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  1 / 7997 MEDLINE  
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[PMID]:29402931
[Au] Autor:Bianchi F; Syga L; Moiset G; Spakman D; Schavemaker PE; Punter CM; Seinen AB; van Oijen AM; Robinson A; Poolman B
[Ad] Endereço:Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9700AB, Groningen, The Netherlands.
[Ti] Título:Steric exclusion and protein conformation determine the localization of plasma membrane transporters.
[So] Source:Nat Commun;9(1):501, 2018 02 05.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The plasma membrane (PM) of Saccharomyces cerevisiae contains membrane compartments, MCC/eisosomes and MCPs, named after the protein residents Can1 and Pma1, respectively. Using high-resolution fluorescence microscopy techniques we show that Can1 and the homologous transporter Lyp1 are able to diffuse into the MCC/eisosomes, where a limited number of proteins are conditionally trapped at the (outer) edge of the compartment. Upon addition of substrate, the immobilized proteins diffuse away from the MCC/eisosomes, presumably after taking a different conformation in the substrate-bound state. Our data indicate that the mobile fraction of all integral plasma membrane proteins tested shows extremely slow Brownian diffusion through most of the PM. We also show that proteins with large cytoplasmic domains, such as Pma1 and synthetic chimera of Can1 and Lyp1, are excluded from the MCC/eisosomes. We hypothesize that the distinct localization patterns found for these integral membrane proteins in S. cerevisiae arises from a combination of slow lateral diffusion, steric exclusion, and conditional trapping in membrane compartments.
[Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos Básicos/química
Membrana Celular/metabolismo
ATPases Translocadoras de Prótons/química
Proteínas de Saccharomyces cerevisiae/química
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Sistemas de Transporte de Aminoácidos Básicos/metabolismo
Membrana Celular/ultraestrutura
Difusão
Recuperação de Fluorescência Após Fotodegradação
Cinética
Microdomínios da Membrana
Conformação Proteica
Transporte Proteico
ATPases Translocadoras de Prótons/metabolismo
Saccharomyces cerevisiae/ultraestrutura
Proteínas de Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acid Transport Systems, Basic); 0 (CAN1 protein, S cerevisiae); 0 (LYP1 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); EC 3.6.1.- (PMA1 protein, S cerevisiae); EC 3.6.3.14 (Proton-Translocating ATPases)
[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:180207
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-018-02864-2


  2 / 7997 MEDLINE  
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[PMID]:29292807
[Au] Autor:Tamiya Y; Watanabe R; Noji H; Li CB; Komatsuzaki T
[Ad] Endereço:Department of Mathematics, Hokkaido University, Sapporo 001-0020, Japan.
[Ti] Título:Effects of non-equilibrium angle fluctuation on F -ATPase kinetics induced by temperature increase.
[So] Source:Phys Chem Chem Phys;20(3):1872-1880, 2018 Jan 17.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:F -ATPase (F ) is an efficient rotary protein motor, whose reactivity is modulated by the rotary angle to utilize thermal fluctuation. In order to elucidate how its kinetics are affected by the change in the fluctuation, we have extended the reaction-diffusion formalism [R. Watanabe et al., Biophys. J., 2013, 105, 2385] applicable to a wider range of temperatures based on experimental data analysis of F derived from thermophilic Bacillus under high ATP concentration conditions. Our simulation shows that the rotary angle distribution manifests a stronger non-equilibrium feature as the temperature increases, because ATP hydrolysis and P release are more accelerated compared with the timescale of rotary angle relaxation. This effect causes the rate coefficient obtained from dwell time fitting to deviate from the Arrhenius relation in P release, which has been assumed in the previous activation thermodynamic quantities estimation using linear Arrhenius fitting. Larger negative correlation is also found between hydrolysis and P release waiting time in a catalytic dwell with the increase in temperature. This loss of independence between the two successive reactions at the catalytic dwell sheds doubt on the conventional dwell time fitting to obtain rate coefficients with a double exponential function at temperatures higher than 65 °C, which is close to the physiological temperature of the thermophilic Bacillus.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
ATPases Translocadoras de Prótons/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/química
Trifosfato de Adenosina/metabolismo
Bacillus/enzimologia
Proteínas de Bactérias/química
Biocatálise
Hidrólise
Cinética
ATPases Translocadoras de Prótons/química
Temperatura Ambiente
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.3.14 (Proton-Translocating ATPases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp06256g


  3 / 7997 MEDLINE  
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[PMID]:28843171
[Au] Autor:Gao J; Zhang T; Kang Z; Ting W; Xu L; Yin D
[Ad] Endereço:Department of Basic Medical Research, The Sixth Affiliated Hospital of Guangzhou Medical University, 511518, Guangdong, PR China. Electronic address: gaojun@gzhmu.edu.cn.
[Ti] Título:The F0F1 ATP synthase regulates human neutrophil migration through cytoplasmic proton extrusion coupled with ATP generation.
[So] Source:Mol Immunol;90:219-226, 2017 Oct.
[Is] ISSN:1872-9142
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cytoplasmic alkalinization and extracellular adenosine triphosphate (ATP) signals are required for migration of chemokineactivated neutrophils, but the precise functions remain unclear. In this work, the effect of the plasma membrane-expressed F0F1-ATP synthase (FATPase) on human neutrophils was examined. We found F-ATPase to be involved in cytoplasm proton extrusion and extracellular ATP generation. Oligomycin A, an F-ATPase inhibitor that blocks proton transfer, inhibited cytoplasmic alkalinization, extracellular ATP generation, adhesion and chemotaxis in N-formyl-Met-Leu-Phe (fMLP)-stimulated neutrophils; however, adenosine diphosphate (ADP), a substrate and activator of F-ATPase, had the opposite effect. Further analysis revealed that cell surface F-ATPase can translocate to the leading edge of directional fMLP-stimulated neutrophils toward ADP hydrolyzed from pannexin 1 channel-released ATP, followed by F-ATPase-catalyzed ATP regeneration using ADP and protons transferred from the cytoplasm. Therefore, the membrane-expressed F-ATPase regulates human neutrophil migration via cytoplasm proton extrusion and extracellular ATP generation.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/biossíntese
Quimiotaxia de Leucócito/fisiologia
Neutrófilos/fisiologia
ATPases Translocadoras de Prótons/metabolismo
[Mh] Termos MeSH secundário: Difosfato de Adenosina/farmacologia
Adulto
Adesão Celular/efeitos dos fármacos
Adesão Celular/fisiologia
Células Cultivadas
Quimiotaxia de Leucócito/efeitos dos fármacos
Conexinas/metabolismo
Seres Humanos
Potencial da Membrana Mitocondrial/fisiologia
N-Formilmetionina Leucil-Fenilalanina/farmacologia
Proteínas do Tecido Nervoso/metabolismo
Oligomicinas/farmacologia
ATPases Translocadoras de Prótons/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Connexins); 0 (Nerve Tissue Proteins); 0 (Oligomycins); 0 (PANX1 protein, human); 05HQS4AI99 (oligomycin A); 59880-97-6 (N-Formylmethionine Leucyl-Phenylalanine); 61D2G4IYVH (Adenosine Diphosphate); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.3.14 (Proton-Translocating ATPases)
[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:170827
[St] Status:MEDLINE


  4 / 7997 MEDLINE  
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[PMID]:28842481
[Au] Autor:Yanagisawa S; Frasch WD
[Ad] Endereço:From the School of Life Sciences, Arizona State University, Tempe, Arizona, 85287-4501.
[Ti] Título:Protonation-dependent stepped rotation of the F-type ATP synthase c-ring observed by single-molecule measurements.
[So] Source:J Biol Chem;292(41):17093-17100, 2017 Oct 13.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The two opposed rotary molecular motors of the F F -ATP synthase work together to provide the majority of ATP in biological organisms. Rotation occurs in 120° power strokes separated by dwells when F synthesizes or hydrolyzes ATP. F and F complexes connect via a central rotor stalk and a peripheral stator stalk. A major unresolved question is the mechanism in which the interaction between subunit-a and rotating subunit-c-ring in the F motor uses the flux of H across the membrane to induce clockwise rotation against the force of counterclockwise rotation driven by the F -ATPase. In single-molecule measurements of F F embedded in lipid bilayer nanodiscs, we observed that the ability of the F motor to form transient dwells increases with decreasing pH. Transient dwells can halt counterclockwise rotation powered by the F -ATPase in steps equivalent to the rotation of single c-subunits in the c-ring of F , and can push the common axle shared by the two motors clockwise by as much as one c-subunit. Because the F proton half-channels that access the periplasm and the cytoplasm are exposed to the same pH, these data are consistent with the conclusion that the periplasmic half-channel is more easily protonated in a manner that halts ATPase-driven rotation by blocking ATPase-dependent proton pumping. The fit of transient dwell occurrence to the sum of three Gaussian curves suggests that the asymmetry of the three ATPase-dependent 120° power strokes imposed by the relative positions of the central and peripheral stalks affects c-subunit stepping efficiency.
[Mh] Termos MeSH primário: Citoplasma/enzimologia
Escherichia coli/enzimologia
Movimento (Física)
Periplasma/enzimologia
ATPases Translocadoras de Prótons/química
[Mh] Termos MeSH secundário: Proteínas de Escherichia coli
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); EC 3.6.3.14 (Proton-Translocating ATPases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170827
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.799940


  5 / 7997 MEDLINE  
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[PMID]:28829771
[Au] Autor:Villa-Pulgarín JA; Gajate C; Botet J; Jimenez A; Justies N; Varela-M RE; Cuesta-Marbán Á; Müller I; Modolell M; Revuelta JL; Mollinedo F
[Ad] Endereço:Instituto de Biología Molecular y Celular del Cáncer, Centro de Investigación del Cáncer, Consejo Superior de Investigaciones Científicas (CSIC)-Universidad de Salamanca, Campus Miguel de Unamuno, Salamanca, Spain.
[Ti] Título:Mitochondria and lipid raft-located FOF1-ATP synthase as major therapeutic targets in the antileishmanial and anticancer activities of ether lipid edelfosine.
[So] Source:PLoS Negl Trop Dis;11(8):e0005805, 2017 Aug.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Leishmaniasis is the world's second deadliest parasitic disease after malaria, and current treatment of the different forms of this disease is far from satisfactory. Alkylphospholipid analogs (APLs) are a family of anticancer drugs that show antileishmanial activity, including the first oral drug (miltefosine) for leishmaniasis and drugs in preclinical/clinical oncology trials, but their precise mechanism of action remains to be elucidated. METHODOLOGY/PRINCIPAL FINDINGS: Here we show that the tumor cell apoptosis-inducer edelfosine was the most effective APL, as compared to miltefosine, perifosine and erucylphosphocholine, in killing Leishmania spp. promastigotes and amastigotes as well as tumor cells, as assessed by DNA breakdown determined by flow cytometry. In studies using animal models, we found that orally-administered edelfosine showed a potent in vivo antileishmanial activity and diminished macrophage pro-inflammatory responses. Edelfosine was also able to kill Leishmania axenic amastigotes. Edelfosine was taken up by host macrophages and killed intracellular Leishmania amastigotes in infected macrophages. Edelfosine accumulated in tumor cell mitochondria and Leishmania kinetoplast-mitochondrion, and led to mitochondrial transmembrane potential disruption, and to the successive breakdown of parasite mitochondrial and nuclear DNA. Ectopic expression of Bcl-XL inhibited edelfosine-induced cell death in both Leishmania parasites and tumor cells. We found that the cytotoxic activity of edelfosine against Leishmania parasites and tumor cells was associated with a dramatic recruitment of FOF1-ATP synthase into lipid rafts following edelfosine treatment in both parasites and cancer cells. Raft disruption and specific FOF1-ATP synthase inhibition hindered edelfosine-induced cell death in both Leishmania parasites and tumor cells. Genetic deletion of FOF1-ATP synthase led to edelfosine drug resistance in Saccharomyces cerevisiae yeast. CONCLUSIONS/SIGNIFICANCE: The present study shows that the antileishmanial and anticancer actions of edelfosine share some common signaling processes, with mitochondria and raft-located FOF1-ATP synthase being critical in the killing process, thus identifying novel druggable targets for the treatment of leishmaniasis.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Antiprotozoários/farmacologia
Leishmania/efeitos dos fármacos
Microdomínios da Membrana/enzimologia
Mitocôndrias/enzimologia
Éteres Fosfolipídicos/farmacologia
ATPases Translocadoras de Prótons/antagonistas & inibidores
[Mh] Termos MeSH secundário: Animais
Sobrevivência Celular/efeitos dos fármacos
Células Cultivadas
Modelos Animais de Doenças
Deleção de Genes
Seres Humanos
Leishmaniose/tratamento farmacológico
Macrófagos/efeitos dos fármacos
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Camundongos
Mitocôndrias/efeitos dos fármacos
Mitocôndrias/fisiologia
Saccharomyces cerevisiae/efeitos dos fármacos
Saccharomyces cerevisiae/enzimologia
Saccharomyces cerevisiae/genética
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Antiprotozoal Agents); 0 (Phospholipid Ethers); 1Y6SNA8L5S (edelfosine); EC 3.6.3.14 (Proton-Translocating ATPases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170910
[Lr] Data última revisão:
170910
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170823
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0005805


  6 / 7997 MEDLINE  
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[PMID]:28763437
[Au] Autor:Brion C; Legrand S; Peter J; Caradec C; Pflieger D; Hou J; Friedrich A; Llorente B; Schacherer J
[Ad] Endereço:Université de Strasbourg, CNRS, GMGM UMR 7156, Strasbourg, France.
[Ti] Título:Variation of the meiotic recombination landscape and properties over a broad evolutionary distance in yeasts.
[So] Source:PLoS Genet;13(8):e1006917, 2017 Aug.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Meiotic recombination is a major factor of genome evolution, deeply characterized in only a few model species, notably the yeast Saccharomyces cerevisiae. Consequently, little is known about variations of its properties across species. In this respect, we explored the recombination landscape of Lachancea kluyveri, a protoploid yeast species that diverged from the Saccharomyces genus more than 100 million years ago and we found striking differences with S. cerevisiae. These variations include a lower recombination rate, a higher frequency of chromosomes segregating without any crossover and the absence of recombination on the chromosome arm containing the sex locus. In addition, although well conserved within the Saccharomyces clade, the S. cerevisiae recombination hotspots are not conserved over a broader evolutionary distance. Finally and strikingly, we found evidence of frequent reversal of commitment to meiosis, resulting in return to mitotic growth after allele shuffling. Identification of this major but underestimated evolutionary phenomenon illustrates the relevance of exploring non-model species.
[Mh] Termos MeSH primário: Genoma Fúngico
Recombinação Homóloga
Meiose/genética
Saccharomyces cerevisiae/genética
Saccharomycetales/genética
[Mh] Termos MeSH secundário: Cromossomos Fúngicos/genética
DNA Fúngico/genética
Evolução Molecular
Mitose/genética
Filogenia
ATPases Translocadoras de Prótons/genética
ATPases Translocadoras de Prótons/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomycetales/classificação
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Fungal); 0 (Saccharomyces cerevisiae Proteins); EC 3.6.3.14 (Proton-Translocating ATPases); EC 3.6.3.14 (VMA1 protein, S cerevisiae)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170802
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006917


  7 / 7997 MEDLINE  
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[PMID]:28681139
[Au] Autor:Yu Y; Duan X; Ding X; Chen C; Zhu D; Yin K; Cao L; Song X; Zhu P; Li Q; Nisa ZU; Yu J; Du J; Song Y; Li H; Liu B; Zhu Y
[Ad] Endereço:Key Laboratory of Agricultural Biological Functional Genes, Northeast Agricultural University, Harbin, 150030, China.
[Ti] Título:A novel AP2/ERF family transcription factor from Glycine soja, GsERF71, is a DNA binding protein that positively regulates alkaline stress tolerance in Arabidopsis.
[So] Source:Plant Mol Biol;94(4-5):509-530, 2017 Jul.
[Is] ISSN:1573-5028
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:KEY MESSAGE: Here we first found that GsERF71, an ERF factor from wild soybean could increase plant alkaline stress tolerance by up-regulating H+-ATPase and by modifing the accumulation of Auxin. Alkaline soils are widely distributed all over the world and greatly limit plant growth and development. In our previous transcriptome analyses, we have identified several ERF (ethylene-responsive factor) genes that responded strongly to bicarbonate stress in the roots of wild soybean G07256 (Glycine soja). In this study, we cloned and functionally characterized one of the genes, GsERF71. When expressed in epidermal cells of onion, GsERF71 localized to the nucleus. It can activate the reporters in yeast cells, and the C-terminus of 170 amino acids is essential for its transactivation activity. Yeast one-hybrid and EMSA assays indicated that GsERF71 specifically binds to the cis-acting elements of the GCC-box, suggesting that GsERF71 may participate in the regulation of transcription of the relevant biotic and abiotic stress-related genes. Furthermore, transgenic Arabidopsis plants overexpressing GsERF71 showed significantly higher tolerance to bicarbonate stress generated by NaHCO or KHCO than the wild type (WT) plants, i.e., the transgenic plants had greener leaves, longer roots, higher total chlorophyll contents and lower MDA contents. qRT-PCR and rhizosphere acidification assays indicated that the expression level and activity of H -ATPase (AHA2) were enhanced in the transgenic plants under alkaline stress. Further analysis indicated that the expression of auxin biosynthetic genes and IAA contents were altered to a lower extent in the roots of transgenic plants than WT plants under alkaline stress in a short-term. Together, our data suggest that GsERF71 enhances the tolerance to alkaline stress by up-regulating the expression levels of H -ATPase and by modifying auxin accumulation in transgenic plants.
[Mh] Termos MeSH primário: Arabidopsis/metabolismo
Proteínas de Ligação a DNA/metabolismo
Proteínas de Plantas/metabolismo
Feijão de Soja/metabolismo
Estresse Fisiológico/fisiologia
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
DNA de Plantas/metabolismo
Proteínas de Ligação a DNA/genética
Regulação Enzimológica da Expressão Gênica/fisiologia
Regulação da Expressão Gênica de Plantas/fisiologia
Concentração de Íons de Hidrogênio
Filogenia
Proteínas de Plantas/genética
Plantas Geneticamente Modificadas
ATPases Translocadoras de Prótons/genética
ATPases Translocadoras de Prótons/metabolismo
Feijão de Soja/genética
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Plant); 0 (DNA-Binding Proteins); 0 (Plant Proteins); 0 (Transcription Factors); EC 3.6.3.14 (Proton-Translocating ATPases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170801
[Lr] Data última revisão:
170801
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170707
[St] Status:MEDLINE
[do] DOI:10.1007/s11103-017-0623-7


  8 / 7997 MEDLINE  
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[PMID]:28652018
[Au] Autor:Nesci S; Trombetti F; Ventrella V; Pirini M; Pagliarani A
[Ad] Endereço:Department of Veterinary Medical Sciences (DIMEVET), University of Bologna, via Tolara di Sopra 50, 40064, Ozzano dell'Emilia, BO, Italy.
[Ti] Título:Kinetic properties of the mitochondrial F F -ATPase activity elicited by Ca in replacement of Mg .
[So] Source:Biochimie;140:73-81, 2017 Sep.
[Is] ISSN:1638-6183
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:The mitochondrial F-ATPase can be activated either by the classical cofactor Mg or, with lower efficiency, by Ca . The latter may play a role when calcium concentration rises in mitochondria, a condition associated with cascade events leading to cell death. Common and distinctive features of these differently activated mitochondrial ATPases were pointed out in swine heart mitochondria. When Ca replaces the natural cofactor Mg , the enzyme responsiveness to the transmembrane electrochemical gradient and to the classical F-ATPase inhibitors DCCD and oligomycin as well as the oligomycin sensitivity loss by thiol oxidation, are maintained. Consistently, the two mitochondrial ATPases apparently share the F F complex basic structure and mechanism. Peculiar cation-dependent properties, which may affect the F catalytic mechanism and/or the F proton binding site features, may be linked to a different physiological role of the mitochondrial Ca-activated F-ATPase with respect to the Mg-activated F-ATPase.
[Mh] Termos MeSH primário: Cálcio/farmacocinética
Magnésio/farmacologia
Mitocôndrias Cardíacas/enzimologia
ATPases Translocadoras de Prótons/metabolismo
[Mh] Termos MeSH secundário: Animais
Cálcio/metabolismo
Dicicloexilcarbodi-Imida/farmacologia
Magnésio/metabolismo
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Oligomicinas/farmacologia
ATPases Translocadoras de Prótons/antagonistas & inibidores
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oligomycins); 538-75-0 (Dicyclohexylcarbodiimide); EC 3.6.3.14 (Proton-Translocating ATPases); I38ZP9992A (Magnesium); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170628
[St] Status:MEDLINE


  9 / 7997 MEDLINE  
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[PMID]:28579774
[Au] Autor:Zhang R; Shao M; Han X; Wang C; Li Y; Hu B; Pang D; Xie Z
[Ad] Endereço:Hubei Key Laboratory of Cell Homeostasis.
[Ti] Título:ATP synthesis in the energy metabolism pathway: a new perspective for manipulating CdSe quantum dots biosynthesized in .
[So] Source:Int J Nanomedicine;12:3865-3879, 2017.
[Is] ISSN:1178-2013
[Cp] País de publicação:New Zealand
[La] Idioma:eng
[Ab] Resumo:Due to a growing trend in their biomedical application, biosynthesized nanomaterials are of great interest to researchers nowadays with their biocompatible, low-energy consumption, economic, and tunable characteristics. It is important to understand the mechanism of biosynthesis in order to achieve more efficient applications. Since there are only rare studies on the influences of cellular energy levels on biosynthesis, the influence of energy is often overlooked. Through determination of the intracellular ATP concentrations during the biosynthesis process, significant changes were observed. In addition, ATP synthesis deficiency caused great decreases in quantum dots (QDs) biosynthesis in the Δ , Δ , Δ , and Δ strains. With inductively coupled plasma-atomic emission spectrometry and atomic absorption spectroscopy analyses, it was found that ATP affected the accumulation of the seleno-precursor and helped with the uptake of Cd and the formation of QDs. We successfully enhanced the fluorescence intensity 1.5 or 2 times through genetic modification to increase ATP or SeAM (the seleno analog of -adenosylmethionine, the product that would accumulate when ATP is accrued). This work explains the mechanism for the correlation of the cellular energy level and QDs biosynthesis in living cells, demonstrates control of the biosynthesis using this mechanism, and thus provides a new manipulation strategy for the biosynthesis of other nanomaterials to widen their applications.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Compostos de Cádmio/metabolismo
Pontos Quânticos/metabolismo
Saccharomyces cerevisiae/metabolismo
Compostos de Selênio/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/biossíntese
Cádmio/análise
Cádmio/metabolismo
Metabolismo Energético
Fluorescência
ATPases Translocadoras de Prótons/genética
ATPases Translocadoras de Prótons/metabolismo
Pontos Quânticos/química
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Selênio/análise
Selênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cadmium Compounds); 0 (Saccharomyces cerevisiae Proteins); 0 (Selenium Compounds); 00BH33GNGH (Cadmium); 8L70Q75FXE (Adenosine Triphosphate); A7F646JC5C (cadmium selenide); EC 3.6.3.14 (ATP2 protein, S cerevisiae); EC 3.6.3.14 (Proton-Translocating ATPases); H6241UJ22B (Selenium)
[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:170606
[St] Status:MEDLINE
[do] DOI:10.2147/IJN.S132719


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[PMID]:28578353
[Au] Autor:Castaing-Berthou A; Malet N; Radojkovic C; Cabou C; Gayral S; Martinez LO; Laffargue M
[Ad] Endereço:Institut National de la Santé et de la Recherche Médicale (INSERM), UMR 1048, Institute of Metabolic and Cardiovascular Diseases, Toulouse, France.
[Ti] Título:PI3Kß Plays a Key Role in Apolipoprotein A-I-Induced Endothelial Cell Proliferation Through Activation of the Ecto-F1-ATPase/P2Y1 Receptors.
[So] Source:Cell Physiol Biochem;42(2):579-593, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: High-density lipoproteins (HDL) exert multiple cardioprotective functions on the arterial wall, including the promotion of endothelial cell survival and proliferation. Among mechanism contributing to endothelial protection, it has been reported that apolipoprotein A-I (apoA-I), the major protein in HDL, binds and activates the endothelial ecto-F1-ATPase receptor. This generates extracellular ADP, which in turn promotes endothelial cell survival. In this study we aimed to further investigate the signaling pathway involved downstream of apoA-I-induced ecto-F1-ATPase activation. METHODS: In human umbilical vein endothelial cells (HUVECs), pharmacological and gene silencing approaches were used to study pathways involved downstream ecto-F1-ATPase activation by apoA-I. RESULTS: ApoA-I and HDL both induced Akt phosphorylation. F1-ATPase inhibitors such as inhibitory factor 1 and oligomycin completely blocked apoA-I-induced Akt phosphorylaton and significantly blocked HDL-induced phosphorylation, indicating that this signaling pathway is dependent on ecto-F1-ATPase activation by apoA-I. Further, we were able to specify roles for the P2Y1-ADPreceptor and the PI3Kß isoform in this pathway since pharmacological inhibition and silencing of these proteins dramatically inhibited apoA-I-induced Akt phosphorylation and cell proliferation. CONCLUSION: Altogether, these data highlight a key role of the P2Y1/PI3Kß axis in endothelial cell proliferation downstream of ecto-F1-ATPase activation by apoA-I. Pharmacological targeting of this pathway could represent a promising approach to enhance vascular endothelial protection.
[Mh] Termos MeSH primário: Apolipoproteína A-I/metabolismo
Classe II de Fosfatidilinositol 3-Quinases/genética
Células Endoteliais/metabolismo
ATPases Translocadoras de Prótons/genética
Receptores Purinérgicos P2Y1/genética
[Mh] Termos MeSH secundário: Difosfato de Adenosina/metabolismo
Apolipoproteína A-I/genética
Artérias/metabolismo
Artérias/patologia
Proliferação Celular/genética
Parede Celular/metabolismo
Parede Celular/patologia
Classe II de Fosfatidilinositol 3-Quinases/biossíntese
Células Endoteliais/efeitos dos fármacos
Regulação da Expressão Gênica/genética
Inativação Gênica
Células Endoteliais da Veia Umbilical Humana
Seres Humanos
Lipoproteínas HDL/metabolismo
Proteína Oncogênica v-akt/genética
Proteína Oncogênica v-akt/metabolismo
ATPases Translocadoras de Prótons/biossíntese
Receptores Purinérgicos P2Y1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (APOA1 protein, human); 0 (Apolipoprotein A-I); 0 (Lipoproteins, HDL); 0 (Receptors, Purinergic P2Y1); 61D2G4IYVH (Adenosine Diphosphate); EC 2.7.1.137 (Class II Phosphatidylinositol 3-Kinases); EC 2.7.1.137 (PIK3C2B protein, human); EC 2.7.11.1 (Oncogene Protein v-akt); EC 3.6.3.14 (Proton-Translocating ATPases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170804
[Lr] Data última revisão:
170804
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170605
[St] Status:MEDLINE
[do] DOI:10.1159/000477607



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