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[PMID]:29305973
[Au] Autor:Sitole BN; Mavri-Damelin D
[Ad] Endereço:The School of Molecular and Cell Biology, University of the Witwatersrand, Johannesburg, South Africa. Electronic address: boitumelo.moleya@students.wits.ac.za.
[Ti] Título:Peroxidasin is regulated by the epithelial-mesenchymal transition master transcription factor Snai1.
[So] Source:Gene;646:195-202, 2018 Mar 10.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Peroxidasin (PXDN), an ECM protein with peroxidase activity, is integral to basement membrane consolidation through catalysis of sulfilimine bonds in collagen IV. PXDN is also involved in processes where epithelial-mesenchymal transition (EMT) takes place, namely fibrosis, development and cancer. We therefore investigated whether PXDN is regulated by the EMT-master-regulator, Snai1. During TGF-ß1-induced EMT, PXDN expression decreased by up to 47% in two cervical-carcinoma cell lines, with concomitant increases in Snai1 and vimentin, and decrease in E-cadherin. TGF-ß1 induced Snai1 binding to the PXDN promoter (as assessed by chromatin immunoprecipitation-PCR) and significantly repressed luciferase reporter gene expression, as did Snai1 overexpression. In summary, our findings show that Snai1 mediates repression of PXDN and consolidate a role for this ECM-modifier during EMT.
[Mh] Termos MeSH primário: Transição Epitelial-Mesenquimal
Peroxidases/metabolismo
Fatores de Transcrição da Família Snail/metabolismo
Neoplasias do Colo do Útero/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Regulação para Baixo
Transição Epitelial-Mesenquimal/efeitos dos fármacos
Feminino
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Células HeLa
Seres Humanos
Peroxidases/genética
Regiões Promotoras Genéticas/efeitos dos fármacos
Fator de Crescimento Transformador beta1/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (SNAI1 protein, human); 0 (Snail Family Transcription Factors); 0 (Transforming Growth Factor beta1); EC 1.11.1.- (Peroxidases); EC 1.11.1.- (VPO1 protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180107
[St] Status:MEDLINE


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[PMID]:29101854
[Au] Autor:Gong L; Zhang S; Chen D; Liu K; Lu J
[Ad] Endereço:Ministry of Education Key Laboratory of Integrated Regulation and Resource Development on Shallow Lakes, College of Environment, Hohai University, Nanjing, 210098, China.
[Ti] Título:Response of biofilms-leaves of two submerged macrophytes to high ammonium.
[So] Source:Chemosphere;192:152-160, 2018 Feb.
[Is] ISSN:1879-1298
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Submerged macrophytes can provide attached surface for biofilms (known as periphyton) growth. In the present study, the alterations in biofilms formation, and chemical compositions and physiological responses were investigated on leaves of Vallisneria asiatica and Hydrilla verticillata exposed to 0.1 mg L (control) or with 10 mg L NH -N for 13 days. Results from physiological and biochemical indices (content of H O , malondialdehyde, total chlorophyll and activity of superoxide dismutase, catalase and peroxidase) showed that high ammonium caused oxidative damage to leaves of two species of plant. Multifractal analysis (based on scanning electron microscope images) showed that for the same plant, the values of width â–³α (â–³α = α -α ) of the f(α) and Δf (Δf = f(α )-f(α )) were smaller on leaves surface of two species of plant treated with 10 mg L NH -N for 13 days than their controls, suggesting high ammonium treatments reduced morphological heterogeneity of leaf surface and enhanced area of the colony-like biofilms. X-ray photoelectron spectroscopy analysis showed that C, O, N and P were dominant elements on leaves surface of two species of plant and ammonium application increased the percentage of C but decreased that of O. High ammonium increased C1 (C-C or C-H) percentage but decreased C2 (C-O) and C3 (O-C-O or C=O) percentage on leaves surface of two species of plant, indicating that ammonium stress changed the surface chemical states and thus might reduce the capacity of leaves to adsorb nutrients from water column. Our results provided useful information to understand ammonium induced toxicity to submerged macrophytes.
[Mh] Termos MeSH primário: Compostos de Amônio/metabolismo
Hydrocharitaceae/fisiologia
Folhas de Planta/fisiologia
[Mh] Termos MeSH secundário: Biofilmes
Catalase/metabolismo
Clorofila/metabolismo
Hydrocharitaceae/enzimologia
Hydrocharitaceae/crescimento & desenvolvimento
Malondialdeído/metabolismo
Peroxidases/metabolismo
Folhas de Planta/enzimologia
Folhas de Planta/crescimento & desenvolvimento
Proteínas de Plantas/metabolismo
Superóxido Dismutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ammonium Compounds); 0 (Plant Proteins); 1406-65-1 (Chlorophyll); 4Y8F71G49Q (Malondialdehyde); EC 1.11.1.- (Peroxidases); EC 1.11.1.6 (Catalase); EC 1.15.1.1 (Superoxide Dismutase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180123
[Lr] Data última revisão:
180123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171105
[St] Status:MEDLINE


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[PMID]:29220655
[Au] Autor:Pannunzio NR; Lieber MR
[Ad] Endereço:USC Norris Comprehensive Cancer Center, University of Southern California Keck School of Medicine, 1441 Eastlake Avenue, Rm. 5428, Los Angeles, CA 90089, USA.
[Ti] Título:AID and Reactive Oxygen Species Can Induce DNA Breaks within Human Chromosomal Translocation Fragile Zones.
[So] Source:Mol Cell;68(5):901-912.e3, 2017 Dec 07.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:DNA double-strand breaks (DSBs) occurring within fragile zones of less than 200 base pairs account for the formation of the most common human chromosomal translocations in lymphoid malignancies, yet the mechanism of how breaks occur remains unknown. Here, we have transferred human fragile zones into S. cerevisiae in the context of a genetic assay to understand the mechanism leading to DSBs at these sites. Our findings indicate that a combination of factors is required to sensitize these regions. Foremost, DNA strand separation by transcription or increased torsional stress can expose these DNA regions to damage from either the expression of human AID or increased oxidative stress. This damage causes DNA lesions that, if not repaired quickly, are prone to nuclease cleavage, resulting in DSBs. Our results provide mechanistic insight into why human neoplastic translocation fragile DNA sequences are more prone to enzymes or agents that cause longer-lived DNA lesions.
[Mh] Termos MeSH primário: Cromossomos Humanos/genética
Citidina Desaminase/genética
Quebras de DNA de Cadeia Dupla
DNA Fúngico/genética
Estresse Oxidativo
Espécies Reativas de Oxigênio/metabolismo
Saccharomyces cerevisiae/genética
Translocação Genética
[Mh] Termos MeSH secundário: Cromossomos Humanos/química
Cromossomos Humanos/metabolismo
Citidina Desaminase/metabolismo
DNA Fúngico/química
DNA Fúngico/metabolismo
Endonucleases/genética
Endonucleases/metabolismo
Regulação Enzimológica da Expressão Gênica
Regulação Fúngica da Expressão Gênica
Seres Humanos
Conformação de Ácido Nucleico
Peroxidases/genética
Peroxidases/metabolismo
Saccharomyces cerevisiae/enzimologia
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Relação Estrutura-Atividade
Transcrição Genética
Uracila-DNA Glicosidase/genética
Uracila-DNA Glicosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Fungal); 0 (Reactive Oxygen Species); 0 (Saccharomyces cerevisiae Proteins); EC 1.11.1.- (Peroxidases); EC 1.11.1.- (Tsa1 protein, S cerevisiae); EC 3.1.- (Endonucleases); EC 3.1.- (artemis nuclease, human); EC 3.2.2.- (Uracil-DNA Glycosidase); EC 3.5.4.- (AICDA (activation-induced cytidine deaminase)); EC 3.5.4.5 (Cytidine Deaminase)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE


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[PMID]:28463583
[Au] Autor:Yang SO; Sodaneath H; Lee JI; Jung H; Choi JH; Ryu HW; Cho KS
[Ad] Endereço:a Department of Environmental Science and Engineering , Ewha Womans University , Seoul , Republic of Korea.
[Ti] Título:Decolorization of acid, disperse and reactive dyes by Trametes versicolor CBR43.
[So] Source:J Environ Sci Health A Tox Hazard Subst Environ Eng;52(9):862-872, 2017 Jul 29.
[Is] ISSN:1532-4117
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The mycoremediation has been considered as a promising method for decolorizing dye wastewater. To explore new bioresource for mycoremediation, a new white-rot fungus that could decolorize various dyes commonly used in textile industries was isolated, and its ligninolytic enzyme activity and decolorization capacity were characterized. The isolated CBR43 was identified as Trametes versicolor based on the morphological properties of its fruit body and spores, as well as through partial 18S rDNA gene sequences. Isolated CBR43 displayed high activities of laccase and Mn-dependent peroxidase, whereas its lignin peroxidase activity was relatively low. These ligninolytic enzyme activities in potato dextrose broth (PDB) medium were enhanced by the addition of yeast extract (1-10 g L ). In particular, lignin peroxidase activity was increased more than 5 times in the PDB medium amended with 10 g L of yeast extract. The CBR43 decolorized more than 90% of 200 mg L acid dyes (red 114, blue 62 and black 172) and reactive dyes (red 120, blue 4, orange 16 and black 5) within 6 days in the PDB medium. CBR43 decolorized 67% of 200 mg L acid orange 7 within 9 days. The decolorization efficiencies for disperse dyes (red 1, orange 3 and black 1) were 51-80% within 9 days. The CBR43 could effectively decolorize high concentrations of acid blue 62 and acid black 172 (500-700 mg L ). The maximum dye decolorization rate was obtained at 28°C, pH 5, and 150 rpm in the PDB medium. T. versicolor CBR43 had high laccase and Mn-dependent peroxidase activities, and could decolorize a wide variety of dyes such as acid, disperse and reactive textile dyes. This fungus had decolorizing activities of azo-type dyes as well as anthraquinone-type dyes. T. versicolor CBR43 is one of promising bioresources for the decolorization of textile wastewater including various dyes.
[Mh] Termos MeSH primário: Compostos Azo/análise
Benzenossulfonatos/análise
Complexos de Coordenação/análise
Naftalenossulfonatos/análise
Trametes/crescimento & desenvolvimento
Poluentes Químicos da Água/análise
Purificação da Água/métodos
[Mh] Termos MeSH secundário: Biodegradação Ambiental
Lacase/metabolismo
Peroxidases/metabolismo
Indústria Têxtil
Trametes/enzimologia
Águas Residuais/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Azo Compounds); 0 (Benzenesulfonates); 0 (Coordination Complexes); 0 (Naphthalenesulfonates); 0 (Waste Water); 0 (Water Pollutants, Chemical); 0 (acid black 172); EC 1.10.3.2 (Laccase); EC 1.11.1.- (Peroxidases); EC 1.11.1.13 (manganese peroxidase); Q1LIY3BO0U (2-naphthol orange)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1080/10934529.2017.1316164


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[PMID]:28973477
[Au] Autor:Einarson OJ; Sen D
[Ad] Endereço:Department of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.
[Ti] Título:Self-biotinylation of DNA G-quadruplexes via intrinsic peroxidase activity.
[So] Source:Nucleic Acids Res;45(17):9813-9822, 2017 Sep 29.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The striking and ubiquitous in vitro affinity between hemin and DNA/RNA G-quadruplexes raises the intriguing possibility of its relevance to biology. To date, no satisfactory experimental framework has been reported for investigating such a possibility. Complexation by G-quadruplexes leads to activation of the bound hemin toward catalysis of 1- and 2-electron oxidative reactions, with phenolic compounds being particularly outstanding substrates. We report here a strategy for exploiting that intrinsic peroxidase activity of hemin•G-quadruplex complexes for self-biotinylation of their G-quadruplex component. Such self-biotinylation occurs with good efficiency and high discrimination in vitro, being specific for G-quadruplexes and not for duplexes. The biotinylated DNA, moreover, remains amenable to polymerase chain reaction amplification, rendering it suitable for analysis by ChIP-Seq and related methods. We anticipate that this self-biotinylation methodology will also serve as a sensitive tool, orthogonal to existing ones, for identifying, labeling and pulling down cellular RNA and DNA G-quadruplexes in general, as well as proteins bound to or proximal to such quadruplexes.
[Mh] Termos MeSH primário: DNA Catalítico/química
Quadruplex G
Hemina/química
Oligonucleotídeos/química
Peroxidases/química
[Mh] Termos MeSH secundário: Biocatálise
Técnicas Biossensoriais/métodos
Biotina/química
Biotinilação
Peróxido de Hidrogênio/química
Cinética
Mimetismo Molecular
Oxirredução
Fenóis/química
Reação em Cadeia da Polimerase
Estreptavidina/química
Tiramina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Catalytic); 0 (Oligonucleotides); 0 (Phenols); 0 (biotin tyramine); 6SO6U10H04 (Biotin); 743LRP9S7N (Hemin); 9013-20-1 (Streptavidin); BBX060AN9V (Hydrogen Peroxide); EC 1.11.1.- (Peroxidases); X8ZC7V0OX3 (Tyramine)
[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:171004
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx765


  6 / 15841 MEDLINE  
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[PMID]:28899945
[Au] Autor:Wu G; Zhao J; Franzen S; Tsai AL
[Ad] Endereço:Division of Hematology, Department of Internal Medicine, The University of Texas Health Science Center at Houston - McGovern Medical School, Houston, TX 77030, U.S.A.
[Ti] Título:Bindings of NO, CO, and O to multifunctional globin type dehaloperoxidase follow the 'sliding scale rule'.
[So] Source:Biochem J;474(20):3485-3498, 2017 Oct 05.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Dehaloperoxidase-hemoglobin (DHP), a multifunctional globin protein, not only functions as an oxygen carrier as typical globins such as myoglobin and hemoglobin, but also as a peroxidase, a mono- and dioxygenase, peroxygenase, and an oxidase. Kinetics of DHP binding to NO, CO, and O were characterized for wild-type DHP A and B and the H55D and H55V DHP A mutants using stopped-flow methods. All three gaseous ligands bind to DHP significantly more weakly than sperm whale myoglobin (SWMb). Both CO and NO bind to DHP in a one-step process to form a stable six-coordinate complex. Multiple-step NO binding is not observed in DHP, which is similar to observations in SWMb, but in contrast with many heme sensor proteins. The weak affinity of DHP for O is mainly due to a fast O dissociation rate, in accordance with a longer N-Fe distance between the heme iron and distal histidine in DHP than that in Mb, and an open-distal pocket that permits ligand escape. Binding affinities in DHP show the same 3-4 orders separation between the pairs NO/CO and CO/O , consistent with the 'sliding scale rule' hypothesis. Strong gaseous ligand discrimination by DHP is very different from that observed in typical peroxidases, which show poor gaseous ligand selectivity, correlating with a neutral proximal imidazole ligand rather than an imidazolate. The present study provides useful insights into the rationale for DHP to function both as mono-oxygenase and oxidase, and is the first example of a globin peroxidase shown to follow the 'sliding scale rule' hypothesis in gaseous ligand discrimination.
[Mh] Termos MeSH primário: Monóxido de Carbono/metabolismo
Globinas/metabolismo
Óxido Nítrico/metabolismo
Oxigênio/metabolismo
Peroxidases/metabolismo
[Mh] Termos MeSH secundário: Hemoglobinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hemoglobins); 31C4KY9ESH (Nitric Oxide); 7U1EE4V452 (Carbon Monoxide); 9004-22-2 (Globins); EC 1.11.1.- (Peroxidases); S88TT14065 (Oxygen)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170914
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170515


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[PMID]:28821623
[Au] Autor:Gomes F; Palma FR; Barros MH; Tsuchida ET; Turano HG; Alegria TGP; Demasi M; Netto LES
[Ad] Endereço:From the Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, 05508-090 São Paulo, fernandopgdna@hotmail.com.
[Ti] Título:Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments.
[So] Source:J Biol Chem;292(41):17011-17024, 2017 Oct 13.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Yeast Prx1 is a mitochondrial 1-Cys peroxiredoxin that catalyzes the reduction of endogenously generated H O Prx1 is synthesized on cytosolic ribosomes as a preprotein with a cleavable N-terminal presequence that is the mitochondrial targeting signal, but the mechanisms underlying Prx1 distribution to distinct mitochondrial subcompartments are unknown. Here, we provide direct evidence of the following dual mitochondrial localization of Prx1: a soluble form in the intermembrane space and a form in the matrix weakly associated with the inner mitochondrial membrane. We show that Prx1 sorting into the intermembrane space likely involves the release of the protein precursor within the lipid bilayer of the inner membrane, followed by cleavage by the inner membrane peptidase. We also found that during its import into the matrix compartment, Prx1 is sequentially cleaved by mitochondrial processing peptidase and then by octapeptidyl aminopeptidase 1 (Oct1). Oct1 cleaved eight amino acid residues from the N-terminal region of Prx1 inside the matrix, without interfering with its peroxidase activity Remarkably, the processing of peroxiredoxin (Prx) proteins by Oct1 appears to be an evolutionarily conserved process because yeast Oct1 could cleave the human mitochondrial peroxiredoxin Prx3 when expressed in Altogether, the processing of peroxiredoxins by Imp2 or Oct1 likely represents systems that control the localization of Prxs into distinct compartments and thereby contribute to various mitochondrial redox processes.
[Mh] Termos MeSH primário: Metaloproteases/metabolismo
Mitocôndrias/enzimologia
Peroxidases/metabolismo
Proteólise
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/enzimologia
[Mh] Termos MeSH secundário: Cisteína Endopeptidases/genética
Cisteína Endopeptidases/metabolismo
Seres Humanos
Metaloproteases/genética
Mitocôndrias/genética
Peroxidases/genética
Transporte Proteico/fisiologia
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Saccharomyces cerevisiae Proteins); 144416-78-4 (LMP-2 protein); EC 1.11.1.- (PRX1 protein, S cerevisiae); EC 1.11.1.- (Peroxidases); EC 3.4.- (Metalloproteases); EC 3.4.22.- (Cysteine Endopeptidases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170820
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.788588


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[PMID]:28755580
[Au] Autor:Jeyaraj Pandian C; Palanivel R; Balasundaram U
[Ad] Endereço:Department of Biochemistry, Manonmaniam Sundaranar University, Tirunelveli 627 012, Tamilnadu, India.
[Ti] Título:Green synthesized nickel nanoparticles for targeted detection and killing of S. typhimurium.
[So] Source:J Photochem Photobiol B;174:58-69, 2017 Sep.
[Is] ISSN:1873-2682
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Simple and sensitive colorimetric immunosensor based on peroxidase mimetic activity and photothermal effect of nickel oxide nanoparticle (NiOGs) has been developed to detect and kill food borne pathogen Salmonella typhimurium. NiOGs showed superior peroxidase mimetic activity for oxidation of peroxidase substrate 3, 3', 5, 5'-tetramethylbenzidine (TMB). Oxidation of TMB by NiOGs followed Michaelis-Menten kinetics with K and V values of 0.25mM and 2.64×10 M/s respectively. NiOGs was coated with citric acid (CA-NiOGs) followed by conjugation with antibody (anti-S. typhimurium) (Ab-CA-NiOGs) that effectively captured S. typhimurium. Colorimetric detection of S. typhimurium by Ab-CA-NiOGs showed a linear relationship between pathogen concentration (1×10 to 1×10 cfu/mL) and color signal (652nm) with limit of detection (LOD) of 10cfu/mL. The proposed method showed no cross reactivity against other pathogens. Recovery of S. typhimurium in milk and juice samples was found to be 95 to 100% and 92 to 99% respectively. NiOGs exposed to laser irradiation showed dose dependent increase in temperature and singlet oxygen within 5min. Bacteria bound to Ab-CA-NiOGs after laser irradiation, induced membrane damage and reduced bacterial viability to 6%. The bifunctional peroxidase-mimetic activity and photothermal effect of NiOGs can be exploited in selective sensing and killing of target pathogens respectively in food products.
[Mh] Termos MeSH primário: Nanopartículas Metálicas
Viabilidade Microbiana/efeitos dos fármacos
Nanotecnologia/métodos
Níquel/química
Níquel/farmacologia
Salmonella typhimurium/efeitos dos fármacos
Salmonella typhimurium/isolamento & purificação
[Mh] Termos MeSH secundário: Animais
Materiais Biomiméticos/química
Materiais Biomiméticos/farmacologia
Técnicas de Química Sintética
Contaminação de Alimentos/análise
Química Verde
Peroxidases/metabolismo
Salmonella typhimurium/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
7OV03QG267 (Nickel); EC 1.11.1.- (Peroxidases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170730
[St] Status:MEDLINE


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[PMID]:28696677
[Au] Autor:Nakano K; Tanabe J; Ishimatsu R; Imato T
[Ad] Endereço:Department of Applied Chemistry, Faculty of Engineering, Kyushu University , 744 Motooka, Nishi-ku, Fukuoka, Japan.
[Ti] Título:Monolithic Peptide-Nucleic Acid Hybrid Functioning as an Artificial Microperoxidase.
[So] Source:Bioconjug Chem;28(8):2031-2034, 2017 Aug 16.
[Is] ISSN:1520-4812
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A new peptide nucleic acid (PNA) with an installed peroxidase function has been developed. Fmoc solid phase peptide synthesis prepared a PNA hybrid (VQKCAQCHTVE-(C H O) CH -[PNA(T)] -G) that renders the microperoxidase backbone, followed by reconstitution with hemin. The resulting holocompound catalyzed the oxidation of 3,3',5,5'-tetramthylbenzidine by H O to 50% that of natural microperoxidase-11, whereas the apo-form and hemin gave no responses. The peroxidase domain was found to be active toward direct electrochemistry and the PNA hybrid served for gene sensor; in the presence of the target DNA (5'-CATGTATAAAAAA-3'), an electrode-attached DNA probe (5'-TsTsTsTsTsTCTCATACATG-3') showed the ferric-to-ferrous quasi-reversible wave (-276 mV vs Ag/AgCl) through sandwich hybridization. Moreover, the hybridization product could accept H O as an oxidant to enhance the reduction current, which occurred likely based on the iron(II)-center-recycling with specific rate constant of 0.19 s .
[Mh] Termos MeSH primário: Materiais Biomiméticos/química
Materiais Biomiméticos/metabolismo
Ácidos Nucleicos Peptídicos/química
Ácidos Nucleicos Peptídicos/metabolismo
Peroxidases/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Modelos Moleculares
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Nucleic Acids); EC 1.11.1.- (Peroxidases); EC 1.11.1.- (microperoxidase)
[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:170712
[St] Status:MEDLINE
[do] DOI:10.1021/acs.bioconjchem.7b00216


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[PMID]:28645608
[Au] Autor:Ge L; Zhang G; You B; Cheng G; Chen L; Shi R
[Ad] Endereço:Department of Cardiovascular Medicine, Xiangya Hospital, Central South University, Changsha 410008, China; Department of Cardiovascular Medicine, The First People's Hospital of Changde City, Changde 415000, Hunan, China.
[Ti] Título:The role of losartan in preventing vascular remodeling in spontaneously hypertensive rats by inhibition of the H O /VPO1/HOCl/MMPs pathway.
[So] Source:Biochem Biophys Res Commun;493(1):855-861, 2017 Nov 04.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Vascular peroxidase 1 (VPO1) has been proved to be associated with vascular endothelial cell apoptosis by producing reactive oxygen species. However, the contribution of VPO1 to the development of vascular remodeling (VR) remains to be fully characterized. We explored the role of VPO1 in VR in spontaneously hypertensive rats (SHRs) and the underlying mechanism of losartan in inhibiting VR. Compared to Wistar-Kyoto (WKY) rats, the SHR showed remodeling of their vascular walls. The level of VPO1 and the hydrogen peroxide (H O ) concentration were increased in the SHRs. However, the SHRs pretreated with losartan showed significant inhibition of blood pressure and VR and decreased levels of VPO1 and H O compared to the non-treated SHRs. Angiotensin II significantly increased the expressions of MMP-2, MMP-9 and the concentrations of H O and hypochlorous acid (HOCl) in vascular smooth muscle cells (VSMCs). However, only the H O level increased in VSMCs when transfected with VPO1 shRNA. These results support a critical but previously unrecognized role of VPO1 in VR and suggest that therapies to reduce VPO1 may be novel approaches for VR.
[Mh] Termos MeSH primário: Peróxido de Hidrogênio/metabolismo
Hipertensão/prevenção & controle
Hipertensão/fisiopatologia
Losartan/administração & dosagem
Metaloproteinases da Matriz/metabolismo
Peroxidases/metabolismo
Remodelação Vascular/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Anti-Hipertensivos/administração & dosagem
Relação Dose-Resposta a Droga
Feminino
Ácido Hipocloroso/metabolismo
Masculino
Ratos
Ratos Endogâmicos SHR
Ratos Endogâmicos WKY
Transdução de Sinais/efeitos dos fármacos
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antihypertensive Agents); 712K4CDC10 (Hypochlorous Acid); BBX060AN9V (Hydrogen Peroxide); EC 1.11.1.- (Peroxidases); EC 1.11.1.- (VPO1 protein, human); EC 3.4.24.- (Matrix Metalloproteinases); JMS50MPO89 (Losartan)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170625
[St] Status:MEDLINE



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