Base de dados : MEDLINE
Pesquisa : E05.393.220.250 [Categoria DeCS]
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  1 / 1971 MEDLINE  
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[PMID]:28461449
[Au] Autor:Stubbendieck RM; Straight PD
[Ad] Endereço:Interdisciplinary Program in Genetics, Texas A&M University, College Station, Texas, USA.
[Ti] Título:Linearmycins Activate a Two-Component Signaling System Involved in Bacterial Competition and Biofilm Morphology.
[So] Source:J Bacteriol;199(18), 2017 09 15.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bacteria use two-component signaling systems to adapt and respond to their competitors and changing environments. For instance, competitor bacteria may produce antibiotics and other bioactive metabolites and sequester nutrients. To survive, some species of bacteria escape competition through antibiotic production, biofilm formation, or motility. Specialized metabolite production and biofilm formation are relatively well understood for bacterial species in isolation. How bacteria control these functions when competitors are present is not well studied. To address fundamental questions relating to the competitive mechanisms of different species, we have developed a model system using two species of soil bacteria, and sp. strain Mg1. Using this model, we previously found that linearmycins produced by sp. strain Mg1 cause lysis of cells and degradation of colony matrix. We identified strains of with mutations in the two-component signaling system operon that confer dual phenotypes of specific linearmycin resistance and biofilm morphology. We determined that expression of the ATP-binding cassette (ABC) transporter operon, particularly and , is necessary for biofilm morphology. Using transposon mutagenesis, we identified genes that are required for YfiLMN-mediated biofilm morphology, including several chaperones. Using transcriptional fusions, we found that YfiJ signaling is activated by linearmycins and other polyene metabolites. Finally, using a truncated YfiJ, we show that YfiJ requires its transmembrane domain to activate downstream signaling. Taken together, these results suggest coordinated dual antibiotic resistance and biofilm morphology by a single multifunctional ABC transporter promotes competitive fitness of DNA sequencing approaches have revealed hitherto unexplored diversity of bacterial species in a wide variety of environments that includes the gastrointestinal tract of animals and the rhizosphere of plants. Interactions between different species in bacterial communities have impacts on our health and industry. However, many approaches currently used to study whole bacterial communities do not resolve mechanistic details of interspecies interactions, including how bacteria sense and respond to their competitors. Using a competition model, we have uncovered dual functions for a previously uncharacterized two-component signaling system involved in specific antibiotic resistance and biofilm morphology. Insights gleaned from signaling within interspecies interaction models build a more complete understanding of gene functions important for bacterial communities and will enhance community-level analytical approaches.
[Mh] Termos MeSH primário: Antibacterianos/metabolismo
Antibiose
Bacillus subtilis/fisiologia
Biofilmes/crescimento & desenvolvimento
Viabilidade Microbiana
Streptomyces/fisiologia
[Mh] Termos MeSH secundário: Transportadores de Cassetes de Ligação de ATP/metabolismo
Fusão Gênica Artificial
Bacillus subtilis/efeitos dos fármacos
Elementos de DNA Transponíveis
Perfilação da Expressão Gênica
Regulação Bacteriana da Expressão Gênica
Mutagênese Insercional
Mutação
Transdução de Sinais
Streptomyces/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (ATP-Binding Cassette Transporters); 0 (Anti-Bacterial Agents); 0 (DNA Transposable Elements)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


  2 / 1971 MEDLINE  
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[PMID]:28486766
[Au] Autor:Ibryashkina EM; Solonin AS; Zakharova MV
[Ad] Endereço:FSBIS G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.
[Ti] Título:Protein NCRII-18: the role of gene fusion in the molecular evolution of restriction endonucleases.
[So] Source:FEBS Lett;591(12):1702-1711, 2017 Jun.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:This work first constructed the fusion protein NCRII-18 by fusing the restriction endonuclease Ecl18kI gene and part of the gene coding for the N-terminal domain of the endonuclease EcoRII. The fusion of the EcoRII N-terminal domain leads to a change in the properties of the recombinant protein. Unlike Ecl18kI, which made the basis of NCRII-18, the fusion protein predominantly recognizes the CCWGG sites, having lost the capability of interacting with the CCSGG sites. Experimental data support the hypothesis of a close evolutionary relationship between type IIE and IIP restriction endonucleases via a recombination between domains with active site structure and elements for recognition with domains responsible for recognition of DNA sequences.
[Mh] Termos MeSH primário: Desoxirribonucleases de Sítio Específico do Tipo II/genética
Proteínas de Escherichia coli/genética
Escherichia coli/enzimologia
Evolução Molecular
Fusão Gênica
Modelos Genéticos
[Mh] Termos MeSH secundário: Fusão Gênica Artificial
Sítios de Ligação
Domínio Catalítico
Enzimas de Restrição do DNA/química
Enzimas de Restrição do DNA/genética
Enzimas de Restrição do DNA/metabolismo
DNA Bacteriano/química
DNA Bacteriano/metabolismo
Desoxirribonucleases de Sítio Específico do Tipo II/química
Desoxirribonucleases de Sítio Específico do Tipo II/metabolismo
Ensaio de Desvio de Mobilidade Eletroforética
Escherichia coli/genética
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/metabolismo
Motivos de Nucleotídeos
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Conformação Proteica
Engenharia de Proteínas
Proteínas Recombinantes de Fusão/metabolismo
Recombinação Genética
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Escherichia coli Proteins); 0 (Peptide Fragments); 0 (Recombinant Fusion Proteins); EC 3.1.21.- (DNA Restriction Enzymes); EC 3.1.21.- (endodeoxyribonuclease Ecl18kI); EC 3.1.21.4 (CCWGG-specific type II deoxyribonucleases); EC 3.1.21.4 (Deoxyribonucleases, Type II Site-Specific)
[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:170510
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12669


  3 / 1971 MEDLINE  
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[PMID]:28193277
[Au] Autor:Meng P; Dong QC; Tan GG; Wen WH; Wang H; Zhang G; Wang YZ; Jing YM; Wang C; Qin WJ; Yuan JL
[Ad] Endereço:Department of Urology, Xijing Hospital, Fourth Military Medical University, Xi'an, Shaanxi, China.
[Ti] Título:Anti-tumor effects of a recombinant anti-prostate specific membrane antigen immunotoxin against prostate cancer cells.
[So] Source:BMC Urol;17(1):14, 2017 Feb 13.
[Is] ISSN:1471-2490
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: To evaluate anti-prostate cancer effects of a chimeric tumor-targeted killer protein. METHODS: We established a novel fusion gene, immunocasp-3, composed of NH2-terminal leader sequence fused with an anti-prostate-specific membrane antigen (PSMA) antibody (J591), the furin cleavage sequences of diphtheria toxin (Fdt), and the reverse coding sequences of the large and small subunits of caspase-3 (revcaspase-3). The expressing level of the immunocasp-3 gene was evaluated by using the reverse transcription-PCR (RT-PCR) and western blot analysis. Cell viability assay and cytotoxicity assay were used to evaluate its anti-tumor effects in vitro. Apoptosis was confirmed by electron microscopy and Annexin V-FITC staining. The antitumor effects of immunocasp-3 were assessed in nude mice xenograft models containing PSMA-overexpressing LNCaP cells. RESULTS: This study shows that the immunocasp-3 proteins selectively recognized and induced apoptotic death in PSMA-overexpressing LNCaP cells in vitro, where apoptotic cells were present in 15.3% of the cells transfected with the immunocasp-3 expression vector at 48 h after the transfection, in contrast to 5.5% in the control cells. Moreover, LNCaP cells were significantly killed under the condition of the co-culture of the immunocasp-3-secreting Jurkat cells and more than 50% of the LNCaP cells died when the two cell lines were co-cultured within 5 days. In addition, The expression of immunocasp-3 also significantly suppressed tumor growth and greatly prolonged the animal survival rate in vivo. CONCLUSION: A novel fusion gene, immunocasp-3, may represent a viable approach to treating PSMA-positive prostate cancer.
[Mh] Termos MeSH primário: Adenocarcinoma/terapia
Antígenos de Superfície
Terapia Genética
Glutamato Carboxipeptidase II
Neoplasias da Próstata/terapia
[Mh] Termos MeSH secundário: Adenocarcinoma/patologia
Animais
Antígenos de Superfície/genética
Fusão Gênica Artificial
Caspase 3/genética
Terapia Genética/métodos
Glutamato Carboxipeptidase II/genética
Seres Humanos
Imunotoxinas/genética
Masculino
Camundongos Nus
Neoplasias da Próstata/patologia
Células Tumorais Cultivadas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Surface); 0 (Immunotoxins); EC 3.4.17.21 (Glutamate Carboxypeptidase II); EC 3.4.17.21 (glutamate carboxypeptidase II, human); EC 3.4.22.- (Caspase 3)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170302
[Lr] Data última revisão:
170302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170215
[St] Status:MEDLINE
[do] DOI:10.1186/s12894-017-0203-9


  4 / 1971 MEDLINE  
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[PMID]:28188619
[Au] Autor:Spraggon L; Martelotto LG; Hmeljak J; Hitchman TD; Wang J; Wang L; Slotkin EK; Fan PD; Reis-Filho JS; Ladanyi M
[Ad] Endereço:Department of Pathology, Memorial Sloan Kettering Cancer Center, New York, NY, USA.
[Ti] Título:Generation of conditional oncogenic chromosomal translocations using CRISPR-Cas9 genomic editing and homology-directed repair.
[So] Source:J Pathol;242(1):102-112, 2017 May.
[Is] ISSN:1096-9896
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Chromosomal rearrangements encoding oncogenic fusion proteins are found in a wide variety of malignancies. The use of programmable nucleases to generate specific double-strand breaks in endogenous loci, followed by non-homologous end joining DNA repair, has allowed several of these translocations to be generated as constitutively expressed fusion genes within a cell population. Here, we describe a novel approach that combines CRISPR-Cas9 technology with homology-directed repair to engineer, capture, and modulate the expression of chromosomal translocation products in a human cell line. We have applied this approach to the genetic modelling of t(11;22)(q24;q12) and t(11;22)(p13;q12), translocation products of the EWSR1 gene and its 3' fusion partners FLI1 and WT1, present in Ewing's sarcoma and desmoplastic small round cell tumour, respectively. Our innovative approach allows for temporal control of the expression of engineered endogenous chromosomal rearrangements, and provides a means to generate models to study tumours driven by fusion genes. Copyright © 2017 Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd.
[Mh] Termos MeSH primário: Repetições Palindrômicas Curtas Agrupadas e Regularmente Espaçadas/genética
Tumor Desmoplásico de Pequenas Células Redondas/genética
Reparo de DNA por Recombinação/genética
Sarcoma de Ewing/genética
Translocação Genética
[Mh] Termos MeSH secundário: Fusão Gênica Artificial/métodos
Cromossomos Humanos Par 11/genética
Cromossomos Humanos Par 22/genética
DNA de Neoplasias/genética
Regulação Neoplásica da Expressão Gênica/genética
Seres Humanos
Proteínas de Fusão Oncogênicas/genética
Células Tumorais Cultivadas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Neoplasm); 0 (Oncogene Proteins, Fusion)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170212
[St] Status:MEDLINE
[do] DOI:10.1002/path.4883


  5 / 1971 MEDLINE  
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[PMID]:27734122
[Au] Autor:Hoshida H; Kondo M; Kobayashi T; Yarimizu T; Akada R
[Ad] Endereço:Department of Applied Chemistry, Graduate School of Sciences and Technology for Innovation, Yamaguchi University, Tokiwadai 2-16-1, Ube, 755-8611, Japan. hoshida@yamaguchi-u.ac.jp.
[Ti] Título:5´-UTR introns enhance protein expression in the yeast Saccharomyces cerevisiae.
[So] Source:Appl Microbiol Biotechnol;101(1):241-251, 2017 Jan.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Saccharomyces cerevisiae is one of the most suitable microorganisms for recombinant protein production. To enhance protein production, various expression systems have been intensively studied. However, the effect of introns on protein expression has not been examined deeply in S. cerevisiae. In this study, we analyzed the effect of some introns on protein expression. RPS25A, RPS26A, and RPS26B contain single introns within the 5´-untranslated regions (5´-UTRs), and RPS24A has an intron just downstream of the initiation codon. Expression activity of the promoter regions containing introns (intron promoters) were analyzed by luciferase reporter assays. These intron promoters showed higher expression than the TDH3 promoter (TDH3p), which is one of the strongest promoters in S. cerevisiae. Deletion of the introns from these promoters decreased luciferase expression, indicating that introns have a role in enhancing protein expression. To develop artificial strong intron promoters, several chimeric promoters were constructed using the TDH3p and the RPS25A intron promoter. A construct containing the entire TDH3p followed by the RPS25A intron showed about 50-fold higher expression than the TDH3p alone. Inducible expressions driven by the GAL10 promoter and the CUP1 promoter were also enhanced by the RPS25A intron. However, enhancement of mRNA accumulation by the TDH3p and the GAL10 promoter with the RPS25A intron was lower than the effect on luciferase activity, suggesting that the intron affects post-transcriptionally. The chimeric promoter, TDH3p-RPS25A-intron, enhanced expressions of some, but not all proteins examined, indicating that 5'-UTR introns increase production of a certain type of recombinant proteins in S. cerevisiae.
[Mh] Termos MeSH primário: Regiões 5´ não Traduzidas
Regulação Fúngica da Expressão Gênica
Íntrons
RNA Mensageiro/genética
Proteínas de Saccharomyces cerevisiae/biossíntese
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Fusão Gênica Artificial
Perfilação da Expressão Gênica
Genes Reporter
Luciferases/análise
Luciferases/genética
Regiões Promotoras Genéticas
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (5' Untranslated Regions); 0 (RNA, Messenger); 0 (Saccharomyces cerevisiae Proteins); EC 1.13.12.- (Luciferases)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170620
[Lr] Data última revisão:
170620
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161014
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-016-7891-z


  6 / 1971 MEDLINE  
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[PMID]:27503246
[Au] Autor:Molina-Henares MA; Ramos-González MI; Daddaoua A; Fernández-Escamilla AM; Espinosa-Urgel M
[Ad] Endereço:Department of Environmental Protection, Estación Experimental del Zaidín, CSIC, Profesor Albareda, 1, Granada 18008, Spain. Electronic address: nene.molina@eez.csic.es.
[Ti] Título:FleQ of Pseudomonas putida KT2440 is a multimeric cyclic diguanylate binding protein that differentially regulates expression of biofilm matrix components.
[So] Source:Res Microbiol;168(1):36-45, 2017 Jan.
[Is] ISSN:1769-7123
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:The intracellular signal molecule cyclic di-GMP (c-di-GMP) is an important element in regulation of biofilm formation by bacteria. In Pseudomonas aeruginosa, FleQ functions as a c-di-GMP-dependent transcriptional regulator of expression of flagellar genes and the exopolysaccharide (EPS) Pel, a component of the biofilm extracellular matrix. In the plant-beneficial bacterium Pseudomonas putida KT2440, a mutation in fleQ reduces biofilm formation and colonization of plant surfaces. Using isothermal titration calorimetry and electrophoretic mobility shift assays, we show in this work that FleQ of P. putida interacts with c-di-GMP and directly binds the promoter regions of flagellar and EPS genes. Data obtained by analytical gel filtration and ultracentrifugation indicate that FleQ is in multiple oligomeric states in solution (dimers, tetramers and hexamers), which do not show altered equilibrium in the presence of c-di-GMP. DNA binding is independent of c-diGMP, although it is favored by the second messenger in the case of the promoter of the operon responsible for synthesis of the species-specific EPS Pea. Analysis of expression using transcriptional fusions showed an influence of FleQ upon two of the four EPS operons under regular growth conditions. Finally, a consensus sequence for promoter recognition by FleQ in P. putida is also proposed.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
Proteínas de Bactérias/metabolismo
Biofilmes/crescimento & desenvolvimento
GMP Cíclico/análogos & derivados
Proteínas de Ligação a DNA/metabolismo
Regulação Bacteriana da Expressão Gênica
Pseudomonas putida/fisiologia
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/genética
Fusão Gênica Artificial
Proteínas de Bactérias/genética
Sítios de Ligação
Calorimetria
Cromatografia em Gel
Sequência Consenso
GMP Cíclico/metabolismo
DNA Bacteriano/metabolismo
Proteínas de Ligação a DNA/genética
Ensaio de Desvio de Mobilidade Eletroforética
Flagelos/metabolismo
Perfilação da Expressão Gênica
Polissacarídeos Bacterianos/metabolismo
Regiões Promotoras Genéticas
Ligação Proteica
Multimerização Proteica
Pseudomonas putida/genética
Pseudomonas putida/metabolismo
Ultracentrifugação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (DNA, Bacterial); 0 (DNA-Binding Proteins); 0 (Polysaccharides, Bacterial); 61093-23-0 (bis(3',5')-cyclic diguanylic acid); EC 3.6.1.- (Adenosine Triphosphatases); H2D2X058MU (Cyclic GMP)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170310
[Lr] Data última revisão:
170310
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160810
[St] Status:MEDLINE


  7 / 1971 MEDLINE  
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[PMID]:27835993
[Au] Autor:Silva MG; Knowles DP; Suarez CE
[Ad] Endereço:Department of Veterinary Microbiology and Pathology, Washington State University, Pullman, WA, USA. marta@vetmed.wsu.edu.
[Ti] Título:Identification of interchangeable cross-species function of elongation factor-1 alpha promoters in Babesia bigemina and Babesia bovis.
[So] Source:Parasit Vectors;9(1):576, 2016 Nov 11.
[Is] ISSN:1756-3305
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Tick-borne Babesia bigemina is responsible for acute and potentially lethal hemolytic disease in cattle. The development of genetic manipulation tools necessary to the better understanding of parasite biology is currently limited by the lack of a complete parasite genome and experimental tools such as transfection. Effective promoters, required to regulate expression of transgenes, such as the elongation factor-1 alpha (ef-1α), have been identified in other apicomplexans such as Babesia bovis and Plasmodium falciparum. METHODS: The B. bigemina ef-1a locus was defined by searching a partial genome library of B. bigemina (Sanger Institute). Presence of an intron in the 5' untranslated region was determined by 5' Rapid Amplification of cDNA Ends (RACE) analysis. Promoter activity was determined by measurement of luciferase expression at several time points after electroporation, efficiency of transfections and normalization of data was determined by quantitative PCR and by the percentage of parasitized erythrocytes. RESULTS: The ef-1α locus contains two identical head to head ef-1α genes separated by a 1.425 kb intergenic (IG) region. Significant sequence divergence in the regions upstream of the inverted repeats on each side of the B. bigemina IG region suggest independent regulation mechanisms for controlling expression of each of the two ef-1α genes. Plasmid constructs containing the 5' and 3' halves of the IG regions controlling the expression of the luciferase gene containing a 3' region of a B. bigemina rap-1a gene, were generated for the testing of luciferase activity in transiently transfected parasites. Both halves of the ef-1α IG region tested showed the ability to promote high level production of luciferase. Moreover, both B. bigemina ef-1α promoters are also active in transiently transfected B. bovis and conversely, a B. bovis ef-1α promoter is active in transiently transfected B. bigemina. CONCLUSIONS: Collectively these data demonstrate the existence of two distinct promoters with homologous and heterologous promoter function in B. bigemina and B. bovis which is described for the first time in Babesia species. This study is of significance for development of interspecies stable transfection systems for B. bigemina and for B. bovis.
[Mh] Termos MeSH primário: Babesia/genética
Fator 1 de Elongação de Peptídeos/biossíntese
Fator 1 de Elongação de Peptídeos/genética
Regiões Promotoras Genéticas
[Mh] Termos MeSH secundário: Fusão Gênica Artificial
Perfilação da Expressão Gênica
Genes Reporter
Luciferases/análise
Luciferases/genética
Reação em Cadeia da Polimerase em Tempo Real
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Elongation Factor 1); EC 1.13.12.- (Luciferases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161113
[St] Status:MEDLINE


  8 / 1971 MEDLINE  
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[PMID]:27697031
[Au] Autor:Li X; Zeng H; Wang P; Lin L; Liu L; Zhen P; Fu Y; Lu P; Zhu H
[Ti] Título:Reactivation of latent HIV-1 in latently infected cells by coumarin compounds: Hymecromone and ScoparoneReactivation of Latent HIV-1 in Latently Infected Cells by Coumarin Compounds: Hymecromone and Scoparone.
[So] Source:Curr HIV Res;14(6):484-490, 2016.
[Is] ISSN:1873-4251
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Current antiretroviral therapy (ART) cannot cure HIV-1 infection due to the presence of latent viral reservoirs. The "shock and kill" strategy is a promising approach to eliminate the viral reservoir. However, there are various limits existing in current latency-reversing agents, searching for new activators are urgently needed. OBJECTIVE: The present study aimed at investigating the ability of hymecromone and scoparone for activating HIV-1 from latent reservoirs. METHODS: Jurkat T cell model of HIV-1 latently were used to evaluate the effect of hymecromone and scoparone. The percentage of green florescence protein expression as a marker for reactivation of HIV-1 promoter was measured via FACScan. The expression of CD25 and CD69 in human peripheral blood mononuclear cells was measured by flow cytometry at 72 h post-treatment with hymecromone or scoparone or prostratin using antibodies against CD25 and CD69. RESULTS: Hymecromone and scoparone can induce HIV-1 LTR reactivation in a dose and timedependent. We further show that hymecromone and scoparone can reactivate latent virus without inducing the activation of global T cells. We also found that scoparone acts by NF-&kgr;B signal pathway. CONCLUSION: Hymecromone and scoparone can effectively reactivate latent HIV-1 with low cellular toxicity, indicating hymecromone and scoparone might be potential drugs for HIV-1 reservoir eradication strategies in the future.
[Mh] Termos MeSH primário: Cumarínicos/metabolismo
HIV-1/efeitos dos fármacos
Himecromona/metabolismo
Provírus/efeitos dos fármacos
Ativação Viral/efeitos dos fármacos
[Mh] Termos MeSH secundário: Adulto
Antígenos CD/análise
Antígenos de Diferenciação de Linfócitos T/análise
Fusão Gênica Artificial
Células Cultivadas
Citometria de Fluxo
Genes Reporter
Proteínas de Fluorescência Verde/análise
Proteínas de Fluorescência Verde/biossíntese
Proteínas de Fluorescência Verde/genética
Seres Humanos
Subunidade alfa de Receptor de Interleucina-2/análise
Lectinas Tipo C/análise
Leucócitos Mononucleares/química
Leucócitos Mononucleares/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD); 0 (Antigens, Differentiation, T-Lymphocyte); 0 (CD69 antigen); 0 (Coumarins); 0 (IL2RA protein, human); 0 (Interleukin-2 Receptor alpha Subunit); 0 (Lectins, C-Type); 147336-22-9 (Green Fluorescent Proteins); 3T5NG4Q468 (Hymecromone); H5841PDT4Y (scoparone)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170810
[Lr] Data última revisão:
170810
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161005
[St] Status:MEDLINE


  9 / 1971 MEDLINE  
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[PMID]:27536883
[Au] Autor:Gao D; Zhan Y; Di W; Moore AR; Sher JJ; Guan Y; Wang S; Zhang Z; Murphy DA; Sawyers CL; Chi P; Chen Y
[Ad] Endereço:Key Laboratory of Systems Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, 200031, China.
[Ti] Título:A Tmprss2-CreERT2 Knock-In Mouse Model for Cancer Genetic Studies on Prostate and Colon.
[So] Source:PLoS One;11(8):e0161084, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fusion between TMPRSS2 and ERG, placing ERG under the control of the TMPRSS2 promoter, is the most frequent genetic alteration in prostate cancer, present in 40-50% of cases. The fusion event is an early, if not initiating, event in prostate cancer, implicating the TMPRSS2-positive prostate epithelial cell as the cancer cell of origin in fusion-positive prostate cancer. To introduce genetic alterations into Tmprss2-positive cells in mice in a temporal-specific manner, we generated a Tmprss2-CreERT2 knock-in mouse. We found robust tamoxifen-dependent Cre activation in the prostate luminal cells but not basal epithelial cells, as well as epithelial cells of the bladder and gastrointestinal (GI) tract. The knock-in allele on the Tmprss2 locus does not noticeably impact prostate, bladder, or gastrointestinal function. Deletion of Pten in Tmprss2-positive cells of adult mice generated neoplasia only in the prostate, while deletion of Apc in these cells generated neoplasia only in the GI tract. These results suggest that this new Tmprss2-CreERT2 mouse model will be a useful resource for genetic studies on prostate and colon.
[Mh] Termos MeSH primário: Neoplasias do Colo/genética
Neoplasias da Próstata/genética
Serina Endopeptidases/genética
[Mh] Termos MeSH secundário: Animais
Fusão Gênica Artificial/métodos
Modelos Animais de Doenças
Feminino
Técnicas de Introdução de Genes
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Regiões Promotoras Genéticas
Tamoxifeno/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
094ZI81Y45 (Tamoxifen); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.- (TMPRSS2 protein, mouse)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170802
[Lr] Data última revisão:
170802
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160819
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0161084


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[PMID]:27289037
[Au] Autor:Zhang Y; Osei-Adjei G; Ni B; Fang H; Zhang L; Zhao X; Huang X; Yang H; Yang W; Sun F
[Ad] Endereço:School of Medicine, Jiangsu University, Zhenjiang, 212013, Jiangsu, China.
[Ti] Título:Transcription of exsD is repressed directly by H-NS in Vibrio parahaemolyticus.
[So] Source:Microb Pathog;97:221-5, 2016 Aug.
[Is] ISSN:1096-1208
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Vibrio parahaemolyticus is a leading cause of seafood-associated diarrhea and gastroenteritis. This bacteria expresses a major virulence determinant called T3SS1. Expression of T3SS1 is tightly regulated by the ExsA-ExsC-ExsD regulatory system. The transcription of exsA and probably exsC is repressed directly by the H-NS protein. In this study, the regulation of exsD by H-NS was investigated using quantitative RT-PCR, primer extension, LacZ fusion, electrophoretic mobility shift, and DNase I footprinting assays. The results showed that His-H-NS protected a single region from 61 bp to 174 bp upstream of exsD against DNase I digestion, and a transcription start site located at 105 bp upstream of exsD was detected and its activity was repressed by H-NS. Therefore, a single H-NS-dependent promoter was transcribed for exsD in V. parahaemolyticus. Thus, all three genes in the ExsA-ExsC-ExsD regulatory system of T3SS1 are directly repressed by H-NS in V. parahaemolyticus.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Proteínas de Ligação a DNA/metabolismo
Regulação Bacteriana da Expressão Gênica
Genes Reguladores
Proteínas de Membrana/biossíntese
Transcrição Genética
Vibrio parahaemolyticus/genética
Vibrio parahaemolyticus/metabolismo
[Mh] Termos MeSH secundário: Fusão Gênica Artificial
Pegada de DNA
Ensaio de Desvio de Mobilidade Eletroforética
Perfilação da Expressão Gênica
Genes Bacterianos
Proteínas de Membrana/genética
Reação em Cadeia da Polimerase em Tempo Real
Sítio de Iniciação de Transcrição
beta-Galactosidase/análise
beta-Galactosidase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (DNA-Binding Proteins); 0 (H-NS protein, bacteria); 0 (Membrane Proteins); EC 3.2.1.23 (beta-Galactosidase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170327
[Lr] Data última revisão:
170327
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160612
[St] Status:MEDLINE



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