Base de dados : MEDLINE
Pesquisa : B05.620 [Categoria DeCS]
Referências encontradas : 2260 [refinar]
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[PMID]:28459387
[Au] Autor:Jenkins RG; Moore BB; Chambers RC; Eickelberg O; Königshoff M; Kolb M; Laurent GJ; Nanthakumar CB; Olman MA; Pardo A; Selman M; Sheppard D; Sime PJ; Tager AM; Tatler AL; Thannickal VJ; White ES; ATS Assembly on Respiratory Cell and Molecular Biology
[Ti] Título:An Official American Thoracic Society Workshop Report: Use of Animal Models for the Preclinical Assessment of Potential Therapies for Pulmonary Fibrosis.
[So] Source:Am J Respir Cell Mol Biol;56(5):667-679, 2017 05.
[Is] ISSN:1535-4989
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Numerous compounds have shown efficacy in limiting development of pulmonary fibrosis using animal models, yet few of these compounds have replicated these beneficial effects in clinical trials. Given the challenges associated with performing clinical trials in patients with idiopathic pulmonary fibrosis (IPF), it is imperative that preclinical data packages be robust in their analyses and interpretations to have the best chance of selecting promising drug candidates to advance to clinical trials. The American Thoracic Society has convened a group of experts in lung fibrosis to discuss and formalize recommendations for preclinical assessment of antifibrotic compounds. The panel considered three major themes (choice of animal, practical considerations of fibrosis modeling, and fibrotic endpoints for evaluation). Recognizing the need for practical considerations, we have taken a pragmatic approach. The consensus view is that use of the murine intratracheal bleomycin model in animals of both genders, using hydroxyproline measurements for collagen accumulation along with histologic assessments, is the best-characterized animal model available for preclinical testing. Testing of antifibrotic compounds in this model is recommended to occur after the acute inflammatory phase has subsided (generally after Day 7). Robust analyses may also include confirmatory studies in human IPF specimens and validation of results in a second system using in vivo or in vitro approaches. The panel also strongly encourages the publication of negative results to inform the lung fibrosis community. These recommendations are for preclinical therapeutic evaluation only and are not intended to dissuade development of emerging technologies to better understand IPF pathogenesis.
[Mh] Termos MeSH primário: Congressos como Assunto
Modelos Animais de Doenças
Fibrose Pulmonar/terapia
Sociedades Médicas
[Mh] Termos MeSH secundário: Animais
Determinação de Ponto Final
Feminino
Seres Humanos
Masculino
Organismos Geneticamente Modificados
Reprodutibilidade dos Testes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1707
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE
[do] DOI:10.1165/rcmb.2017-0096ST


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[PMID]:29364605
[Au] Autor:Skladnev DA; Mulyukin AL; Filippoval SN; Kulikov EE; Letaroval MA; Yuzbasheva EA; Karnysheva EA; Brushkov AV; Gal'chenko VF
[Ti] Título:[Modeling the Propagation of Microbial Cells and Phage Particles from the Sites of Permafrost Thawing.]
[So] Source:Mikrobiologiia;85(5):580-587, 2016 Sep.
[Is] ISSN:0026-3656
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:A method is proposed for integral assessment of the propagation of microbial cells and viral parti- cles during seasonal thawing of relic ice wedge layers. The results of on-site and laboratory investigation car- ried out in the upper part of permafrost exposure at Mamontova Gora (Yakutiya, Russia) are presented. To increase reliability of the results, suspensions of two microbial species and two coliphage species were intro- duced as biomarkers directly on the surface of thaing ice and in the meltwater flow. Each of the four different model biological objects was shown to possess unique parameters of movement in the meltwater flow and is able to move 132 m in 25-35 min with the water flow.
[Mh] Termos MeSH primário: Colífagos/fisiologia
Corynebacterium/fisiologia
Movimento/fisiologia
Pergelissolo/microbiologia
Rios/microbiologia
Yarrowia/fisiologia
[Mh] Termos MeSH secundário: Gelo/análise
Modelos Biológicos
Organismos Geneticamente Modificados
Transição de Fase
Reologia/métodos
Estações do Ano
Sibéria
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ice)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180125
[St] Status:MEDLINE


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[PMID]:29236423
[Au] Autor:Kromka NJ
[Ti] Título:GMOs, genetically modified organisms or genuinely mixed opinions? A reasonable Consumer's understanding of the terms "GMO" and "non-GMO," and the struggle to set a Standard. 
[So] Source:Seton Hall Law Rev;48(1):221-48, 2017.
[Is] ISSN:0586-5964
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Comportamento do Consumidor
Rotulagem de Alimentos/legislação & jurisprudência
Alimentos Geneticamente Modificados
Rotulagem de Produtos/legislação & jurisprudência
United States Department of Agriculture/legislação & jurisprudência
United States Food and Drug Administration/legislação & jurisprudência
[Mh] Termos MeSH secundário: Ração Animal
Animais
Rotulagem de Alimentos/normas
Regulamentação Governamental
Conhecimentos, Atitudes e Prática em Saúde
Seres Humanos
Organismos Geneticamente Modificados
Plantas Geneticamente Modificadas
Rotulagem de Produtos/normas
Restaurantes/legislação & jurisprudência
Estados Unidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:T
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE


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[PMID]:29048592
[Au] Autor:McQuaid ME; Pinder JB; Arumuggam N; Lacoste JSC; Chew JSK; Dobson MJ
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Dalhousie University, Halifax, Nova Scotia B3H 4R2, Canada.
[Ti] Título:The yeast 2-µm plasmid Raf protein contributes to plasmid inheritance by stabilizing the Rep1 and Rep2 partitioning proteins.
[So] Source:Nucleic Acids Res;45(18):10518-10533, 2017 Oct 13.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The yeast 2-µm plasmid is a remarkable genetic parasite, managing efficient maintenance at high-copy number with minimal impact on the host. Equal partitioning of the plasmid upon host cell division requires plasmid proteins Rep1 and Rep2 and the plasmid STB locus. The Rep proteins and the plasmid-encoded Raf protein also regulate plasmid gene transcription. In this study, protein interaction assays, sequence analyses and mutational approaches were used to identify domains and residues in Rep2 and Raf required for association with Rep1 and Rep2 and to delineate the Rep2 DNA-binding domain. Rep2 and Raf displayed similarities in interactions with Rep1 and Rep2, in having Rep1 promote their STB association in vivo, and in stabilizing Rep protein levels. Rep2 mutants impaired for self-association were competent for transcriptional repression while those deficient for Rep1 association were not. Surprisingly, Rep2 mutants impaired for either Rep1 interaction or self-association were able to maintain efficient plasmid inheritance provided Raf was present and competent for Rep protein interaction. Our findings provide insight into the Rep protein complexes required for partitioning and transcriptional repression, and suggest that in addition to its transcriptional function, Raf stabilization of Rep partitioning proteins contributes to the remarkable persistence of the 2-µm plasmid.
[Mh] Termos MeSH primário: Plasmídeos/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/genética
Transativadores/metabolismo
Quinases raf/metabolismo
Quinases raf/fisiologia
[Mh] Termos MeSH secundário: Divisão Celular
Padrões de Herança
Organismos Geneticamente Modificados
Ligação Proteica
Estabilidade Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (REP1 protein, S cerevisiae); 0 (REP2 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Trans-Activators); EC 2.7.11.1 (raf Kinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171020
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx703


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[PMID]:28985361
[Au] Autor:Bonaldi K; Li Z; Kang SE; Breton G; Pruneda-Paz JL
[Ad] Endereço:Division of Biological Sciences, University of California San Diego, La Jolla, CA 92093, USA.
[Ti] Título:Novel cell surface luciferase reporter for high-throughput yeast one-hybrid screens.
[So] Source:Nucleic Acids Res;45(18):e157, 2017 Oct 13.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Gene-centered yeast one-hybrid (Y1H) screens provide a powerful and effective strategy to identify transcription factor (TF)-promoter interactions. While genome-wide TF ORFeome clone collections are increasingly available, screening protocols have limitations inherent to the properties of the enzymatic reaction used to identify interactions and to the procedure required to perform the assay in a high-throughput format. Here, we present the development and validation of a streamlined strategy for quantitative and fully automated gene-centered Y1H screens using a novel cell surface Gaussia luciferase reporter.
[Mh] Termos MeSH primário: Genes Reporter
Ensaios de Triagem em Larga Escala/métodos
Luciferases/genética
Técnicas do Sistema de Duplo-Híbrido
[Mh] Termos MeSH secundário: Automação Laboratorial
Sítios de Ligação/genética
Regulação da Expressão Gênica/genética
Técnicas de Transferência de Genes
Organismos Geneticamente Modificados
Regiões Promotoras Genéticas
Ligação Proteica
Elementos Reguladores de Transcrição/genética
Saccharomyces cerevisiae
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
0 (Transcription Factors); EC 1.13.12.- (Luciferases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171007
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx682


  6 / 2260 MEDLINE  
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[PMID]:28981863
[Au] Autor:Tashiro S; Nishihara Y; Kugou K; Ohta K; Kanoh J
[Ad] Endereço:Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.
[Ti] Título:Subtelomeres constitute a safeguard for gene expression and chromosome homeostasis.
[So] Source:Nucleic Acids Res;45(18):10333-10349, 2017 Oct 13.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The subtelomere, a telomere-adjacent chromosomal domain, contains species-specific homologous DNA sequences, in addition to various genes. However, the functions of subtelomeres, particularly subtelomeric homologous (SH) sequences, remain elusive. Here, we report the first comprehensive analyses of the cellular functions of SH sequences in the fission yeast, Schizosaccharomyces pombe. Complete removal of SH sequences from the genome revealed that they are dispensable for mitosis, meiosis and telomere length control. However, when telomeres are lost, SH sequences prevent deleterious inter-chromosomal end fusion by facilitating intra-chromosomal circularization. Surprisingly, SH-deleted cells sometimes survive telomere loss through inter-chromosomal end fusions via homologous loci such as LTRs, accompanied by centromere inactivation of either chromosome. Moreover, SH sequences function as a buffer region against the spreading of subtelomeric heterochromatin into the neighboring gene-rich regions. Furthermore, we found a nucleosome-free region at the subtelomeric border, which may be a second barrier that blocks heterochromatin spreading into the subtelomere-adjacent euchromatin. Thus, our results demonstrate multiple defense functions of subtelomeres in chromosome homeostasis and gene expression.
[Mh] Termos MeSH primário: Cromossomos Fúngicos/fisiologia
Expressão Gênica
Homeostase/genética
Proteínas de Schizosaccharomyces pombe/genética
Schizosaccharomyces/genética
Telômero/fisiologia
[Mh] Termos MeSH secundário: Centrômero/metabolismo
Instabilidade Cromossômica/genética
Regulação Fúngica da Expressão Gênica
Heterocromatina/metabolismo
Organismos Geneticamente Modificados
Deleção de Sequência
Proteínas de Ligação a Telômeros/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Heterochromatin); 0 (Schizosaccharomyces pombe Proteins); 0 (Telomere-Binding Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171006
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx780


  7 / 2260 MEDLINE  
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[PMID]:28902865
[Au] Autor:Boldinova EO; Stojkovic G; Khairullin R; Wanrooij S; Makarova AV
[Ad] Endereço:Institute of Molecular Genetics of Russian Academy of Sciences, Kurchatov sq. 2, Moscow, Russia.
[Ti] Título:Optimization of the expression, purification and polymerase activity reaction conditions of recombinant human PrimPol.
[So] Source:PLoS One;12(9):e0184489, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human PrimPol is a DNA primase/polymerase involved in DNA damage tolerance and prevents nuclear genome instability. PrimPol is also localized to the mitochondria, but its precise function in mitochondrial DNA maintenance has remained elusive. PrimPol works both as a translesion (TLS) polymerase and as the primase that restarts DNA replication after a lesion. However, the observed biochemical activities of PrimPol vary considerably between studies as a result of different reaction conditions used. To reveal the effects of reaction composition on PrimPol DNA polymerase activity, we tested the polymerase activity in the presence of various buffer agents, salt concentrations, pH values and metal cofactors. Additionally, the enzyme stability was analyzed under various conditions. We demonstrate that the reaction buffer with pH 6-6.5, low salt concentrations and 3 mM Mg2+ or 0.3-3 mM Mn2+ cofactor ions supports the highest DNA polymerase activity of human PrimPol in vitro. The DNA polymerase activity of PrimPol was found to be stable after multiple freeze-thaw cycles and prolonged protein incubation on ice. However, rapid heat-inactivation of the enzyme was observed at 37ºC. We also for the first time describe the purification of human PrimPol from a human cell line and compare the benefits of this approach to the expression in Escherichia coli and in Saccharomyces cerevisiae cells. Our results show that active PrimPol can be purified from E. coli and human suspension cell line in high quantities and that the activity of the purified enzyme is similar in both expression systems. Conversely, the yield of full-length protein expressed in S. cerevisiae was considerably lower and this system is therefore not recommended for expression of full-length recombinant human PrimPol.
[Mh] Termos MeSH primário: DNA Primase/genética
DNA Primase/isolamento & purificação
DNA Polimerase Dirigida por DNA/genética
DNA Polimerase Dirigida por DNA/isolamento & purificação
Enzimas Multifuncionais/genética
Enzimas Multifuncionais/isolamento & purificação
Reação em Cadeia da Polimerase/normas
[Mh] Termos MeSH secundário: Calibragem
Células Cultivadas
DNA Primase/metabolismo
DNA Polimerase Dirigida por DNA/metabolismo
Escherichia coli/química
Escherichia coli/genética
Escherichia coli/metabolismo
Regulação Bacteriana da Expressão Gênica
Células HEK293
Seres Humanos
Engenharia Metabólica/normas
Enzimas Multifuncionais/metabolismo
Organismos Geneticamente Modificados
Reação em Cadeia da Polimerase/métodos
Estabilidade Proteica
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Multifunctional Enzymes); 0 (Recombinant Proteins); EC 2.7.7.- (DNA Primase); EC 2.7.7.- (PrimPol protein, human); EC 2.7.7.7 (DNA-Directed DNA Polymerase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170914
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184489


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[PMID]:28902855
[Au] Autor:Claassens NJ; Siliakus MF; Spaans SK; Creutzburg SCA; Nijsse B; Schaap PJ; Quax TEF; van der Oost J
[Ad] Endereço:Laboratory of Microbiology, Wageningen University and Research, Wageningen, The Netherlands.
[Ti] Título:Improving heterologous membrane protein production in Escherichia coli by combining transcriptional tuning and codon usage algorithms.
[So] Source:PLoS One;12(9):e0184355, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:High-level, recombinant production of membrane-integrated proteins in Escherichia coli is extremely relevant for many purposes, but has also been proven challenging. Here we study a combination of transcriptional fine-tuning in E. coli LEMO21(DE3) with different codon usage algorithms for heterologous production of membrane proteins. The overexpression of 6 different membrane proteins is compared for the wild-type gene codon usage variant, a commercially codon-optimized variant, and a codon-harmonized variant. We show that transcriptional fine-tuning plays a major role in improving the production of all tested proteins. Moreover, different codon usage variants significantly improved production of some of the tested proteins. However, not a single algorithm performed consistently best for the membrane-integrated production of the 6 tested proteins. In conclusion, for improving heterologous membrane protein production in E. coli, the major effect is accomplished by transcriptional tuning. In addition, further improvements may be realized by attempting different codon usage variants, such as codon harmonized variants, which can now be easily generated through our online Codon Harmonizer tool.
[Mh] Termos MeSH primário: Algoritmos
Códon/genética
Escherichia coli
Regulação Bacteriana da Expressão Gênica
Proteínas de Membrana/biossíntese
Software
[Mh] Termos MeSH secundário: Escherichia coli/genética
Escherichia coli/metabolismo
Código Genético
Proteínas de Membrana/genética
Engenharia Metabólica/métodos
Organismos Geneticamente Modificados
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/genética
Transcrição Genética/genética
Transformação Bacteriana/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon); 0 (Membrane Proteins); 0 (Recombinant Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170914
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184355


  9 / 2260 MEDLINE  
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[PMID]:28900030
[Au] Autor:Xu Y; Chen G; Greer MS; Caldo KMP; Ramakrishnan G; Shah S; Wu L; Lemieux MJ; Ozga J; Weselake RJ
[Ad] Endereço:From the Department of Agricultural, Food, and Nutritional Science, University of Alberta, Edmonton, Alberta T6G 2P5.
[Ti] Título:Multiple mechanisms contribute to increased neutral lipid accumulation in yeast producing recombinant variants of plant diacylglycerol acyltransferase 1.
[So] Source:J Biol Chem;292(43):17819-17831, 2017 Oct 27.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The apparent bottleneck in the accumulation of oil during seed development in some oleaginous plant species is the formation of triacylglycerol (TAG) by the acyl-CoA-dependent acylation of -1,2-diacylglycerol catalyzed by diacylglycerol acyltransferase (DGAT, EC 2.3.1.20). Improving DGAT activity using protein engineering could lead to improvements in seed oil yield ( in canola-type ). Directed evolution of DGAT1 (BnaDGAT1) previously revealed that one of the regions where amino acid residue substitutions lead to higher performance in BnaDGAT1 is in the ninth predicted transmembrane domain (PTMD9). In this study, several BnaDGAT1 variants with amino acid residue substitutions in PTMD9 were characterized. Among these enzyme variants, the extent of yeast TAG production was affected by different mechanisms, including increased enzyme activity, increased polypeptide accumulation, and possibly reduced substrate inhibition. The kinetic properties of the BnaDGAT1 variants were affected by the amino acid residue substitutions, and a new kinetic model based on substrate inhibition and sigmoidicity was generated. Based on sequence alignment and further biochemical analysis, the amino acid residue substitutions that conferred increased TAG accumulation were shown to be present in the DGAT1-PTMD9 region of other higher plant species. When amino acid residue substitutions that increased BnaDGAT1 enzyme activity were introduced into recombinant DGAT1, they also improved enzyme performance. Thus, the knowledge generated from directed evolution of DGAT1 in one plant species can be transferred to other plant species and has potentially broad applications in genetic engineering of oleaginous crops and microorganisms.
[Mh] Termos MeSH primário: Brassica napus/genética
Diacilglicerol O-Aciltransferase
Metabolismo dos Lipídeos
Proteínas de Plantas
Saccharomyces cerevisiae/enzimologia
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Brassica napus/enzimologia
Diacilglicerol O-Aciltransferase/biossíntese
Diacilglicerol O-Aciltransferase/genética
Mutação de Sentido Incorreto
Organismos Geneticamente Modificados/genética
Organismos Geneticamente Modificados/metabolismo
Proteínas de Plantas/biossíntese
Proteínas de Plantas/genética
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/genética
Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Proteins); 0 (Recombinant Proteins); EC 2.3.1.20 (Diacylglycerol O-Acyltransferase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170914
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.811489


  10 / 2260 MEDLINE  
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[PMID]:28798144
[Au] Autor:Hurrell BP; Beaumann M; Heyde S; Regli IB; Müller AJ; Tacchini-Cottier F
[Ad] Endereço:Department of Biochemistry, World Health Organization-Immunology Research and Training Collaborative Center, University of Lausanne, Epalinges, Switzerland; and.
[Ti] Título:Frontline Science: amastigotes can replicate within neutrophils.
[So] Source:J Leukoc Biol;102(5):1187-1198, 2017 Nov.
[Is] ISSN:1938-3673
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cutaneous leishmaniasis is a neglected tropical disease, causing a spectrum of clinical manifestations varying from self-healing to unhealing lesions that may be very difficult to treat. Emerging evidence points to a detrimental role for neutrophils during the first hours following infection with many distinct species (spp.) at a time when the parasite is in its nonreplicative promastigote form. Neutrophils have also been detected at later stages of infection in unhealing chronic cutaneous lesions. However, the interactions between these cells and the replicative intracellular amastigote form of the parasite have been poorly studied. Here, we show that amastigotes are efficiently internalized by neutrophils and that this process has only a low impact on neutrophil activation and apoptosis. In neutrophils, the amastigotes were found in acidified vesicles. Furthermore, within cutaneous unhealing lesions, heavily infected neutrophils were found with up to 6 parasites per cell. To investigate if the amastigotes could replicate within neutrophils, we generated photoconvertible fluorescent parasites. With the use of flow cytometry imaging and time-lapse microscopy, we could demonstrate that a subset of parasites replicated within neutrophils. Overall, our data reveal a novel role for neutrophils that can act as a niche for parasite replication during the chronic phase of infection, thereby contributing to disease pathology.
[Mh] Termos MeSH primário: Divisão Celular
Leishmania mexicana/crescimento & desenvolvimento
Leishmaniose Cutânea/parasitologia
Estágios do Ciclo de Vida/genética
Neutrófilos/parasitologia
Organismos Geneticamente Modificados/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: Animais
Feminino
Citometria de Fluxo
Corantes Fluorescentes/metabolismo
Genes Reporter
Interações Hospedeiro-Parasita/imunologia
Leishmania mexicana/patogenicidade
Leishmania mexicana/ultraestrutura
Leishmaniose Cutânea/patologia
Camundongos
Camundongos Endogâmicos C57BL
Neutrófilos/ultraestrutura
Fagocitose
Processos Fotoquímicos
Imagem com Lapso de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fluorescent Dyes)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170812
[St] Status:MEDLINE
[do] DOI:10.1189/jlb.4HI0417-158R



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