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[PMID]:29028835
[Au] Autor:Mullen NJ; Price DH
[Ad] Endereço:Department of Biochemistry, University of Iowa, Iowa City, Iowa, United States of America.
[Ti] Título:Hydrogen peroxide yields mechanistic insights into human mRNA capping enzyme function.
[So] Source:PLoS One;12(10):e0186423, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Capping of nascent RNA polymerase II (Pol II) transcripts is required for gene expression and the first two steps are catalyzed by separate 5' triphosphatase and guanylyltransferase activities of the human capping enzyme (HCE). The cap is added co-transcriptionally, but how the two activities are coordinated is unclear. Our previous in vitro work has suggested that an unidentified factor modulates the minimum length at which nascent transcripts can be capped. Using the same well-established in vitro system with hydrogen peroxide as a capping inhibitor, we show that this unidentified factor targets the guanylyltransferase activity of HCE. We also uncover the mechanism of HCE inhibition by hydrogen peroxide, and by using mass spectrometry demonstrate that the active site cysteine residue of the HCE triphosphatase domain becomes oxidized. Using recombinant proteins for the two separated HCE domains, we provide evidence that the triphosphatase normally acts on transcripts shorter than can be acted upon by the guanylyltransferase. Our further characterization of the capping reaction dependence on transcript length and its interaction with the unidentified modulator of capping raises the interesting possibility that the capping reaction could be regulated.
[Mh] Termos MeSH primário: Peróxido de Hidrogênio/farmacologia
Nucleosídeo-Trifosfatase/metabolismo
Nucleotidiltransferases/metabolismo
Capuzes de RNA/metabolismo
[Mh] Termos MeSH secundário: Sequência de Bases
Biocatálise
Inibidores Enzimáticos/farmacologia
Seres Humanos
Modelos Moleculares
Nucleosídeo-Trifosfatase/antagonistas & inibidores
Nucleosídeo-Trifosfatase/química
Nucleotidiltransferases/antagonistas & inibidores
Nucleotidiltransferases/química
Domínios Proteicos
Capuzes de RNA/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (RNA Caps); BBX060AN9V (Hydrogen Peroxide); EC 2.7.7.- (Nucleotidyltransferases); EC 2.7.7.- (guanylyltransferase); EC 3.6.1.15 (Nucleoside-Triphosphatase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171014
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186423


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[PMID]:28890337
[Au] Autor:Ghalei H; Trepreau J; Collins JC; Bhaskaran H; Strunk BS; Karbstein K
[Ad] Endereço:Department of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, FL 33458, USA.
[Ti] Título:The ATPase Fap7 Tests the Ability to Carry Out Translocation-like Conformational Changes and Releases Dim1 during 40S Ribosome Maturation.
[So] Source:Mol Cell;67(6):990-1000.e3, 2017 Sep 21.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Late in their maturation, nascent small (40S) ribosomal subunits bind 60S subunits to produce 80S-like ribosomes. Because of the analogy of this translation-like cycle to actual translation, and because 80S-like ribosomes do not produce any protein, it has been suggested that this represents a quality control mechanism for subunit functionality. Here we use genetic and biochemical experiments to show that the essential ATPase Fap7 promotes formation of the rotated state, a key intermediate in translocation, thereby releasing the essential assembly factor Dim1 from pre-40S subunits. Bypassing this quality control step produces defects in reading frame maintenance. These results show how progress in the maturation cascade is linked to a test for a key functionality of 40S ribosomes: their ability to translocate the mRNAâ‹…tRNA pair. Furthermore, our data demonstrate for the first time that the translation-like cycle is a quality control mechanism that ensures the fidelity of the cellular ribosome pool.
[Mh] Termos MeSH primário: Adenilato Quinase/metabolismo
Mudança da Fase de Leitura do Gene Ribossômico
Metiltransferases/metabolismo
Proteínas Nucleares/metabolismo
Nucleosídeo-Trifosfatase/metabolismo
Subunidades Ribossômicas Menores de Eucariotos/enzimologia
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/enzimologia
[Mh] Termos MeSH secundário: Adenilato Quinase/química
Adenilato Quinase/genética
Genótipo
Metiltransferases/química
Metiltransferases/genética
Modelos Moleculares
Proteínas Nucleares/química
Proteínas Nucleares/genética
Nucleosídeo-Trifosfatase/química
Nucleosídeo-Trifosfatase/genética
Fenótipo
Ligação Proteica
Conformação Proteica
Proteólise
Subunidades Ribossômicas Menores de Eucariotos/química
Subunidades Ribossômicas Menores de Eucariotos/genética
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
Relação Estrutura-Atividade
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nuclear Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 2.1.1.- (DIM1 protein, S cerevisiae); EC 2.1.1.- (Methyltransferases); EC 2.7.4.3 (Adenylate Kinase); EC 2.7.4.3 (FAP7 protein, S cerevisiae); EC 3.6.1.15 (Nucleoside-Triphosphatase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170912
[St] Status:MEDLINE


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[PMID]:28547747
[Au] Autor:Bhagavat R; Srinivasan N; Chandra N
[Ad] Endereço:Department of Biochemistry, Molecular Biophysics Unit, National Mathematics Initiative, Indian Institute of Science, Bangalore, 560012, Karnataka, India.
[Ti] Título:Deciphering common recognition principles of nucleoside mono/di and tri-phosphates binding in diverse proteins via structural matching of their binding sites.
[So] Source:Proteins;85(9):1699-1712, 2017 Sep.
[Is] ISSN:1097-0134
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nucleoside triphosphate (NTP) ligands are of high biological importance and are essential for all life forms. A pre-requisite for them to participate in diverse biochemical processes is their recognition by diverse proteins. It is thus of great interest to understand the basis for such recognition in different proteins. Towards this, we have used a structural bioinformatics approach and analyze structures of 4677 NTP complexes available in Protein Data Bank (PDB). Binding sites were extracted and compared exhaustively using PocketMatch, a sensitive in-house site comparison algorithm, which resulted in grouping the entire dataset into 27 site-types. Each of these site-types represent a structural motif comprised of two or more residue conservations, derived using another in-house tool for superposing binding sites, PocketAlign. The 27 site-types could be grouped further into 9 super-types by considering partial similarities in the sites, which indicated that the individual site-types comprise different combinations of one or more site features. A scan across PDB using the 27 structural motifs determined the motifs to be specific to NTP binding sites, and a computational alanine mutagenesis indicated that residues identified to be highly conserved in the motifs are also most contributing to binding. Alternate orientations of the ligand in several site-types were observed and rationalized, indicating the possibility of some residues serving as anchors for NTP recognition. The presence of multiple site-types and the grouping of multiple folds into each site-type is strongly suggestive of convergent evolution. Knowledge of determinants obtained from this study will be useful for detecting function in unknown proteins. Proteins 2017; 85:1699-1712. © 2017 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Nucleosídeo-Trifosfatase/química
Nucleotídeos/química
Proteínas/química
[Mh] Termos MeSH secundário: Algoritmos
Sítios de Ligação
Biologia Computacional
Bases de Dados de Proteínas
Ligantes
Fosfatos/química
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ligands); 0 (Nucleotides); 0 (Phosphates); 0 (Proteins); EC 3.6.1.15 (Nucleoside-Triphosphatase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170527
[St] Status:MEDLINE
[do] DOI:10.1002/prot.25328


  4 / 472 MEDLINE  
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[PMID]:28423339
[Au] Autor:Abe T; Lee A; Sitharam R; Kesner J; Rabadan R; Shapira SD
[Ad] Endereço:Department of Systems Biology, Columbia University, New York, NY 10032, USA; Department of Microbiology and Immunology, Columbia University, New York, NY 10032, USA.
[Ti] Título:Germ-Cell-Specific Inflammasome Component NLRP14 Negatively Regulates Cytosolic Nucleic Acid Sensing to Promote Fertilization.
[So] Source:Immunity;46(4):621-634, 2017 Apr 18.
[Is] ISSN:1097-4180
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cytosolic sensing of nucleic acids initiates tightly regulated programs to limit infection. Oocyte fertilization represents a scenario wherein inappropriate responses to exogenous yet non-pathogen-derived nucleic acids would have negative consequences. We hypothesized that germ cells express negative regulators of nucleic acid sensing (NAS) in steady state and applied an integrated data-mining and functional genomics approach to identify a rheostat of DNA and RNA sensing-the inflammasome component NLRP14. We demonstrated that NLRP14 interacted physically with the nucleic acid sensing pathway and targeted TBK1 (TANK binding kinase 1) for ubiquitination and degradation. We further mapped domains in NLRP14 and TBK1 that mediated the inhibitory function. Finally, we identified a human nonsense germline variant associated with male sterility that results in loss of NLRP14 function and hyper-responsiveness to nucleic acids. The discovery points to a mechanism of nucleic acid sensing regulation that may be of particular importance in fertilization.
[Mh] Termos MeSH primário: Fertilização/imunologia
Células Germinativas/imunologia
Inflamassomos/imunologia
Ácidos Nucleicos/imunologia
Nucleosídeo-Trifosfatase/imunologia
[Mh] Termos MeSH secundário: Células A549
Animais
Cercopithecus aethiops
Citosol/imunologia
Citosol/metabolismo
Feminino
Fertilização/genética
Expressão Gênica/imunologia
Células Germinativas/metabolismo
Mutação em Linhagem Germinativa/imunologia
Células HEK293
Seres Humanos
Immunoblotting
Infertilidade Masculina/genética
Infertilidade Masculina/imunologia
Inflamassomos/genética
Inflamassomos/metabolismo
Masculino
Ácidos Nucleicos/metabolismo
Nucleosídeo-Trifosfatase/genética
Nucleosídeo-Trifosfatase/metabolismo
Ligação Proteica/imunologia
Proteínas Serina-Treonina Quinases/genética
Proteínas Serina-Treonina Quinases/imunologia
Proteínas Serina-Treonina Quinases/metabolismo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Transdução de Sinais/genética
Transdução de Sinais/imunologia
Células Vero
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Inflammasomes); 0 (Nucleic Acids); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (TBK1 protein, human); EC 3.6.1.15 (NLRP14 protein, human); EC 3.6.1.15 (Nucleoside-Triphosphatase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE


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[PMID]:28315769
[Au] Autor:Pang R; Qiu J; Li T; Yang P; Yue L; Pan Y; Zhang W
[Ad] Endereço:State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-sen University, Guangzhou, 510275, China.
[Ti] Título:The regulation of lipid metabolism by a hypothetical P-loop NTPase and its impact on fecundity of the brown planthopper.
[So] Source:Biochim Biophys Acta;1861(7):1750-1758, 2017 07.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Insect fecundity can be regulated by multiple genes in several important signaling pathways which form an extremely complicated regulatory network. However, there are still many genes that have significant impact on insect fecundity but their action mode are still unknown. METHODS: Quantitative real-time PCR (qRT-PCR), immunofluorescence and western blot were used to study the expression profile of Nl23867 in the brown planthopper, Nilaparvata lugens. RNA interference (RNAi), RNA-seq and isobaric tags for relative and absolute quantification (iTRAQ) were performed to investigate the action mode of Nl23867 in the regulation of fecundity. High performance liquid chromatography (HPLC) analysis was performed to detect the fatty acid contents. RESULTS: We show that knockdown of Nl23867, a gene encoding a hypothetical P-loop NTPase, significantly decreased fecundity of N. lugens. Underdeveloped ovaries, fewer eggs laid and reduction in vitellogenin (Vg) protein expression were observed after RNAi knockdown of Nl23867, and most of the affected genes and pathways are fatty acid metabolism-related. We further determined that Nl23867 directly impacts the palmitic acid biosynthesis by regulating the expression of palmitoyl-protein thioesterase (PPT), subsequently affecting the content of total lipids in N. lugens. CONCLUSIONS: Nl23867 regulates the fecundity of N. lugens by modulating the biosynthetic pathway of palmitic acid and affecting lipid metabolism during vitellogenesis and oocyte development. GENERAL SIGNIFICANCE: The presented study pioneers the exploration into how a function-unknown gene takes part in the regulation of fecundity in an insect, and will contribute to the construction of gene regulatory network for insect fecundity.
[Mh] Termos MeSH primário: Hemípteros/fisiologia
Metabolismo dos Lipídeos
Nucleosídeo-Trifosfatase/genética
[Mh] Termos MeSH secundário: Animais
Fertilidade
Redes Reguladoras de Genes
Oócitos/fisiologia
Ácido Palmítico/metabolismo
Vitelogênese
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
2V16EO95H1 (Palmitic Acid); EC 3.6.1.15 (Nucleoside-Triphosphatase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170320
[St] Status:MEDLINE


  6 / 472 MEDLINE  
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[PMID]:28017740
[Au] Autor:Katz FE; Shi X; Owens CP; Joseph S; Tezcan FA
[Ad] Endereço:Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, 92093, United States.
[Ti] Título:Determination of nucleoside triphosphatase activities from measurement of true inorganic phosphate in the presence of labile phosphate compounds.
[So] Source:Anal Biochem;520:62-67, 2017 Mar 01.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:One of the most common assays for nucleoside triphosphatase (NTPase) activity entails the quantification of inorganic phosphate (P ) as a colored phosphomolybdate complex at low pH. While this assay is very sensitive, it is not selective for P in the presence of labile organic phosphate compounds (OPCs). Since NTPase activity assays typically require a large excess of OPCs, such as nucleotides, selectivity for P in the presence of OPCs is often critical in evaluating enzyme activity. Here we present an improved method for the measurement of enzymatic nucleotide hydrolysis as P released, which achieves selectivity for P in the presence of OPCs while also avoiding the costs and hazards inherent in other methods for measuring nucleotide hydrolysis. We apply this method to the measurement of ATP hydrolysis by nitrogenase and GTP hydrolysis by elongation factor G (EF-G) in order to demonstrate the broad applicability of our method for the determination of nucleotide hydrolysis in the presence of interfering OPCs.
[Mh] Termos MeSH primário: Colorimetria
Nucleosídeo-Trifosfatase/metabolismo
Fosfatos/metabolismo
[Mh] Termos MeSH secundário: Hidrólise
Molibdênio/análise
Molibdênio/química
Molibdênio/metabolismo
Fosfatos/análise
Ácidos Fosfóricos/análise
Ácidos Fosfóricos/metabolismo
Fósforo/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phosphates); 0 (Phosphoric Acids); 27YLU75U4W (Phosphorus); 81AH48963U (Molybdenum); EC 3.6.1.15 (Nucleoside-Triphosphatase); I96N991J1N (molybdic acid); RN225F04V1 (phosphomolybdic acid)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161227
[St] Status:MEDLINE


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[PMID]:27940233
[Au] Autor:Zheng L; Hu Y; Hua Q; Luo F; Xie G; Li X; Lin J; Wan Y; Ren S; Pan C; Tan F
[Ad] Endereço:Department of Parasitology, School of Basic Medical Sciences, Wenzhou Medical University, Wenzhou, Zhejiang 325035, PR China; School and Hospital of Stomatology, Wenzhou Medical University, Wenzhou 325027, PR China.
[Ti] Título:Protective immune response in mice induced by a suicidal DNA vaccine encoding NTPase-II gene of Toxoplasma gondii.
[So] Source:Acta Trop;166:336-342, 2017 Feb.
[Is] ISSN:1873-6254
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:DNA-based alphaviral RNA replicon vectors, also called suicidal DNA vectors, have been employed to alleviate biosafety concerns attribution to its ability to induce apoptotic cell death of the transfected cells. Toxoplasma gondii nucleoside triphosphate hydrolase-II (TgNTPase-II), which facilitates the parasite to salvage purines from the host cell for survival and replication, have been demonstrated to be a potential vaccine candidate for toxoplasmosis. Herein, we evaluated the immunogenic potential of a suicidal DNA vaccine encoding TgNTPase-II gene, pDREP-TgNTPase-II, delivered intramuscularly in combination with electroporation. Immunization of mice with pDREP-TgNTPase-II elicited specific humoral responses, with high IgG antibody titers and a mixed IgG1/IgG2a response. The cellular immune response was associated with high level production of IFN-γ, IL-2, IL-10 cytokines and low level IL-4 production as well as the increase of the percentage of CD8+ T cells, indicating that a Th1 predominant response was elicited. Furthermore, mice vaccinated with this suicidal DNA vaccine displayed partial protection against acute infection with the virulent RH strain as well as chronic infection with PRU cyst, which shows 77.7% and 71.4% reduction in brain cyst burden in comparison to PBS and pDREP-eGFP control group, respectively. Based on the cellular and antibody responses, the suicidal DNA vaccine elicited a Th1-predominant immune response against T. gondii challenge.
[Mh] Termos MeSH primário: Nucleosídeo-Trifosfatase/genética
Proteínas de Protozoários/genética
Vacinas Protozoárias/genética
Toxoplasma/imunologia
Toxoplasmose Animal/prevenção & controle
Vacinas de DNA/imunologia
[Mh] Termos MeSH secundário: Animais
Citocinas/metabolismo
Imunidade Celular
Imunoglobulina G/metabolismo
Injeções Intramusculares
Camundongos
Camundongos Endogâmicos BALB C
Vacinas Protozoárias/administração & dosagem
Vacinas Protozoárias/imunologia
Toxoplasma/genética
Toxoplasmose Animal/imunologia
Vacinas de DNA/administração & dosagem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (Immunoglobulin G); 0 (Protozoan Proteins); 0 (Protozoan Vaccines); 0 (Vaccines, DNA); EC 3.6.1.15 (Nucleoside-Triphosphatase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161213
[St] Status:MEDLINE


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[PMID]:27745872
[Au] Autor:Amin N; Belonogova NM; Jovanova O; Brouwer RW; van Rooij JG; van den Hout MC; Svishcheva GR; Kraaij R; Zorkoltseva IV; Kirichenko AV; Hofman A; Uitterlinden AG; van IJcken WF; Tiemeier H; Axenovich TI; van Duijn CM
[Ad] Endereço:Departments of Epidemiology, Erasmus University Medical Center, Rotterdam, the Netherlands. Electronic address: n.amin@erasmusmc.nl.
[Ti] Título:Nonsynonymous Variation in NKPD1 Increases Depressive Symptoms in European Populations.
[So] Source:Biol Psychiatry;81(8):702-707, 2017 Apr 15.
[Is] ISSN:1873-2402
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Despite high heritability, little success was achieved in mapping genetic determinants of depression-related traits by means of genome-wide association studies. METHODS: To identify genes associated with depressive symptomology, we performed a gene-based association analysis of nonsynonymous variation captured using exome-sequencing and exome-chip genotyping in a genetically isolated population from the Netherlands (n = 1999). Finally, we reproduced our significant findings in an independent population-based cohort (n = 1604). RESULTS: We detected significant association of depressive symptoms with a gene NKPD1 (p = 3.7 × 10 ). Nonsynonymous variants in the gene explained 0.9% of sex- and age-adjusted variance of depressive symptoms in the discovery study, which is translated into 3.8% of the total estimated heritability (h = 0.24). Significant association of depressive symptoms with NKPD1 was also observed (n = 1604; p = 1.5 × 10 ) in the independent replication sample despite little overlap with the discovery cohort in the set of nonsynonymous genetic variants observed in the NKPD1 gene. Meta-analysis of the discovery and replication studies improved the association signal (p = 1.0 × 10 ). CONCLUSIONS: Our study suggests that nonsynonymous variation in the gene NKPD1 affects depressive symptoms in the general population. NKPD1 is predicted to be involved in the de novo synthesis of sphingolipids, which have been implicated in the pathogenesis of depression.
[Mh] Termos MeSH primário: Depressão/genética
Transtorno Depressivo Maior/genética
Nucleosídeo-Trifosfatase/genética
[Mh] Termos MeSH secundário: Grupo com Ancestrais do Continente Europeu/genética
Exoma
Feminino
Variação Genética
Estudo de Associação Genômica Ampla
Seres Humanos
Masculino
Proteínas de Membrana/genética
Meia-Idade
Proteínas do Tecido Nervoso/genética
Países Baixos
Polimorfismo de Nucleotídeo Único
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (KIDINS220 protein, human); 0 (Membrane Proteins); 0 (Nerve Tissue Proteins); EC 3.6.1.15 (NKPD1 protein, human); EC 3.6.1.15 (Nucleoside-Triphosphatase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170822
[Lr] Data última revisão:
170822
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161018
[St] Status:MEDLINE


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[PMID]:26879755
[Au] Autor:Baldissarelli J; Santi A; Schmatz R; Abdalla FH; Cardoso AM; Martins CC; Dias GR; Calgaroto NS; Pelinson LP; Reichert KP; Loro VL; Morsch VM; Schetinger MR
[Ad] Endereço:Programa de Pós-Graduação em Ciências Biológicas: Bioquímica Toxicológica, Centro de Ciências Naturais e Exatas, Universidade Federal de Santa Maria, Campus Universitário Camobi, Santa Maria, RS, 97105-900, Brazil. jucimarabaldissarelli@gmail.com.
[Ti] Título:Hypothyroidism Enhanced Ectonucleotidases and Acetylcholinesterase Activities in Rat Synaptosomes can be Prevented by the Naturally Occurring Polyphenol Quercetin.
[So] Source:Cell Mol Neurobiol;37(1):53-63, 2017 Jan.
[Is] ISSN:1573-6830
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Thyroid hormones have an influence on the functioning of the central nervous system. Furthermore, the cholinergic and purinergic systems also are extensively involved in brain function. In this context, quercetin is a polyphenol with antioxidant and neuroprotective properties. This study investigated the effects of (MMI)-induced hypothyroidism on the NTPDase, 5'-nucleotidase, adenosine deaminase (ADA), and acetylcholinesterase (AChE) activities in synaptosomes of rats and whether the quercetin can prevent it. MMI at a concentration of 20 mg/100 mL was administered for 90 days in the drinking water. The animals were divided into six groups: control/water (CT/W), control/quercetin 10 mg/kg, control/quercetin 25 mg/kg, methimazole/water (MMI/W), methimazole/quercetin 10 mg/kg (MMI/Q10), and methimazole/quercetin 25 mg/kg (MMI/Q25). On the 30th day, hormonal dosing was performed to confirm hypothyroidism, and the animals were subsequently treated with 10 or 25 mg/kg quercetin for 60 days. NTPDase activity was not altered in the MMI/W group. However, treatment with quercetin decreased ATP and ADP hydrolysis in the MMI/Q10 and MMI/Q25 groups. 5'-nucleotidase activity increased in the MMI/W group, but treatments with 10 or 25 mg/kg quercetin decreased 5'-nucleotidase activity. ADA activity decreased in the CT/25 and MMI/Q25 groups. Furthermore, AChE activity was reduced in all groups with hypothyroidism. In vitro tests also demonstrated that quercetin per se decreased NTPDase, 5'-nucleotidase, and AChE activities. This study demonstrated changes in the 5'-nucleotidase and AChE activities indicating that purinergic and cholinergic neurotransmission are altered in this condition. In addition, quercetin can alter these parameters and may be a promising natural compound with important neuroprotective actions in hypothyroidism.
[Mh] Termos MeSH primário: 5´-Nucleotidase/metabolismo
Acetilcolinesterase/metabolismo
Hipotireoidismo/enzimologia
Nucleosídeo-Trifosfatase/metabolismo
Quercetina/uso terapêutico
Sinaptossomos/enzimologia
[Mh] Termos MeSH secundário: Animais
Ativação Enzimática/efeitos dos fármacos
Ativação Enzimática/fisiologia
Hipotireoidismo/tratamento farmacológico
Masculino
Polifenóis/farmacologia
Polifenóis/uso terapêutico
Quercetina/farmacologia
Ratos
Ratos Wistar
Sinaptossomos/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polyphenols); 9IKM0I5T1E (Quercetin); EC 3.1.1.7 (Acetylcholinesterase); EC 3.1.3.5 (5'-Nucleotidase); EC 3.6.1.15 (Nucleoside-Triphosphatase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160217
[St] Status:MEDLINE
[do] DOI:10.1007/s10571-016-0342-7


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[PMID]:27329357
[Au] Autor:Pastor-Fernández I; Regidor-Cerrillo J; Álvarez-García G; Marugán-Hernández V; García-Lunar P; Hemphill A; Ortega-Mora LM
[Ad] Endereço:SALUVET, Animal Health Department, Faculty of Veterinary Sciences, Complutense University of Madrid, Ciudad Universitaria s/n, 28040, Madrid, Spain.
[Ti] Título:The tandemly repeated NTPase (NTPDase) from Neospora caninum is a canonical dense granule protein whose RNA expression, protein secretion and phosphorylation coincides with the tachyzoite egress.
[So] Source:Parasit Vectors;9(1):352, 2016 06 21.
[Is] ISSN:1756-3305
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: NTPases (also NTPDases) are enzymes with apyrase activity. They are widely distributed among eukaryotes, and also among members of the family Sarcocystidae. In Toxoplasma gondii, the TgNTPase accumulates in the dense granules, and has been commonly associated with the strain virulence. In the closely related Neospora caninum, the NcNTPase lacks nucleoside diphosphate hydrolase activity and appears to be more abundant in virulent isolates, indicating that it may contribute to the pathogenicity of neosporosis. However, so far no additional information on NcNTPase has been provided. METHODS: Herein, the NcNTPase coding sequences were analysed by different in silico and de novo sequencing approaches. A comparative analysis of NcNTPase and NcGRA7 in terms of protein dynamics, secretion, phosphorylation, and mRNA expression profiles during the tachyzoite lytic cycle was also carried out. Moreover, NcNTPase immunolocalization was analysed by confocal microscopy techniques over a set number of time-points. RESULTS: We describe the presence of three different loci containing three copies of the NcNTPase within the Nc-Liv genome, and report the existence of up to four different NcNTPase alleles in Nc-Liv. We also provide evidence for the occurrence of diverse protein species of the NcNTPase by two-dimensional gel electrophoresis. Both NcNTPase and NcGRA7 were similarly up-regulated and secreted during the egress and/or early invasion phases, and were phosphorylated. However, its secretion was not affected by the addition of calcium modulators such as A23187 and ethanol. NcNTPase and NcGRA7 localized in dense granules and parasitophorous vacuole membrane throughout the lytic cycle, although differed in their inmunolocalization during early invasion and egress. CONCLUSIONS: The present study reveals the complexity of the NcNTPase loci in N. caninum. We hypothesize that the expression of different isoforms of the NcNTPase protein could contribute to parasite virulence. Our findings showed regulation of expression, secretion and phosphorylation of NcNTPase suggesting a potential role for progression through the tachyzoites lytic cycle.
[Mh] Termos MeSH primário: Neospora/enzimologia
Nucleosídeo-Trifosfatase/metabolismo
Transporte Proteico/fisiologia
Proteínas de Protozoários/metabolismo
RNA Mensageiro/metabolismo
RNA de Protozoário/metabolismo
[Mh] Termos MeSH secundário: Cálcio
Regulação Enzimológica da Expressão Gênica
Nucleosídeo-Trifosfatase/genética
Fosforilação
Proteínas de Protozoários/genética
RNA Mensageiro/genética
RNA de Protozoário/genética
Sequências de Repetição em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protozoan Proteins); 0 (RNA, Messenger); 0 (RNA, Protozoan); EC 3.6.1.15 (Nucleoside-Triphosphatase); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170222
[Lr] Data última revisão:
170222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160623
[St] Status:MEDLINE
[do] DOI:10.1186/s13071-016-1620-4



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