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Pesquisa : D08.811.913.400.725 [Categoria DeCS]
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[PMID]:29177276
[Au] Autor:Dallabernardina P; Ruprecht C; Smith PJ; Hahn MG; Urbanowicz BR; Pfrengle F
[Ad] Endereço:Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Am Mühlenberg 1, 14476 Potsdam, Germany. Fabian.Pfrengle@mpikg.mpg.de.
[Ti] Título:Automated glycan assembly of galactosylated xyloglucan oligosaccharides and their recognition by plant cell wall glycan-directed antibodies.
[So] Source:Org Biomol Chem;15(47):9996-10000, 2017 Dec 06.
[Is] ISSN:1477-0539
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We report the automated glycan assembly of oligosaccharides related to the plant cell wall hemicellulosic polysaccharide xyloglucan. The synthesis of galactosylated xyloglucan oligosaccharides was enabled by introducing p-methoxybenzyl (PMB) as a temporary protecting group for automated glycan assembly. The generated oligosaccharides were printed as microarrays, and the binding of a collection of xyloglucan-directed monoclonal antibodies (mAbs) to the oligosaccharides was assessed. We also demonstrated that the printed glycans can be further enzymatically modified while appended to the microarray surface by Arabidopsis thaliana xyloglucan xylosyltransferase 2 (AtXXT2).
[Mh] Termos MeSH primário: Anticorpos Monoclonais/química
Arabidopsis/química
Automação
Parede Celular/química
Oligossacarídeos/síntese química
Polissacarídeos/química
[Mh] Termos MeSH secundário: Arabidopsis/enzimologia
Parede Celular/enzimologia
Análise em Microsséries
Oligossacarídeos/química
Oligossacarídeos/metabolismo
Pentosiltransferases/metabolismo
Polissacarídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Oligosaccharides); 0 (Polysaccharides); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.- (xyloglucan xylosyltransferase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1039/c7ob02605f


  2 / 3447 MEDLINE  
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[PMID]:28748410
[Au] Autor:Komissarov A; Demidyuk I; Safina D; Roschina M; Shubin A; Lunina N; Karaseva M; Kostrov S
[Ad] Endereço:Laboratory of Protein Engineering, Institute of Molecular Genetics, Russian Academy of Science, 2 Kurchatova Sq., Moscow, Russia, 123182.
[Ti] Título:Cytotoxic effect of co-expression of human hepatitis A virus 3C protease and bifunctional suicide protein FCU1 genes in a bicistronic vector.
[So] Source:Mol Biol Rep;44(4):323-332, 2017 Aug.
[Is] ISSN:1573-4978
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Recent reports on various cancer models demonstrate a great potential of cytosine deaminase/5-fluorocytosine suicide system in cancer therapy. However, this approach has limited success and its application to patients has not reached the desirable clinical significance. Accordingly, the improvement of this suicide system is an actively developing trend in gene therapy. The purpose of this study was to explore the cytotoxic effect observed after co-expression of hepatitis A virus 3C protease (3C) and yeast cytosine deaminase/uracil phosphoribosyltransferase fusion protein (FCU1) in a bicistronic vector. A set of mono- and bicistronic plasmid constructs was generated to provide individual or combined expression of 3C and FCU1. The constructs were introduced into HEK293 and HeLa cells, and target protein synthesis as well as the effect of 5-fluorocytosine on cell death and the time course of the cytotoxic effect was studied. The obtained vectors provide for the synthesis of target proteins in human cells. The expression of the genes in a bicistronic construct provide for the cytotoxic effect comparable to that observed after the expression of genes in monocistronic constructs. At the same time, co-expression of FCU1 and 3C recapitulated their cytotoxic effects. The combined effect of the killer and suicide genes was studied for the first time on human cells in vitro. The integration of different gene therapy systems inducing cell death (FCU1 and 3C genes) in a bicistronic construct allowed us to demonstrate that it does not interfere with the cytotoxic effect of each of them. A combination of cytotoxic genes in multicistronic vectors can be used to develop pluripotent gene therapy agents.
[Mh] Termos MeSH primário: Cisteína Endopeptidases/biossíntese
Citosina Desaminase/biossíntese
Flucitosina/farmacologia
Terapia Genética/métodos
Vírus da Hepatite A Humana/enzimologia
Pentosiltransferases/biossíntese
Proteínas Virais/biossíntese
[Mh] Termos MeSH secundário: Cisteína Endopeptidases/genética
Cisteína Endopeptidases/metabolismo
Citosina Desaminase/genética
Citosina Desaminase/metabolismo
Flucitosina/farmacocinética
Genes Transgênicos Suicidas
Vetores Genéticos
Células HEK293
Células HeLa
Vírus da Hepatite A Humana/metabolismo
Seres Humanos
Pentosiltransferases/genética
Pentosiltransferases/metabolismo
Plasmídeos/genética
Pró-Fármacos/farmacocinética
Pró-Fármacos/farmacologia
Transdução Genética
Proteínas Virais/genética
Proteínas Virais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Prodrugs); 0 (Viral Proteins); D83282DT06 (Flucytosine); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.9 (uracil phosphoribosyltransferase); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.28 (3C proteases); EC 3.5.4.1 (Cytosine Deaminase)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171227
[Lr] Data última revisão:
171227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1007/s11033-017-4113-4


  3 / 3447 MEDLINE  
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[PMID]:28921690
[Au] Autor:Nakayama T; Sawai T; Masuda I; Kaneko S; Yamauchi K; Blyth BJ; Shimada Y; Tachibana A; Kakinuma S
[Ad] Endereço:Department of Radiation Effects Research, National Institute of Radiological Sciences, National Institutes for Quantum and Radiological Science and Technology, Inage-ku, Chiba, 263-8555, Japan.
[Ti] Título:Tissue-specific and time-dependent clonal expansion of ENU-induced mutant cells in gpt delta mice.
[So] Source:Environ Mol Mutagen;58(8):592-606, 2017 Oct.
[Is] ISSN:1098-2280
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:DNA mutations play a crucial role in the origins of cancer, and the clonal expansion of mutant cells is one of the fundamental steps in multistage carcinogenesis. In this study, we correlated tumor incidence in B6C3F1 mice during the period after exposure to N-ethyl-N-nitrosourea (ENU) with the persistence of ENU-induced mutant clones in transgenic gpt delta B6C3F1 mice. The induced gpt mutations afforded no selective advantage in the mouse cells and could be distinguished by a mutational spectrum that is characteristic of ENU treatment. The gpt mutations were passengers of the mutant cell of origin and its daughter cells and thus could be used as neutral markers of clones that arose and persisted in the tissues. Female B6C3F1 mice exposed for 1 month to 200 ppm ENU in the drinking water developed early thymic lymphomas and late liver and lung tumors. To assay gpt mutations, we sampled the thymus, liver, lung, and small intestine of female gpt delta mice at 3 days, 4 weeks, and 8 weeks after the end of ENU exposure. Our results reveal that, in all four tissues, the ENU-induced gpt mutations persisted for weeks after the end of mutagen exposure. Clonal expansion of mutant cells was observed in the thymus and small intestine, with the thymus showing larger clone sizes. These results indicate that the clearance of mutant cells and the potential for clonal expansion during normal tissue growth depends on tissue type and that these factors may affect the sensitivity of different tissues to carcinogenesis. Environ. Mol. Mutagen. 58:592-606, 2017. © 2017 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Carcinogênese/genética
Proteínas de Escherichia coli/genética
Etilnitrosoureia/toxicidade
Mutagênicos/toxicidade
Pentosiltransferases/genética
[Mh] Termos MeSH secundário: Animais
Carcinogênese/efeitos dos fármacos
Proteínas de Escherichia coli/biossíntese
Seres Humanos
Intestino Delgado/efeitos dos fármacos
Intestino Delgado/patologia
Fígado/efeitos dos fármacos
Fígado/patologia
Pulmão/efeitos dos fármacos
Pulmão/patologia
Camundongos
Camundongos Transgênicos
Testes de Mutagenicidade/métodos
Mutação/efeitos dos fármacos
Especificidade de Órgãos/efeitos dos fármacos
Pentosiltransferases/biossíntese
Timo/efeitos dos fármacos
Timo/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Mutagens); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.22 (Gpt protein, E coli); P8M1T4190R (Ethylnitrosourea)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170919
[St] Status:MEDLINE
[do] DOI:10.1002/em.22132


  4 / 3447 MEDLINE  
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[PMID]:28813147
[Au] Autor:Spacek P; Keough DT; Chavchich M; Dracínský M; Janeba Z; Naesens L; Edstein MD; Guddat LW; Hocková D
[Ad] Endereço:The Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences , Flemingovo nám. 2, CZ-16610 Prague 6, Czech Republic.
[Ti] Título:Synthesis and Evaluation of Asymmetric Acyclic Nucleoside Bisphosphonates as Inhibitors of Plasmodium falciparum and Human Hypoxanthine-Guanine-(Xanthine) Phosphoribosyltransferase.
[So] Source:J Med Chem;60(17):7539-7554, 2017 Sep 14.
[Is] ISSN:1520-4804
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acyclic nucleoside bisphosphonates (ANbPs) have previously been shown to be good inhibitors of human hypoxanthine-guanine phosphoribosyltransferase (HGPRT) and Plasmodium falciparum (Pf) hypoxanthine-guanine-xanthine phosphoribosyltransferase (PfHGXPRT). On the basis of this scaffold, a new series of ANbPs was synthesized. One of these new ANbPs, [3-(guanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methylphosphonic acid, exhibited K values of 6 and 70 nM for human HGPRT and Pf HGXPRT, respectively. These low K values were achieved by inserting an extra carbon atom in the linker connecting the N atom of guanine to one of the phosphonate groups. The crystal structure of this ANbP in complex with human HGPRT was determined at 2.0 Å resolution and shows that it fills three key pockets in the active site. The most potent phosphoramidate prodrugs of these compounds have IC values in the low micromolar range in Pf lines and low toxicity in human A549 cells, demonstrating that these ANbPs are excellent antimalarial drug leads.
[Mh] Termos MeSH primário: Antimaláricos/química
Antimaláricos/farmacologia
Difosfonatos/química
Difosfonatos/farmacologia
Pentosiltransferases/antagonistas & inibidores
Plasmodium falciparum/efeitos dos fármacos
Plasmodium falciparum/enzimologia
[Mh] Termos MeSH secundário: Seres Humanos
Malária Falciparum/tratamento farmacológico
Malária Falciparum/enzimologia
Simulação de Acoplamento Molecular
Nucleosídeos/química
Nucleosídeos/farmacologia
Pentosiltransferases/metabolismo
Plasmodium falciparum/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antimalarials); 0 (Diphosphonates); 0 (Nucleosides); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.- (hypoxanthine-guanine-xanthine phosphoribosyltransferase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170817
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jmedchem.7b00926


  5 / 3447 MEDLINE  
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[PMID]:28764042
[Au] Autor:Del Arco J; Cejudo-Sanches J; Esteban I; Clemente-Suárez VJ; Hormigo D; Perona A; Fernández-Lucas J
[Ad] Endereço:Applied Biotechnology Group, Universidad Europea de Madrid, Urbanización El Bosque, Calle Tajo, s/n, 28670 Villaviciosa de Odón, Madrid, Spain.
[Ti] Título:Enzymatic production of dietary nucleotides from low-soluble purine bases by an efficient, thermostable and alkali-tolerant biocatalyst.
[So] Source:Food Chem;237:605-611, 2017 Dec 15.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Traditionally, enzymatic synthesis of nucleoside-5'-monophosphates (5'-NMPs) using low water-soluble purine bases has been described as less efficient due to their low solubility in aqueous media. The use of enzymes from extremophiles, such as thermophiles or alkaliphiles, offers the potential to increase solubilisation of these bases by employing high temperatures or alkaline pH. This study describes the cloning, expression and purification of hypoxanthine-guanine-xanthine phosphoribosyltransferase from Thermus thermophilus (TtHGXPRT). Biochemical characterization indicates TtHGXPRT as a homotetramer with excellent activity and stability across a broad range of temperatures (50-90°C) and ionic strengths (0-500mMNaCl), but it also reveals an unusually high activity and stability under alkaline conditions (pH range 8-11). In order to explore the potential of TtHGXPRT as an industrial biocatalyst, enzymatic production of several dietary 5'-NMPs, such as 5'-GMP and 5'-IMP, was carried out at high concentrations of guanine and hypoxanthine.
[Mh] Termos MeSH primário: Nucleotídeos/química
Purinas/química
[Mh] Termos MeSH secundário: Hipoxantina
Pentosiltransferases
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nucleotides); 0 (Purines); 2TN51YD919 (Hypoxanthine); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.- (hypoxanthine-guanine-xanthine phosphoribosyltransferase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE


  6 / 3447 MEDLINE  
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[PMID]:28641402
[Au] Autor:Hida N; Aboukilila MY; Burow DA; Paul R; Greenberg MM; Fazio M; Beasley S; Spitale RC; Cleary MD
[Ad] Endereço:Molecular and Cell Biology Unit, Quantitative and Systems Biology Graduate Program, University of California, Merced, CA 95343, USA.
[Ti] Título:EC-tagging allows cell type-specific RNA analysis.
[So] Source:Nucleic Acids Res;45(15):e138, 2017 Sep 06.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Purification of cell type-specific RNAs remains a significant challenge. One solution involves biosynthetic tagging of target RNAs. RNA tagging via incorporation of 4-thiouracil (TU) in cells expressing transgenic uracil phosphoribosyltransferase (UPRT), a method known as TU-tagging, has been used in multiple systems but can have limited specificity due to endogenous pathways of TU incorporation. Here, we describe an alternative method that requires the activity of two enzymes: cytosine deaminase (CD) and UPRT. We found that the sequential activity of these enzymes converts 5-ethynylcytosine (EC) to 5-ethynyluridine monophosphate that is subsequently incorporated into nascent RNAs. The ethynyl group allows efficient detection and purification of tagged RNAs. We show that 'EC-tagging' occurs in tissue culture cells and Drosophila engineered to express CD and UPRT. Additional control can be achieved through a split-CD approach in which functional CD is reconstituted from independently expressed fragments. We demonstrate the sensitivity and specificity of EC-tagging by obtaining cell type-specific gene expression data from intact Drosophila larvae, including transcriptome measurements from a small population of central brain neurons. EC-tagging provides several advantages over existing techniques and should be broadly useful for investigating the role of differential RNA expression in cell identity, physiology and pathology.
[Mh] Termos MeSH primário: Linhagem da Célula/genética
Citosina/análogos & derivados
RNA/análise
Coloração e Rotulagem/métodos
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Células Cultivadas
Citosina/metabolismo
Citosina/farmacologia
Citosina Desaminase/metabolismo
Drosophila melanogaster
Perfilação da Expressão Gênica/métodos
Células HeLa
Seres Humanos
Especificidade de Órgãos/genética
Pentosiltransferases/metabolismo
RNA/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (5-ethynylcytosine); 63231-63-0 (RNA); 8J337D1HZY (Cytosine); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.9 (uracil phosphoribosyltransferase); EC 3.5.4.1 (Cytosine Deaminase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170624
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx551


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[PMID]:28628279
[Au] Autor:Kaiser MM; Baszczynski O; Hocková D; Postová-Slavetínská L; Dracínský M; Keough DT; Guddat LW; Janeba Z
[Ad] Endereço:The Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nám. 2, 16610, Prague 6, Czech Republic.
[Ti] Título:Acyclic Nucleoside Phosphonates Containing 9-Deazahypoxanthine and a Five-Membered Heterocycle as Selective Inhibitors of Plasmodial 6-Oxopurine Phosphoribosyltransferases.
[So] Source:ChemMedChem;12(14):1133-1141, 2017 Jul 20.
[Is] ISSN:1860-7187
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Acyclic nucleoside phosphonates (ANPs) are an important class of therapeutic drugs that act as antiviral agents by inhibiting viral DNA polymerases and reverse transcriptases. ANPs containing a 6-oxopurine unit instead of a 6-aminopurine or pyrimidine base are inhibitors of the purine salvage enzyme, hypoxanthine-guanine-[xanthine] phosphoribosyltransferase (HG[X]PRT). Such compounds, and their prodrugs, are able to arrest the growth of Plasmodium falciparum (Pf) in cell culture. A new series of ANPs were synthesized and tested as inhibitors of human HGPRT, PfHGXPRT, and Plasmodium vivax (Pv) HGPRT. The novelty of these compounds is that they contain a five-membered heterocycle (imidazoline, imidazole, or triazole) inserted between the acyclic linker(s) and the nucleobase, namely, 9-deazahypoxanthine. Five of the compounds were found to be micromolar inhibitors of PfHGXPRT and PvHGPRT, but no inhibition of human HGPRT was observed under the same assay conditions. This demonstrates selectivity of these types of compounds for the two parasitic enzymes compared to the human counterpart and confirms the importance of the chemical nature of the acyclic moiety in conferring affinity/selectivity for these three enzymes.
[Mh] Termos MeSH primário: Antimaláricos/síntese química
Hipoxantinas/química
Nucleosídeos/síntese química
Organofosfonatos/síntese química
Pentosiltransferases/antagonistas & inibidores
Plasmodium falciparum/enzimologia
Plasmodium vivax/enzimologia
[Mh] Termos MeSH secundário: Antimaláricos/química
Seres Humanos
Hipoxantina Fosforribosiltransferase/antagonistas & inibidores
Modelos Moleculares
Nucleosídeos/química
Organofosfonatos/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (9-deazahypoxanthine); 0 (Antimalarials); 0 (Hypoxanthines); 0 (Nucleosides); 0 (Organophosphonates); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.- (hypoxanthine-guanine-xanthine phosphoribosyltransferase); EC 2.4.2.8 (Hypoxanthine Phosphoribosyltransferase)
[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:170620
[St] Status:MEDLINE
[do] DOI:10.1002/cmdc.201700293


  8 / 3447 MEDLINE  
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[PMID]:28618168
[Au] Autor:Booth WT; Morris TL; Mysona DP; Shah MJ; Taylor LK; Karlin TW; Clary K; Majorek KA; Offermann LR; Chruszcz M
[Ad] Endereço:Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA.
[Ti] Título:Streptococcus pyogenes quinolinate-salvage pathway-structural and functional studies of quinolinate phosphoribosyl transferase and NH -dependent NAD synthetase.
[So] Source:FEBS J;284(15):2425-2441, 2017 Aug.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Streptococcus pyogenes, also known as Group A Strep (GAS), is an obligate human pathogen that is responsible for millions of infections and numerous deaths per year. Infection manifestations can range from simple, acute pharyngitis to more complex, necrotizing fasciitis. To date, most treatments for GAS infections involve the use of common antibiotics including tetracycline and clindamycin. Unfortunately, new strains have been identified that are resistant to these drugs, therefore, new targets must be identified to treat drug-resistant strains. This work is focused on the structural and functional characterization of three proteins: spNadC, spNadD, and spNadE. These enzymes are involved in the biosynthesis of nicotinamide adenine dinucleotide (NAD ). The structures of spNadC and spNadE were determined. SpNadC is suggested to play a role in GAS virulence, while spNadE, functions as an NAD synthetase and is considered to be a new drug target. Determination of the spNadE structure uncovered a putative, NH channel, which may provide insight into the mechanistic details of NH -dependent NAD synthetases in prokaryotes. ENZYMES: Quinolinate phosphoribosyltransferase: EC2.4.2.19 and NAD synthetase: EC6.3.1.5. DATABASE: Protein structures for spNadC, spNadC , and spNadE are deposited into Protein Data Bank under the accession codes 5HUL, 5HUO & 5HUP, and 5HUH & 5HUJ, respectively.
[Mh] Termos MeSH primário: Amida Sintases/metabolismo
Proteínas de Bactérias/metabolismo
Modelos Moleculares
Nicotinamida-Nucleotídeo Adenililtransferase/metabolismo
Pentosiltransferases/metabolismo
Ácido Quinolínico/metabolismo
Streptococcus pyogenes/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/química
Trifosfato de Adenosina/metabolismo
Amida Sintases/química
Amida Sintases/genética
Apoenzimas/química
Apoenzimas/genética
Apoenzimas/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Sítios de Ligação
Domínio Catalítico
Análise por Conglomerados
Biologia Computacional
Cristalografia por Raios X
Dimerização
Deleção de Genes
Nicotinamida-Nucleotídeo Adenililtransferase/química
Nicotinamida-Nucleotídeo Adenililtransferase/genética
Pentosiltransferases/química
Pentosiltransferases/genética
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Estrutura Quaternária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Homologia Estrutural de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apoenzymes); 0 (Bacterial Proteins); 0 (Recombinant Proteins); 8L70Q75FXE (Adenosine Triphosphate); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.19 (nicotinate-nucleotide diphosphorylase (carboxylating)); EC 2.7.7.1 (Nicotinamide-Nucleotide Adenylyltransferase); EC 2.7.7.18 (nicotinic acid mononucleotide adenylyltransferase); EC 6.3.1.- (Amide Synthases); EC 6.3.1.5 (NAD+ synthase); F6F0HK1URN (Quinolinic Acid)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14136


  9 / 3447 MEDLINE  
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[PMID]:28446462
[Au] Autor:Fischereder M; Michalke B; Schmöckel E; Habicht A; Kunisch R; Pavelic I; Szabados B; Schönermarck U; Nelson PJ; Stangl M
[Ad] Endereço:Medizinische Klinik und Poliklinik IV, Renal Division, Klinikum der Ludwig Maximilians Universitaet, Munich, Germany; Michael.fischereder@med.uni-muenchen.de.
[Ti] Título:Sodium storage in human tissues is mediated by glycosaminoglycan expression.
[So] Source:Am J Physiol Renal Physiol;313(2):F319-F325, 2017 Aug 01.
[Is] ISSN:1522-1466
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The current paradigm regarding sodium handling in animals and humans postulates that total body sodium is regulated predominately via regulation of extracellular volume. Active sodium storage independent of volume retention is thought to be negligible. However, studies in animals, hypertensive patients, and healthy humans suggest water-free storage of sodium in skin. We hypothesized that tissue sodium concentrations ([Na] ) found in humans vary and reflect regulation due to variable glycosaminoglycan content due to variable expression of XYLT-1. Twenty seven patients on dialysis and 21 living kidney transplant donors free of clinically detectable edema were studied. During surgery, abdominal skin, muscle, and arteries were biopsied. [Na] was determined by inductively coupled plasma-optical emission spectrometry, semiquantitative glycosaminoglycan content with Alcian stain, and XYLT-1 expression by real-time PCR. [Na] of arteries were ranging between 0.86 and 9.83 g/kg wet wt and were significantly higher in arteries (4.52 ± 1.82 g/kg) than in muscle (2.03 ± 1.41 g/kg; < 0.001) or skin (3.24 ± 2.26 g/kg wet wt; = 0.038). For individual patients [Na] correlated for skin and arterial tissue ( = 0.440, = 0.012). [Na] also correlated significantly with blinded semiquantitative analysis of glycosaminoglycans staining ( = 0.588, = 0.004). In arteries XYLT-1 expression was also correlated with [Na] ( = 0.392, = 0.003). Our data confirm highly variable [Na] in human skin and muscle and extend this observation to [Na] in human arteries. These data support the hypothesis of water-independent sodium storage via regulated glycosaminoglycan synthesis in human tissues, including arteries.
[Mh] Termos MeSH primário: Músculos Abdominais/química
Artérias Epigástricas/química
Glicosaminoglicanos/análise
Nefropatias/metabolismo
Pele/química
Sódio/análise
[Mh] Termos MeSH secundário: Adulto
Idoso
Biópsia
Estudos de Casos e Controles
Linhagem Celular
Feminino
Fibroblastos/enzimologia
Seres Humanos
Nefropatias/diagnóstico
Nefropatias/terapia
Masculino
Meia-Idade
Osmose
Pentosiltransferases/genética
Pentosiltransferases/metabolismo
Diálise Renal
Espectrofotometria/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycosaminoglycans); 9NEZ333N27 (Sodium); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.26 (UDP xylose-protein xylosyltransferase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1152/ajprenal.00703.2016


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[PMID]:28431245
[Au] Autor:Scott TA; Quintaneiro LM; Norvaisas P; Lui PP; Wilson MP; Leung KY; Herrera-Dominguez L; Sudiwala S; Pessia A; Clayton PT; Bryson K; Velagapudi V; Mills PB; Typas A; Greene NDE; Cabreiro F
[Ad] Endereço:Institute of Structural and Molecular Biology, University College London and Birkbeck, London WC1E 6BT, UK.
[Ti] Título:Host-Microbe Co-metabolism Dictates Cancer Drug Efficacy in C. elegans.
[So] Source:Cell;169(3):442-456.e18, 2017 Apr 20.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fluoropyrimidines are the first-line treatment for colorectal cancer, but their efficacy is highly variable between patients. We queried whether gut microbes, a known source of inter-individual variability, impacted drug efficacy. Combining two tractable genetic models, the bacterium E. coli and the nematode C. elegans, we performed three-way high-throughput screens that unraveled the complexity underlying host-microbe-drug interactions. We report that microbes can bolster or suppress the effects of fluoropyrimidines through metabolic drug interconversion involving bacterial vitamin B , B , and ribonucleotide metabolism. Also, disturbances in bacterial deoxynucleotide pools amplify 5-FU-induced autophagy and cell death in host cells, an effect regulated by the nucleoside diphosphate kinase ndk-1. Our data suggest a two-way bacterial mediation of fluoropyrimidine effects on host metabolism, which contributes to drug efficacy. These findings highlight the potential therapeutic power of manipulating intestinal microbiota to ensure host metabolic health and treat disease.
[Mh] Termos MeSH primário: Antineoplásicos/metabolismo
Escherichia coli/metabolismo
Fluoruracila/metabolismo
Microbioma Gastrointestinal
[Mh] Termos MeSH secundário: Animais
Autofagia
Caenorhabditis elegans
Morte Celular
Neoplasias Colorretais/tratamento farmacológico
Dieta
Escherichia coli/enzimologia
Escherichia coli/genética
Seres Humanos
Modelos Animais
Pentosiltransferases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.9 (uracil phosphoribosyltransferase); U3P01618RT (Fluorouracil)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170623
[Lr] Data última revisão:
170623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170422
[St] Status:MEDLINE



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