteínas de Xenopus/genética
Xenopus laevis/genética
[Mh] Termos MeSH secundário: Animais
Regulação da Expressão Gênica no Desenvolvimento/efeitos dos fármacos
Técnicas de Silenciamento de Genes
Morfolinos/farmacologia
Mutação/genética
Fenótipo
Pigmentação da Pele/efeitos dos fármacos
Trocador de Sódio e Cálcio/metabolismo
Proteínas de Xenopus/metabolismo
Xenopus laevis/embriologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Morpholinos); 0 (Sodium-Calcium Exchanger); 0 (Xenopus Proteins)
[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:170711
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180465



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