Base de dados : MEDLINE
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  1 / 2919 MEDLINE  
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[PMID]:29340527
[Au] Autor:Ribeiro LP; Freitas-Lima LC; Naumann GB; Meyrelles SS; Lunz W; Pires SF; Andrade HM; Carnielli JBT; Figueiredo SG
[Ad] Endereço:Departamento de Ciências Fisiológicas, Universidade Federal do Espírito Santo, Vitória, ES, Brasil.
[Ti] Título:Cardiac protein expression patterns are associated with distinct inborn exercise capacity in non-selectively bred rats.
[So] Source:Braz J Med Biol Res;51(3):e7033, 2018 Jan 11.
[Is] ISSN:1414-431X
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:In the present study, we successfully demonstrated for the first time the existence of cardiac proteomic differences between non-selectively bred rats with distinct intrinsic exercise capacities. A proteomic approach based on two-dimensional gel electrophoresis coupled to mass spectrometry was used to study the left ventricle (LV) tissue proteome of rats with distinct intrinsic exercise capacity. Low running performance (LRP) and high running performance (HRP) rats were categorized by a treadmill exercise test, according to distance run to exhaustion. The running capacity of HRPs was 3.5-fold greater than LRPs. Protein profiling revealed 29 differences between HRP and LRP rats (15 proteins were identified). We detected alterations in components involved in metabolism, antioxidant and stress response, microfibrillar and cytoskeletal proteins. Contractile proteins were upregulated in the LVs of HRP rats (α-myosin heavy chain-6, myosin light chain-1 and creatine kinase), whereas the LVs of LRP rats exhibited upregulation in proteins associated with stress response (aldehyde dehydrogenase 2, α-crystallin B chain and HSPß-2). In addition, the cytoskeletal proteins desmin and α-actin were upregulated in LRPs. Taken together, our results suggest that the increased contractile protein levels in HRP rats partly accounted for their improved exercise capacity, and that proteins considered risk factors to the development of cardiovascular disease were expressed in higher amounts in LRP animals.
[Mh] Termos MeSH primário: Testes de Função Cardíaca/métodos
Miocárdio/metabolismo
Condicionamento Físico Animal/fisiologia
Proteínas/metabolismo
Corrida/fisiologia
[Mh] Termos MeSH secundário: Animais
Proteínas Contráteis/metabolismo
Proteínas do Citoesqueleto/metabolismo
Desmina/metabolismo
Eletroforese em Gel Bidimensional
Ventrículos do Coração/metabolismo
Proteínas de Choque Térmico/metabolismo
Masculino
Espectrometria de Massas
Tamanho do Órgão
Proteínas/isolamento & purificação
Proteômica
Ratos
Ratos Endogâmicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Contractile Proteins); 0 (Cytoskeletal Proteins); 0 (Desmin); 0 (Heat-Shock Proteins); 0 (Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180301
[Lr] Data última revisão:
180301
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE


  2 / 2919 MEDLINE  
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[PMID]:27773687
[Au] Autor:Ulrich AKC; Seeger M; Schütze T; Bartlick N; Wahl MC
[Ad] Endereço:Laboratory of Structural Biochemistry, Freie Universität Berlin, Takustraße 6, 14195 Berlin, Germany.
[Ti] Título:Scaffolding in the Spliceosome via Single α Helices.
[So] Source:Structure;24(11):1972-1983, 2016 11 01.
[Is] ISSN:1878-4186
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The spliceosomal B complex-specific protein Prp38 forms a complex with the intrinsically unstructured proteins MFAP1 and Snu23. Our binding and crystal structure analyses show that MFAP1 and Snu23 contact Prp38 via ER/K motif-stabilized single α helices, which have previously been recognized only as rigid connectors or force springs between protein domains. A variant of the Prp38-binding single α helix of MFAP1, in which ER/K motifs not involved in Prp38 binding were mutated, was less α-helical in isolation and showed a reduced Prp38 affinity, with opposing tendencies in interaction enthalpy and entropy. Our results indicate that the strengths of single α helix-based interactions can be tuned by the degree of helix stabilization in the unbound state. MFAP1, Snu23, and several other spliceosomal proteins contain multiple regions that likely form single α helices via which they might tether several binding partners and act as intermittent scaffolds that facilitate remodeling steps during assembly of an active spliceosome.
[Mh] Termos MeSH primário: Proteínas Contráteis/química
Proteínas da Matriz Extracelular/química
Fatores de Processamento de RNA/química
Ribonucleoproteínas Nucleares Pequenas/química
Spliceossomos/química
[Mh] Termos MeSH secundário: Sítios de Ligação
Dicroísmo Circular
Cristalografia por Raios X
Seres Humanos
Modelos Moleculares
Ligação Proteica
Estrutura Secundária de Proteína
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Contractile Proteins); 0 (Extracellular Matrix Proteins); 0 (RNA Splicing Factors); 0 (Ribonucleoproteins, Small Nuclear); 0 (microfibrillar protein)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171230
[Lr] Data última revisão:
171230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161103
[St] Status:MEDLINE


  3 / 2919 MEDLINE  
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[PMID]:28837687
[Au] Autor:Rode S; Ohm H; Zipfel J; Rumpf S
[Ad] Endereço:Institute for Neurobiology, University of Münster, Badestrasse 9, Münster, Germany.
[Ti] Título:The spliceosome-associated protein Mfap1 binds to VCP in Drosophila.
[So] Source:PLoS One;12(8):e0183733, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Posttranscriptional regulation of gene expression contributes to many developmental transitions. Previously, we found that the AAA chaperone Valosin-Containing Protein (VCP) regulates ecdysone-dependent dendrite pruning of Drosophila class IV dendritic arborization (c4da) neurons via an effect on RNA metabolism. In a search for RNA binding proteins associated with VCP, we identified the spliceosome-associated protein Mfap1, a component of the tri-snRNP complex. Mfap1 is a nucleolar protein in neurons and its levels are regulated by VCP. Mfap1 binds to VCP and TDP-43, a disease-associated RNA-binding protein. via distinct regions in its N- and C-terminal halfs. Similar to vcp mutations, Mfap1 overexpression causes c4da neuron dendrite pruning defects and mislocalization of TDP-43 in these cells, but genetic analyses show that Mfap1 is not a crucial VCP target during dendrite pruning. Finally, rescue experiments with a lethal mfap1 mutant show that the VCP binding region is not essential for Mfap1 function, but may act to increase its stability or activity.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
Proteínas Contráteis/metabolismo
Proteínas de Drosophila/metabolismo
Proteínas da Matriz Extracelular/metabolismo
Spliceossomos/metabolismo
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/genética
Animais
Regulação para Baixo
Drosophila
Proteínas de Drosophila/genética
Mutação
Neurônios/metabolismo
Nucleotídeos/metabolismo
Ligação Proteica
Proteína com Valosina
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Contractile Proteins); 0 (Drosophila Proteins); 0 (Extracellular Matrix Proteins); 0 (Nucleotides); 0 (microfibrillar protein); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.6 (Valosin Containing Protein); EC 3.6.4.6 (ter94 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:170825
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183733


  4 / 2919 MEDLINE  
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[PMID]:28476928
[Au] Autor:Gatfield J; Menyhart K; Wanner D; Gnerre C; Monnier L; Morrison K; Hess P; Iglarz M; Clozel M; Nayler O
[Ad] Endereço:Actelion Pharmaceuticals Ltd, Allschwil, Switzerland john.gatfield@actelion.com.
[Ti] Título:Selexipag Active Metabolite ACT-333679 Displays Strong Anticontractile and Antiremodeling Effects but Low -Arrestin Recruitment and Desensitization Potential.
[So] Source:J Pharmacol Exp Ther;362(1):186-199, 2017 Jul.
[Is] ISSN:1521-0103
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Prostacyclin (PGI ) receptor (IP receptor) agonists, which are indicated for the treatment of pulmonary arterial hypertension (PAH), increase cytosolic cAMP levels and thereby inhibit pulmonary vasoconstriction, pulmonary arterial smooth muscle cell (PASMC) proliferation, and extracellular matrix synthesis. Selexipag (Uptravi, 2-{4-[(5,6-diphenylpyrazin-2-yl)(isopropyl)amino]butoxy}- -(methylsulfonyl)acetamide) is the first nonprostanoid IP receptor agonist, it is available orally and was recently approved for the treatment of PAH. In this study we show that the active metabolite of selexipag and the main contributor to clinical efficacy ACT-333679 (previously known as MRE-269) behaved as a full agonist in multiple PAH-relevant receptor-distal-or downstream-cellular assays with a maximal efficacy ( ) comparable to that of the prototypic PGI analog iloprost. In PASMC, ACT-333679 potently induced cellular relaxation (EC 4.3 nM) and inhibited cell proliferation (IC 4.0 nM) as well as extracellular matrix synthesis (IC 8.3 nM). In contrast, ACT-333679 displayed partial agonism in receptor-proximal-or upstream-cAMP accumulation assays ( 56%) when compared with iloprost and the PGI analogs beraprost and treprostinil ( ∼100%). Partial agonism of ACT-333679 also resulted in limited -arrestin recruitment ( 40%) and lack of sustained IP receptor internalization, whereas all tested PGI analogs behaved as full agonists in these desensitization-related assays. In line with these in vitro findings, selexipag, but not treprostinil, displayed sustained efficacy in rat models of pulmonary and systemic hypertension. Thus, the partial agonism of ACT-333679 allows for full efficacy in amplified receptor-distal PAH-relevant readouts while causing limited activity in desensitization-related receptor-proximal readouts.
[Mh] Termos MeSH primário: Acetamidas/farmacologia
Acetatos/farmacologia
Proteínas Contráteis/antagonistas & inibidores
Contração Muscular/efeitos dos fármacos
Pirazinas/farmacologia
beta-Arrestinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Células CHO
Proliferação Celular/efeitos dos fármacos
Cricetinae
Cricetulus
AMP Cíclico/metabolismo
Epoprostenol/análogos & derivados
Epoprostenol/farmacologia
Matriz Extracelular/efeitos dos fármacos
Matriz Extracelular/metabolismo
Seres Humanos
Hipertensão Pulmonar/tratamento farmacológico
Hipertensão Pulmonar/fisiopatologia
Iloprosta/farmacologia
Masculino
Relaxamento Muscular/efeitos dos fármacos
Ratos
Ratos Endogâmicos SHR
Ratos Wistar
Receptores de Epoprostenol/agonistas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 ((4-((5,6-diphenylpyrazin-2-yl)(isopropyl)amino)butoxy)acetic acid); 0 (Acetamides); 0 (Acetates); 0 (Contractile Proteins); 0 (Pyrazines); 0 (Receptors, Epoprostenol); 0 (beta-Arrestins); 5EXC0E384L (selexipag); DCR9Z582X0 (Epoprostenol); E0399OZS9N (Cyclic AMP); JED5K35YGL (Iloprost); RUM6K67ESG (treprostinil)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170507
[St] Status:MEDLINE
[do] DOI:10.1124/jpet.116.239665


  5 / 2919 MEDLINE  
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[PMID]:28428257
[Au] Autor:Leal-Egaña A; Letort G; Martiel JL; Christ A; Vignaud T; Roelants C; Filhol O; Théry M
[Ad] Endereço:CytoMorpho Lab, LPCV, Biosciences and Biotechnology Institute of Grenoble, UMR5168, CEA, CNRS, INRA, Université Grenoble-Alpes, 38054 Grenoble, France.
[Ti] Título:The size-speed-force relationship governs migratory cell response to tumorigenic factors.
[So] Source:Mol Biol Cell;28(12):1612-1621, 2017 Jun 15.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tumor development progresses through a complex path of biomechanical changes leading first to cell growth and contraction and then cell deadhesion, scattering, and invasion. Tumorigenic factors may act specifically on one of these steps or have a wider spectrum of actions, leading to a variety of effects and thus sometimes to apparent contradictory outcomes. Here we used micropatterned lines of collagen type I/fibronectin on deformable surfaces to standardize cell behavior and measure simultaneously cell size, speed of motion and magnitude of the associated traction forces at the level of a single cell. We analyzed and compared the normal human breast cell line MCF10A in control conditions and in response to various tumorigenic factors. In all conditions, a wide range of biomechanical properties was identified. Despite this heterogeneity, normal and transformed motile cells followed a common trend whereby size and contractile forces were negatively correlated with cell speed. Some tumorigenic factors, such as activation of ErbB2 or loss of the ßsubunit of casein kinase 2, shifted the whole population toward a faster speed and lower contractility state. Treatment with transforming growth factor ß induced some cells to adopt opposing behaviors such as extremely high versus extremely low contractility. Thus tumor transformation amplified preexisting population heterogeneity and led some cells to exhibit biomechanical properties that were more extreme than those observed with normal cells.
[Mh] Termos MeSH primário: Fenômenos Biomecânicos/efeitos dos fármacos
Movimento Celular/efeitos dos fármacos
[Mh] Termos MeSH secundário: Fenômenos Biomecânicos/fisiologia
Neoplasias da Mama
Carcinogênese
Adesão Celular/efeitos dos fármacos
Linhagem Celular Tumoral/efeitos dos fármacos
Movimento Celular/fisiologia
Proliferação Celular
Tamanho Celular
Transformação Celular Neoplásica/efeitos dos fármacos
Colágeno Tipo I/efeitos dos fármacos
Proteínas Contráteis/efeitos dos fármacos
Feminino
Seres Humanos
Receptor ErbB-2/farmacologia
Fator de Crescimento Transformador beta/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Collagen Type I); 0 (Contractile Proteins); 0 (Transforming Growth Factor beta); EC 2.7.10.1 (ERBB2 protein, human); EC 2.7.10.1 (Receptor, ErbB-2)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170422
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-10-0694


  6 / 2919 MEDLINE  
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[PMID]:28335716
[Au] Autor:Ulrich AK; Wahl MC
[Ad] Endereço:Laboratory of Structural Biochemistry, Freie Universität Berlin, Takustr. 6, D-14195, Berlin, Germany. alexander.ulrich@fu-berlin.de.
[Ti] Título:Human MFAP1 is a cryptic ortholog of the Saccharomyces cerevisiae Spp381 splicing factor.
[So] Source:BMC Evol Biol;17(1):91, 2017 Mar 24.
[Is] ISSN:1471-2148
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Pre-mRNA splicing involves the stepwise assembly of a pre-catalytic spliceosome, followed by its catalytic activation, splicing catalysis and disassembly. Formation of the pre-catalytic spliceosomal B complex involves the incorporation of the U4/U6.U5 tri-snRNP and of a group of non-snRNP B-specific proteins. While in Saccharomyces cerevisiae the Prp38 and Snu23 proteins are recruited as components of the tri-snRNP, metazoan orthologs of Prp38 and Snu23 associate independently of the tri-snRNP as members of the B-specific proteins. The human spliceosome contains about 80 proteins that lack obvious orthologs in yeast, including most of the B-specific proteins apart from Prp38 and Snu23. Conversely, the tri-snRNP protein Spp381 is one of only five S. cerevisiae splicing factors without a known human ortholog. RESULTS: Using InParanoid, a state-of-the-art method for ortholog inference between pairs of species, and systematic BLAST searches we identified the human B-specific protein MFAP1 as a putative ortholog of the S. cerevisiae tri-snRNP protein Spp381. Bioinformatics revealed that MFAP1 and Spp381 share characteristic structural features, including intrinsic disorder, an elongated shape, solvent exposure of most residues and a trend to adopt α-helical structures. In vitro binding studies showed that human MFAP1 and yeast Spp381 bind their respective Prp38 proteins via equivalent interfaces and that they cross-interact with the Prp38 proteins of the respective other species. Furthermore, MFAP1 and Spp381 both form higher-order complexes that additionally include Snu23, suggesting that they are parts of equivalent spliceosomal sub-complexes. Finally, similar to yeast Spp381, human MFAP1 partially rescued a growth defect of the temperature-sensitive mutant yeast strain prp38-1. CONCLUSIONS: Human B-specific protein MFAP1 structurally and functionally resembles the yeast tri-snRNP-specific protein Spp381 and thus qualifies as its so far missing ortholog. Our study indicates that the yeast Snu23-Prp38-Spp381 triple complex was evolutionarily reprogrammed from a tri-snRNP-specific module in yeast to the B-specific Snu23-Prp38-MFAP1 module in metazoa, affording higher flexibility in spliceosome assembly and thus, presumably, in splicing regulation.
[Mh] Termos MeSH primário: Proteínas Contráteis/genética
Proteínas da Matriz Extracelular/genética
Fatores de Processamento de RNA/metabolismo
Processamento de RNA
[Mh] Termos MeSH secundário: Seres Humanos
Proteínas Nucleares/genética
Precursores de RNA/metabolismo
Ribonucleoproteína Nuclear Pequena U4-U6
Ribonucleoproteínas Nucleares Pequenas/genética
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Spliceossomos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Contractile Proteins); 0 (Extracellular Matrix Proteins); 0 (Nuclear Proteins); 0 (RNA Precursors); 0 (RNA Splicing Factors); 0 (Ribonucleoprotein, U4-U6 Small Nuclear); 0 (Ribonucleoproteins, Small Nuclear); 0 (Saccharomyces cerevisiae Proteins); 0 (Spp381 protein, S cerevisiae); 0 (microfibrillar protein)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170627
[Lr] Data última revisão:
170627
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170325
[St] Status:MEDLINE
[do] DOI:10.1186/s12862-017-0923-1


  7 / 2919 MEDLINE  
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[PMID]:28147230
[Au] Autor:Jananji S; Risi C; Lindamulage IKS; Picard LP; Van Sciver R; Laflamme G; Albaghjati A; Hickson GRX; Kwok BH; Galkin VE
[Ad] Endereço:Sainte-Justine Hospital Research Center, 3175 Chemin de la Côte Ste-Catherine, Montréal, Québec H3T 1C5, Canada.
[Ti] Título:Multimodal and Polymorphic Interactions between Anillin and Actin: Their Implications for Cytokinesis.
[So] Source:J Mol Biol;429(5):715-731, 2017 Mar 10.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cytokinesis of animal cells requires the assembly of a contractile ring, which promotes daughter cell splitting. Anillin is a conserved scaffold protein involved in organizing the structural components of the contractile ring including filamentous actin (F-actin), myosin, and septins and in forming the subsequent midbody ring. Like other metazoan homologs, Drosophila anillin contains a conserved domain that can bind and bundle F-actin, but the importance and molecular details of its interaction with F-actin remain unclear. Here, we show that in a depletion-and-rescue assay in Drosophila S2 cells, anillin lacking the entire actin-binding domain (ActBD) exhibits defective cortical localization during mitosis and a greatly diminished ability to support cytokinesis. Using in vitro binding assays and electron microscopy on recombinant fragments, we determine that the anillin ActBD harbors three distinct actin-binding sites (ABS 1-3). We show that each ABS binds to a distinct place on F-actin. Importantly, ABS1 and ABS3 partially overlap on the surface of actin and, therefore, interact with F-actin in a mutually exclusive fashion. Although ABS2 and ABS3 are sufficient for bundling, ABS1 contributes to the overall F-actin bundling activity of anillin and enables anillin to switch between two actin-bundling morphologies and promote the formation of three-dimensional F-actin bundles. Finally, we show that in live S2 cells, ABS2 and ABS3 are each required and together sufficient for the robust cortical localization of the ActBD during cytokinesis. Collectively, our structural, biochemical, and cell biological data suggest that multiple anillin-actin interaction modes promote the faithful progression of cytokinesis.
[Mh] Termos MeSH primário: Actinas/metabolismo
Proteínas Contráteis/metabolismo
Citocinese
Domínios e Motivos de Interação entre Proteínas
[Mh] Termos MeSH secundário: Animais
Drosophila/metabolismo
Processamento de Imagem Assistida por Computador
Mitose
Miosinas
Septinas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Contractile Proteins); 0 (anillin); EC 3.6.1.- (Septins); EC 3.6.4.1 (Myosins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170202
[St] Status:MEDLINE


  8 / 2919 MEDLINE  
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[PMID]:28107513
[Au] Autor:Cepero Malo M; Duchemin AL; Guglielmi L; Patzel E; Sel S; Auffarth GU; Carl M; Poggi L
[Ad] Endereço:Centre for Organismal Studies, Heidelberg University, Heidelberg, Germany.
[Ti] Título:The Zebrafish Anillin-eGFP Reporter Marks Late Dividing Retinal Precursors and Stem Cells Entering Neuronal Lineages.
[So] Source:PLoS One;12(1):e0170356, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Monitoring cycling behaviours of stem and somatic cells in the living animal is a powerful tool to better understand tissue development and homeostasis. The tg(anillin:anillin-eGFP) transgenic line carries the full-length zebrafish F-actin binding protein Anillin fused to eGFP from a bacterial artificial chromosome (BAC) containing Anillin cis-regulatory sequences. Here we report the suitability of the Anillin-eGFP reporter as a direct indicator of cycling cells in the late embryonic and post-embryonic retina. We show that combining the anillin:anillin-eGFP with other transgenes such as ptf1a:dsRed and atoh7:gap-RFP allows obtaining spatial and temporal resolution of the mitotic potentials of specific retinal cell populations. This is exemplified by the analysis of the origin of the previously reported apically and non-apically dividing late committed precursors of the photoreceptor and horizontal cell layers.
[Mh] Termos MeSH primário: Proteínas Contráteis/genética
Genes Reporter
Proteínas de Fluorescência Verde/genética
Neurônios/citologia
Retina/citologia
Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Animais
Divisão Celular
Linhagem da Célula
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Contractile Proteins); 0 (anillin); 0 (enhanced green fluorescent protein); 147336-22-9 (Green Fluorescent Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170811
[Lr] Data última revisão:
170811
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170121
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0170356


  9 / 2919 MEDLINE  
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[PMID]:28065320
[Au] Autor:Kechad A; Hickson GR
[Ad] Endereço:Sainte-Justine Hospital Research Center, Montreal, QC, Canada; Université de Montréal, Montréal, QC, Canada.
[Ti] Título:Imaging cytokinesis of Drosophila S2 cells.
[So] Source:Methods Cell Biol;137:47-72, 2017.
[Is] ISSN:0091-679X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Animal cell cytokinesis proceeds through three successive stages: a contractile ring stage, an intercellular bridge stage, and an abscission stage. Many studies have identified a complex network of key proteins required for successful cytokinesis. While each component interacts with, and depends on, several other components, our understanding of how these proteins cooperate in space and time to ensure faithful progression through the stages of cytokinesis remains incomplete. A full understanding of the complexity of the process and its underlying machinery necessitates experimental systems that allow both genetic manipulation and real-time visualization of the various components throughout the successive stages of cytokinesis. Cultured Drosophila S2 cells provide such a system. They are genetically tractable thanks to their exquisite sensitivity to RNA interference mediated by double-stranded RNAs, which can be generated with ease in the laboratory. Furthermore, S2 cells grow well under normal atmospheric conditions, and stable lines expressing fluorescently tagged proteins can be readily generated, making them ideal for long-term live-cell fluorescence microscopy. Here we describe methodology for exploiting S2 cells for the study of cytokinesis, with an emphasis on live-cell imaging. We describe a variety of fluorescent markers available and their utility for highlighting different structures at different stages of cytokinesis. We describe our experimental setup that forms the basis for live-cell analysis of loss-of-function RNAi experiments, rescue experiments, and structure-function analyses of key regulators of cytokinesis. Finally, we describe the types of phenotypes that one can observe at the different stages of Drosophila S2 cell cytokinesis.
[Mh] Termos MeSH primário: Rastreamento de Células/métodos
Citocinese/genética
Biologia Molecular/métodos
Imagem Molecular/métodos
[Mh] Termos MeSH secundário: Animais
Proteínas Contráteis/genética
Drosophila melanogaster/citologia
Drosophila melanogaster/genética
Interferência de RNA
RNA de Cadeia Dupla/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Contractile Proteins); 0 (RNA, Double-Stranded)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170110
[St] Status:MEDLINE


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[PMID]:28065318
[Au] Autor:Mabuchi I; Kashiwazaki J; Mishra M
[Ad] Endereço:Gakushuin University, Tokyo, Japan.
[Ti] Título:In vitro reactivation of the cytokinetic contractile ring of fission yeast cells.
[So] Source:Methods Cell Biol;137:387-394, 2017.
[Is] ISSN:0091-679X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cytokinesis is a process by which a mother cell is divided into two daughter cells after chromosome segregation. In both animal and fungal cells, cytokinesis is carried out by the constriction of the contractile ring made up of actin, myosin-II, and other conserved proteins. Detailed genetic and cell biological analysis of cytokinesis has led to the identification of various genes involved in the process of cytokinesis including the cytological description of the process. However, detailed biochemical analysis of the process is lacking. Critical questions that aim to understand aspects, such as the organization of actin and myosin in the contractile ring, the architecture of the ring, and the molecular process of ring contraction, remain unanswered. We have developed a method to address these aspects of cytokinesis. Using the fission yeast Schizosaccharomyces pombe, we present a method whereby cell-ghosts containing functional contractile rings can be isolated and used to perform various biochemical analysis as well as detailed electron microscopy studies.
[Mh] Termos MeSH primário: Proteínas Contráteis/isolamento & purificação
Citocinese/genética
Biologia Molecular/métodos
Miosina Tipo II/isolamento & purificação
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/química
Actinas/química
Actinas/isolamento & purificação
Divisão Celular/genética
Proteínas Contráteis/química
Miosina Tipo II/química
Miosina Tipo II/genética
Schizosaccharomyces/química
Schizosaccharomyces/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Contractile Proteins); EC 3.6.1.- (Myosin Type II)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170818
[Lr] Data última revisão:
170818
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170110
[St] Status:MEDLINE



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