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  1 / 1256 MEDLINE  
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[PMID]:27777102
[Au] Autor:Mumaw CL; Surace M; Levesque S; Kodavanti UP; Kodavanti PRS; Royland JE; Block ML
[Ad] Endereço:Department of Anatomy and Cell Biology, The Stark Neuroscience Research Institute, Indiana University School of Medicine, Indianapolis, IN 46202, USA.
[Ti] Título:Atypical microglial response to biodiesel exhaust in healthy and hypertensive rats.
[So] Source:Neurotoxicology;59:155-163, 2017 03.
[Is] ISSN:1872-9711
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Accumulating evidence suggests a deleterious role for urban air pollution in central nervous system (CNS) diseases and neurodevelopmental disorders. Microglia, the resident innate immune cells and sentinels in the brain, are a common source of neuroinflammation and are implicated in air pollution-induced CNS effects. While renewable energy, such as soy-based biofuel, is of increasing public interest, there is little information on how soy biofuel may affect the brain, especially in people with preexisting disease conditions. To address this, male spontaneously hypertensive rats (SHR) and normotensive Wistar Kyoto (WKY) rats were exposed to 100% Soy-based Biodiesel Exhaust (100SBDE; 0, 50, 150 and 500µg/m ) by inhalation, 4h/day for 4 weeks (5 days/week). Ionized calcium-binding adapter molecule-1 (IBA-1) staining of microglia in the substantia nigra revealed significant changes in morphology with 100SBDE exposure in rats from both genotypes, where SHR were less sensitive. Aconitase activity was inhibited in the frontal cortex and cerebellum of WKY rats exposed to 100SBDE. No consistent changes occurred in pro-inflammatory cytokine expression, nitrated protein, or arginase1 expression in brain regions from either rat strain exposed to 100SBDE. However, while IBA-1 mRNA expression was not modified, CX3CR1 mRNA expression was lower in the striatum of 100SBDE exposed rats regardless of genotype, suggesting a downregulation of the fractalkine receptor on microglia in this brain region. Together, these data indicate that while microglia are detecting and responding to 100SBDE exposure with changes in morphology, there is reduced expression of CX3CR1 regardless of genetic background and the activation response is atypical without traditional inflammatory markers of M1 or M2 activation in the brain.
[Mh] Termos MeSH primário: Biocombustíveis/toxicidade
Quimiocina CX3CL1/metabolismo
Hipertensão/fisiopatologia
Microglia/efeitos dos fármacos
Substância Negra/patologia
Emissões de Veículos/toxicidade
[Mh] Termos MeSH secundário: Aconitato Hidratase/metabolismo
Animais
Antioxidantes/metabolismo
Proteínas de Ligação ao Cálcio/metabolismo
Citocinas/metabolismo
Relação Dose-Resposta a Droga
Hipertensão/genética
Hipertensão/patologia
Masculino
Proteínas dos Microfilamentos/metabolismo
Microglia/classificação
Estresse Oxidativo/efeitos dos fármacos
RNA Mensageiro/metabolismo
Ratos
Ratos Endogâmicos SHR
Ratos Endogâmicos WKY
Tirosina/análogos & derivados
Tirosina/metabolismo
Tirosina 3-Mono-Oxigenase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Aif1 protein, rat); 0 (Antioxidants); 0 (Biofuels); 0 (Calcium-Binding Proteins); 0 (Chemokine CX3CL1); 0 (Cytokines); 0 (Microfilament Proteins); 0 (RNA, Messenger); 0 (Vehicle Emissions); 3604-79-3 (3-nitrotyrosine); 42HK56048U (Tyrosine); EC 1.14.16.2 (Tyrosine 3-Monooxygenase); EC 4.2.1.3 (Aconitate Hydratase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


  2 / 1256 MEDLINE  
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[PMID]:27773628
[Au] Autor:Choby JE; Mike LA; Mashruwala AA; Dutter BF; Dunman PM; Sulikowski GA; Boyd JM; Skaar EP
[Ad] Endereço:Department of Pathology, Microbiology, & Immunology, Vanderbilt University Medical Center, Nashville, TN 37232, USA; Graduate Program in Microbiology & Immunology, Vanderbilt University, Nashville, TN 37232, USA.
[Ti] Título:A Small-Molecule Inhibitor of Iron-Sulfur Cluster Assembly Uncovers a Link between Virulence Regulation and Metabolism in Staphylococcus aureus.
[So] Source:Cell Chem Biol;23(11):1351-1361, 2016 Nov 17.
[Is] ISSN:2451-9448
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The rising problem of antimicrobial resistance in Staphylococcus aureus necessitates the discovery of novel therapeutic targets for small-molecule intervention. A major obstacle of drug discovery is identifying the target of molecules selected from high-throughput phenotypic assays. Here, we show that the toxicity of a small molecule termed '882 is dependent on the constitutive activity of the S. aureus virulence regulator SaeRS, uncovering a link between virulence factor production and energy generation. A series of genetic, physiological, and biochemical analyses reveal that '882 inhibits iron-sulfur (Fe-S) cluster assembly most likely through inhibition of the Suf complex, which synthesizes Fe-S clusters. In support of this, '882 supplementation results in decreased activity of the Fe-S cluster-dependent enzyme aconitase. Further information regarding the effects of '882 has deepened our understanding of virulence regulation and demonstrates the potential for small-molecule modulation of Fe-S cluster assembly in S. aureus and other pathogens.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Proteínas de Bactérias/metabolismo
Proteínas com Ferro-Enxofre/metabolismo
Bibliotecas de Moléculas Pequenas/farmacologia
Infecções Estafilocócicas/tratamento farmacológico
Staphylococcus aureus/efeitos dos fármacos
Fatores de Virulência/metabolismo
[Mh] Termos MeSH secundário: Aconitato Hidratase/metabolismo
Antibacterianos/química
Descoberta de Drogas
Seres Humanos
Proteínas Quinases/metabolismo
Transdução de Sinais/efeitos dos fármacos
Bibliotecas de Moléculas Pequenas/química
Infecções Estafilocócicas/microbiologia
Staphylococcus aureus/crescimento & desenvolvimento
Staphylococcus aureus/metabolismo
Fatores de Transcrição/metabolismo
Virulência/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Iron-Sulfur Proteins); 0 (SaeR protein, Staphylococcus aureus); 0 (Small Molecule Libraries); 0 (Transcription Factors); 0 (Virulence Factors); EC 2.7.- (Protein Kinases); EC 2.7.3.- (SaeS protein, Staphylococcus aureus); EC 4.2.1.3 (Aconitate Hydratase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180201
[Lr] Data última revisão:
180201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  3 / 1256 MEDLINE  
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[PMID]:27771440
[Au] Autor:Marcus D; Lichtenstein M; Cohen N; Hadad R; Erlich-Hadad T; Greif H; Lorberboum-Galski H
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Institute for Medical Research Israel-Canada (IMRIC), Faculty of Medicine, Hebrew University of Jerusalem, Jerusalem 91120, Israel.
[Ti] Título:Heterologous mitochondrial targeting sequences can deliver functional proteins into mitochondria.
[So] Source:Int J Biochem Cell Biol;81(Pt A):48-56, 2016 12.
[Is] ISSN:1878-5875
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Mitochondrial Targeting Sequences (MTSs) are responsible for trafficking nuclear-encoded proteins into mitochondria. Once entering the mitochondria, the MTS is recognized and cleaved off. Some MTSs are long and undergo two-step processing, as in the case of the human frataxin (FXN) protein (80aa), implicated in Friedreich's ataxia (FA). Therefore, we chose the FXN protein to examine whether nuclear-encoded mitochondrial proteins can efficiently be targeted via a heterologous MTS (hMTS) and deliver a functional protein into mitochondria. We examined three hMTSs; that of citrate synthase (cs), lipoamide deydrogenase (LAD) and C6ORF66 (ORF), as classically MTS sequences, known to be removed by one-step processing, to deliver FXN into mitochondria, in the form of fusion proteins. We demonstrate that using hMTSs for delivering FXN results in the production of 4-5-fold larger amounts of the fusion proteins, and at 4-5-fold higher concentrations. Moreover, hMTSs delivered a functional FXN protein into the mitochondria even more efficiently than the native MTSfxn, as evidenced by the rescue of FA patients' cells from oxidative stress; demonstrating a 18%-54% increase in cell survival; and a 13%-33% increase in ATP levels, as compared to the fusion protein carrying the native MTS. One fusion protein with MTScs increased aconitase activity within patients' cells, by 400-fold. The implications form our studies are of vast importance for both basic and translational research of mitochondrial proteins as any mitochondrial protein can be delivered efficiently by an hMTS. Moreover, effective targeting of functional proteins is important for restoration of mitochondrial function and treatment of related disorders.
[Mh] Termos MeSH primário: Proteínas de Ligação ao Ferro/metabolismo
Mitocôndrias/metabolismo
[Mh] Termos MeSH secundário: Aconitato Hidratase/metabolismo
Ataxia de Friedreich/metabolismo
Seres Humanos
Estresse Oxidativo
Transporte Proteico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Iron-Binding Proteins); 0 (frataxin); EC 4.2.1.3 (Aconitate Hydratase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171217
[Lr] Data última revisão:
171217
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161106
[St] Status:MEDLINE


  4 / 1256 MEDLINE  
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[PMID]:28400269
[Au] Autor:Zhou F; Xu X; Wu J; Wang D; Wang J
[Ad] Endereço:State Key Laboratory of Bioelectronics, Southeast University, Nanjing 210096, China.
[Ti] Título:NF-κB controls four genes encoding core enzymes of tricarboxylic acid cycle.
[So] Source:Gene;621:12-20, 2017 Jul 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:NF-κB may promote tumor progression by altering cell metabolism. Hence, finding its target genes that are involved in cell metabolism is helpful for understanding its role in tumor growth. Here we discovered four metabolism-related target genes of this transcription factor. By analyzing a chromatin immunoprecipitation followed by deep sequencing (ChIP-Seq) data that characterizing the global binding sites (BSs) of NF-κB RelA in the TNFα-stimulated HeLa cells, we found that four genes that encode core enzymes of the tricarboxylic acid (TCA) cycle, including IDH1, IDH3A, ACO2, and SUCLA2, were multiply bound by this transcription factor. The subsequent bioinformatic analysis revealed that the NF-κB BSs contained many canonical κB sequences and the NF-κB-like DNA-binding motifs. Detection of ChIPed DNA with polymerase chain reaction (ChIP-PCR) also indicated that the NF-κB BSs were bound by NF-κB in both TNFα-treated HeLa and HepG2 cells. The reporter construct showed that the NF-κB BSs could activate the luciferase expression in cells in a NF-κB-specific manner. The quantitative PCR and Western blot detections demonstrated that NF-κB could regulate the expressions of IDH1, IDH3A, and ACO2 genes at both mRNA and protein levels and that of SUCLA2 gene at mRNA level in the TNFα-treated HeLa and HepG2 cells. Based on these investigations we identified the four genes as new target genes of NF-κB. The finding provides new insights into the role of NF-κB in cellular energetic metabolism, which may be beneficial for understanding the metabolic physiology of tumor growth.
[Mh] Termos MeSH primário: Ciclo do Ácido Cítrico/genética
Regulação Neoplásica da Expressão Gênica
NF-kappa B/metabolismo
[Mh] Termos MeSH secundário: Aconitato Hidratase/genética
Aconitato Hidratase/metabolismo
Células HeLa
Células Hep G2
Seres Humanos
Isocitrato Desidrogenase/genética
Isocitrato Desidrogenase/metabolismo
Succinato-CoA Ligases/genética
Succinato-CoA Ligases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NF-kappa B); EC 1.1.1.41 (Isocitrate Dehydrogenase); EC 1.1.1.42. (IDH1 protein, human); EC 4.2.1.3 (ACO2 protein, human); EC 4.2.1.3 (Aconitate Hydratase); EC 6.2.1.- (Succinate-CoA Ligases); EC 6.2.1.5 (SUCLA2 protein, human)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170615
[Lr] Data última revisão:
170615
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170413
[St] Status:MEDLINE


  5 / 1256 MEDLINE  
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[PMID]:28099473
[Au] Autor:Mashruwala AA; Boyd JM
[Ad] Endereço:Department of Biochemistry and Microbiology, Rutgers University, New Brunswick, New Jersey, United States of America.
[Ti] Título:The Staphylococcus aureus SrrAB Regulatory System Modulates Hydrogen Peroxide Resistance Factors, Which Imparts Protection to Aconitase during Aerobic Growth.
[So] Source:PLoS One;12(1):e0170283, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The SrrAB two-component regulatory system (TCRS) positively influences the transcription of genes involved in aerobic respiration in response to changes in respiratory flux. Hydrogen peroxide (H2O2) can arise as a byproduct of spontaneous interactions between dioxygen and components of respiratory pathways. H2O2 damages cellular factors including protein associated iron-sulfur cluster prosthetic groups. We found that a Staphylococcus aureus strain lacking the SrrAB two-component regulatory system (TCRS) is sensitive to H2O2 intoxication. We tested the hypothesis that SrrAB manages the mutually inclusive expression of genes required for aerobic respiration and H2O2 resistance. Consistent with our hypothesis, a ΔsrrAB strain had decreased transcription of genes encoding for H2O2 resistance factors (kat, ahpC, dps). SrrAB was not required for the inducing the transcription of these genes in cells challenged with H2O2. Purified SrrA bound to the promoter region for dps suggesting that SrrA directly influences dps transcription. The H2O2 sensitivity of the ΔsrrAB strain was alleviated by iron chelation or deletion of the gene encoding for the peroxide regulon repressor (PerR). The positive influence of SrrAB upon H2O2 metabolism bestowed protection upon the solvent accessible iron-sulfur (FeS) cluster of aconitase from H2O2 poisoning. SrrAB also positively influenced transcription of scdA (ytfE), which encodes for a FeS cluster repair protein. Finally, we found that SrrAB positively influences H2O2 resistance only during periods of high dioxygen-dependent respiratory activity. SrrAB did not influence H2O2 resistance when cellular respiration was diminished as a result of decreased dioxygen availability, and negatively influenced it in the absence of respiration (fermentative growth). We propose a model whereby SrrAB-dependent regulatory patterns facilitate the adaptation of cells to changes in dioxygen concentrations, and thereby aids in the prevention of H2O2 intoxication during respiratory growth upon dixoygen.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Farmacorresistência Bacteriana/genética
Peróxido de Hidrogênio/farmacologia
Estresse Oxidativo/efeitos dos fármacos
Proteínas Repressoras/genética
Proteínas Repressoras/metabolismo
Staphylococcus aureus/metabolismo
[Mh] Termos MeSH secundário: Aconitato Hidratase/metabolismo
Testes de Sensibilidade Microbiana
Regiões Promotoras Genéticas/genética
Staphylococcus aureus/genética
Staphylococcus aureus/crescimento & desenvolvimento
Transcrição Genética/genética
Ativação Transcricional/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Repressor Proteins); 0 (SrrA protein, Staphyolococcus aureus); 0 (SrrB protein, Staphyolococcus aureus); 0 (peroxide repressor proteins); BBX060AN9V (Hydrogen Peroxide); EC 4.2.1.3 (Aconitate Hydratase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170816
[Lr] Data última revisão:
170816
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170119
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0170283


  6 / 1256 MEDLINE  
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[PMID]:27872198
[Au] Autor:Pavón N; Cabrera-Orefice A; Gallardo-Pérez JC; Uribe-Alvarez C; Rivero-Segura NA; Vazquez-Martínez ER; Cerbón M; Martínez-Abundis E; Torres-Narvaez JC; Martínez-Memije R; Roldán-Gómez FJ; Uribe-Carvajal S
[Ad] Endereço:Departamento de FarmacologíaInstituto Nacional de Cardiología Ignacio Chávez, México, Mexico pavitonat@yahoo.com.mx.
[Ti] Título:In female rat heart mitochondria, oophorectomy results in loss of oxidative phosphorylation.
[So] Source:J Endocrinol;232(2):221-235, 2017 Feb.
[Is] ISSN:1479-6805
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Oophorectomy in adult rats affected cardiac mitochondrial function. Progression of mitochondrial alterations was assessed at one, two and three months after surgery: at one month, very slight changes were observed, which increased at two and three months. Gradual effects included decrease in the rates of oxygen consumption and in respiratory uncoupling in the presence of complex I substrates, as well as compromised Ca buffering ability. Malondialdehyde concentration increased, whereas the ROS-detoxifying enzyme Mn superoxide dismutase (MnSOD) and aconitase lost activity. In the mitochondrial respiratory chain, the concentration and activity of complex I and complex IV decreased. Among other mitochondrial enzymes and transporters, adenine nucleotide carrier and glutaminase decreased. 2-Oxoglutarate dehydrogenase and pyruvate dehydrogenase also decreased. Data strongly suggest that in the female rat heart, estrogen depletion leads to progressive, severe mitochondrial dysfunction.
[Mh] Termos MeSH primário: Mitocôndrias Cardíacas/metabolismo
Ovariectomia
Fosforilação Oxidativa
Consumo de Oxigênio/fisiologia
Espécies Reativas de Oxigênio/metabolismo
[Mh] Termos MeSH secundário: Aconitato Hidratase/metabolismo
Animais
Feminino
Malondialdeído/metabolismo
Ratos
Superóxido Dismutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Reactive Oxygen Species); 4Y8F71G49Q (Malondialdehyde); EC 1.15.1.1 (Superoxide Dismutase); EC 4.2.1.3 (Aconitate Hydratase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170614
[Lr] Data última revisão:
170614
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161123
[St] Status:MEDLINE


  7 / 1256 MEDLINE  
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[PMID]:27744476
[Au] Autor:Lu XM; Chen C; Zheng TL
[Ad] Endereço:Institute for Eco-Environmental Sciences, Wenzhou Vocational College of Science & Technology, Wenzhou, 325006, People's Republic of China. 13736961468@163.com.
[Ti] Título:Metagenomic Insights into Effects of Chemical Pollutants on Microbial Community Composition and Function in Estuarine Sediments Receiving Polluted River Water.
[So] Source:Microb Ecol;73(4):791-800, 2017 May.
[Is] ISSN:1432-184X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pyrosequencing and metagenomic profiling were used to assess the phylogenetic and functional characteristics of microbial communities residing in sediments collected from the estuaries of Rivers Oujiang (OS) and Jiaojiang (JS) in the western region of the East China Sea. Another sediment sample was obtained from near the shore far from estuaries, used for contrast (CS). Characterization of estuary sediment bacterial communities showed that toxic chemicals potentially reduced the natural variability in microbial communities, while they increased the microbial metabolic enzymes and pathways. Polycyclic aromatic hydrocarbons (PAHs) and nitrobenzene were negatively correlated with the bacterial community variation. The dominant class in the sediments was Gammaproteobacteria. According to Kyoto Encyclopedia of Genes and Genomes (KEGG) enzyme profiles, dominant enzymes were found in estuarine sediments, which increased greatly, such as 2-oxoglutarate synthase, acetolactate synthase, inorganic diphosphatase, and aconitate hydratase. In KEGG pathway profiles, most of the pathways were also dominated by specific metabolism in these sediments and showed a marked increase, for instance alanine, aspartate, and glutamate metabolism, carbon fixation pathways in prokaryotes, and aminoacyl-tRNA biosynthesis. The estuarine sediment bacterial diversity varied with the polluted river water inputs. In the estuary receiving river water from the more seriously polluted River Oujiang, the sediment bacterial community function was more severely affected.
[Mh] Termos MeSH primário: Bactérias/classificação
Bactérias/genética
Estuários
Sedimentos Geológicos/microbiologia
Metagenômica/métodos
Consórcios Microbianos/genética
Rios/microbiologia
Poluentes Químicos da Água/análise
[Mh] Termos MeSH secundário: Acetolactato Sintase/metabolismo
Aconitato Hidratase/metabolismo
Aminoácidos/metabolismo
Bactérias/enzimologia
Bactérias/metabolismo
Sequência de Bases
Ciclo do Carbono
China
Água Doce
Sedimentos Geológicos/química
Cetona Oxirredutases/metabolismo
Redes e Vias Metabólicas
Consórcios Microbianos/efeitos dos fármacos
Nitrobenzenos/efeitos adversos
Filogenia
Hidrocarbonetos Aromáticos Policíclicos/efeitos adversos
RNA Ribossômico 16S/genética
Salinidade
Análise de Sequência
Poluentes Químicos da Água/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Nitrobenzenes); 0 (Polycyclic Aromatic Hydrocarbons); 0 (RNA, Ribosomal, 16S); 0 (Water Pollutants, Chemical); E57JCN6SSY (nitrobenzene); EC 1.2.- (Ketone Oxidoreductases); EC 1.2.7.3 (2-oxoglutarate synthase); EC 2.2.1.6 (Acetolactate Synthase); EC 4.2.1.3 (Aconitate Hydratase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161017
[St] Status:MEDLINE
[do] DOI:10.1007/s00248-016-0868-8


  8 / 1256 MEDLINE  
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[PMID]:27543843
[Au] Autor:Yang Z; Gao X; Xie H; Wang F; Ren Y; Wei D
[Ad] Endereço:State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai 200237, China.
[Ti] Título:Enhanced itaconic acid production by self-assembly of two biosynthetic enzymes in Escherichia coli.
[So] Source:Biotechnol Bioeng;114(2):457-462, 2017 Feb.
[Is] ISSN:1097-0290
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Here, we described a novel strategy for the production of itaconic acid in Escherichia coli by self-assembly of aconitase (ACO) and cis-aconitate decarboxylase (CAD) existing in the metabolic pathway of itaconic acid via the protein-peptide interactions of PDZ domain and PDZ ligand. Co-expression of ACO and CAD in E. coli (uCA) resulted in low levels of itaconate (117.25 mg/L) after 48 h fermentation while the itaconate titre was significantly improved up to 222.15 mg/L by self-assembly of ACO-PDZ (APd) and CAD-PDZlig (CPl) in E. coli (sPP) under the same conditions. To further confirm the effect of self-assembly, the itaconate catalyzed from sodium citrate was determined. The sPP was extra efficacious in the early catalytic period, showing approximately threefold itaconate yields increased after 2 h catalysis, when compared to uCA. Furthermore, the itaconate production of sPP was increased from 5 to 8.7 g/L after 30 h of reaction compared to uCA. This self-assembly strategy showed remarkable potential for the further improvement of itaconate production. Biotechnol. Bioeng. 2017;114: 457-462. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Aconitato Hidratase/metabolismo
Carboxiliases/metabolismo
Escherichia coli/genética
Engenharia Metabólica/métodos
Succinatos/metabolismo
[Mh] Termos MeSH secundário: Aconitato Hidratase/química
Aconitato Hidratase/genética
Aspergillus/enzimologia
Aspergillus/genética
Carboxiliases/química
Carboxiliases/genética
Escherichia coli/metabolismo
Fermentação
Proteínas Fúngicas/química
Proteínas Fúngicas/genética
Proteínas Fúngicas/metabolismo
Multimerização Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Succinatos/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Recombinant Proteins); 0 (Succinates); EC 4.1.1.- (Carboxy-Lyases); EC 4.1.1.6 (aconitate decarboxylase); EC 4.2.1.3 (Aconitate Hydratase); Q4516562YH (itaconic acid)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160821
[St] Status:MEDLINE
[do] DOI:10.1002/bit.26081


  9 / 1256 MEDLINE  
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[PMID]:27506145
[Au] Autor:Nanduri J; Peng YJ; Wang N; Khan SA; Semenza GL; Kumar GK; Prabhakar NR
[Ad] Endereço:Institute For Integrative Physiology and Center for Systems Biology of O2 Sensing, Biological Science Division, The University of Chicago, Chicago, IL, USA.
[Ti] Título:Epigenetic regulation of redox state mediates persistent cardiorespiratory abnormalities after long-term intermittent hypoxia.
[So] Source:J Physiol;595(1):63-77, 2017 Jan 01.
[Is] ISSN:1469-7793
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:KEY POINTS: The effects of short-term (ST; 10 days) and long-term (LT; 30 days) intermittent hypoxia (IH) on blood pressure (BP), breathing and carotid body (CB) chemosensory reflex were examined in adult rats. ST- and LT-IH treated rats exhibited hypertension, irregular breathing with apnoea and augmented the CB chemosensory reflex, with all these responses becoming normalized during recovery from ST- but not from LT-IH. The persistent cardiorespiratory responses to LT-IH were associated with elevated reactive oxygen species (ROS) levels in the CB and adrenal medulla, which were a result of DNA methylation-dependent suppression of genes encoding anti-oxidant enzymes (AOEs). Treating rats with decitabine either during LT-IH or during recovery from LT-IH prevented DNA methylation of AOE genes, normalized the expression of AOE genes and ROS levels, reversed the heightened CB chemosensory reflex and hypertension, and also stabilized breathing. ABSTRACT: Rodents exposed to chronic intermittent hypoxia (IH), simulating blood O saturation profiles during obstructive sleep apnoea (OSA), have been shown to exhibit a heightened carotid body (CB) chemosensory reflex and hypertension. CB chemosensory reflex activation also results in unstable breathing with apnoeas. However, the effect of chronic IH on breathing is not known. In the present study, we examined the effects of chronic IH on breathing along with blood pressure (BP) and assessed whether the autonomic responses are normalized after recovery from chronic IH. Studies were performed on adult, male, Sprague-Dawley rats exposed to either short-term (ST; 10 days) or long-term (LT, 30 days) IH. Rats exposed to either ST- or LT-IH exhibited hypertension, irregular breathing with apnoeas, an augmented CB chemosensory reflex as indicated by elevated CB neural activity and plasma catecholamine levels, and elevated reactive oxygen species (ROS) levels in the CB and adrenal medulla (AM). All these effects were normalized after recovery from ST-IH but not from LT-IH. Analysis of the molecular mechanisms underlying the persistent effects of LT-IH revealed increased DNA methylation of genes encoding anti-oxidant enzymes (AOEs). Treatment with decitabine, a DNA methylation inhibitor, either during LT-IH or during recovery from LT-IH, prevented DNA methylation, normalized the expression of AOE genes, ROS levels, CB chemosensory reflex and BP, and also stabilized breathing. These results suggest that persistent cardiorespiratory abnormalities caused by LT-IH are mediated by epigenetic re-programming of the redox state in the CB chemosensory reflex pathway.
[Mh] Termos MeSH primário: Hipertensão/fisiopatologia
Hipóxia/fisiopatologia
Transtornos Respiratórios/fisiopatologia
[Mh] Termos MeSH secundário: Aconitato Hidratase/metabolismo
Medula Suprarrenal/metabolismo
Animais
Pressão Sanguínea
Corpo Carotídeo/metabolismo
Corpo Carotídeo/fisiologia
Catalase/genética
Metilação de DNA
Epigênese Genética
Expressão Gênica
Glutationa Peroxidase/genética
Hipertensão/sangue
Hipertensão/genética
Hipertensão/metabolismo
Hipóxia/sangue
Hipóxia/genética
Hipóxia/metabolismo
Masculino
Malondialdeído/metabolismo
Norepinefrina/sangue
Oxirredução
Peroxirredoxinas/genética
Ratos Sprague-Dawley
Espécies Reativas de Oxigênio/metabolismo
Transtornos Respiratórios/sangue
Transtornos Respiratórios/genética
Transtornos Respiratórios/metabolismo
Superóxido Dismutase/genética
Superóxido Dismutase/metabolismo
Superóxido Dismutase-1/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Reactive Oxygen Species); 4Y8F71G49Q (Malondialdehyde); EC 1.11.1.15 (Peroxiredoxins); EC 1.11.1.15 (Prdx4 protein, rat); EC 1.11.1.6 (Catalase); EC 1.11.1.9 (Glutathione Peroxidase); EC 1.11.1.9 (glutathione peroxidase 2, rat); EC 1.15.1.1 (Sod1 protein, rat); EC 1.15.1.1 (Superoxide Dismutase); EC 1.15.1.1 (Superoxide Dismutase-1); EC 1.15.1.1 (superoxide dismutase 2); EC 4.2.1.3 (Aconitate Hydratase); X4W3ENH1CV (Norepinephrine)
[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:160811
[St] Status:MEDLINE
[do] DOI:10.1113/JP272346


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Fotocópia
[PMID]:27714684
[Au] Autor:Peña-Ortega F; Rivera-Angulo AJ; Lorea-Hernández JJ
[Ad] Endereço:Departamento de Neurobiología del Desarrollo y Neurofisiología, Instituto de Neurobiología, Universidad Nacional Autónoma de México, Boulevard Juriquilla 3001, Querétaro, 76230, Mexico. jfpena@unam.mx.
[Ti] Título:Pharmacological Tools to Study the Role of Astrocytes in Neural Network Functions.
[So] Source:Adv Exp Med Biol;949:47-66, 2016.
[Is] ISSN:0065-2598
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Despite that astrocytes and microglia do not communicate by electrical impulses, they can efficiently communicate among them, with each other and with neurons, to participate in complex neural functions requiring broad cell-communication and long-lasting regulation of brain function. Glial cells express many receptors in common with neurons; secrete gliotransmitters as well as neurotrophic and neuroinflammatory factors, which allow them to modulate synaptic transmission and neural excitability. All these properties allow glial cells to influence the activity of neuronal networks. Thus, the incorporation of glial cell function into the understanding of nervous system dynamics will provide a more accurate view of brain function. Our current knowledge of glial cell biology is providing us with experimental tools to explore their participation in neural network modulation. In this chapter, we review some of the classical, as well as some recent, pharmacological tools developed for the study of astrocyte's influence in neural function. We also provide some examples of the use of these pharmacological agents to understand the role of astrocytes in neural network function and dysfunction.
[Mh] Termos MeSH primário: Astrócitos/efeitos dos fármacos
Encéfalo/efeitos dos fármacos
Metionina Sulfoximina/farmacologia
Rede Nervosa/efeitos dos fármacos
Oligopeptídeos/farmacologia
[Mh] Termos MeSH secundário: Aconitato Hidratase/antagonistas & inibidores
Aconitato Hidratase/metabolismo
Animais
Astrócitos/citologia
Astrócitos/metabolismo
Encéfalo/citologia
Encéfalo/metabolismo
Caprilatos/farmacologia
Comunicação Celular/efeitos dos fármacos
Citratos/farmacologia
Fluoracetatos/farmacologia
Glutamato-Amônia Ligase/antagonistas & inibidores
Glutamato-Amônia Ligase/metabolismo
Seres Humanos
Microglia/citologia
Microglia/efeitos dos fármacos
Microglia/metabolismo
Rede Nervosa/citologia
Rede Nervosa/metabolismo
Neuroglia/citologia
Neuroglia/efeitos dos fármacos
Neuroglia/metabolismo
Neurônios/citologia
Neurônios/efeitos dos fármacos
Neurônios/metabolismo
Transmissão Sináptica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Caprylates); 0 (Citrates); 0 (Fluoroacetates); 0 (ONO2506); 0 (Oligopeptides); 0 (PAR-1-activating peptide); 1982-67-8 (Methionine Sulfoximine); 357-89-1 (fluorocitrate); EC 4.2.1.3 (Aconitate Hydratase); EC 6.3.1.2 (Glutamate-Ammonia Ligase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161008
[St] Status:MEDLINE



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