Base de dados : MEDLINE
Pesquisa : D02.540.505.620 [Categoria DeCS]
Referências encontradas : 2828 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 283 ir para página                         

  1 / 2828 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28470519
[Au] Autor:Smolina N; Bruton J; Kostareva A; Sejersen T
[Ad] Endereço:Karolinska Institutet, Stockholm, Sweden. natalia.smolina@ki.se.
[Ti] Título:Assaying Mitochondrial Respiration as an Indicator of Cellular Metabolism and Fitness.
[So] Source:Methods Mol Biol;1601:79-87, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondrial respiration is the most important generator of cellular energy under most circumstances. It is a process of energy conversion of substrates into ATP. The Seahorse equipment allows measuring oxygen consumption rate (OCR) in living cells and estimates key parameters of mitochondrial respiration in real-time mode. Through use of mitochondrial inhibitors, four key mitochondrial respiration parameters can be measured: basal, ATP production-linked, maximal, and proton leak-linked OCR. This approach requires application of mitochondrial inhibitors-oligomycin to block ATP synthase, FCCP-to make the inner mitochondrial membrane permeable for protons and allow maximum electron flux through the electron transport chain, and rotenone and antimycin A-to inhibit complexes I and III, respectively. This chapter describes the protocol of OCR assessment in the culture of primary myotubes obtained upon satellite cell fusion.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Bioensaio/instrumentação
Mitocôndrias/metabolismo
Fosforilação Oxidativa
Consumo de Oxigênio
[Mh] Termos MeSH secundário: Animais
Antimicina A/farmacologia
Carbonil Cianeto p-Trifluormetoxifenil Hidrazona/farmacologia
Respiração Celular
Sobrevivência Celular
Complexo I de Transporte de Elétrons/antagonistas & inibidores
Complexo III da Cadeia de Transporte de Elétrons/antagonistas & inibidores
Camundongos
Mitocôndrias/efeitos dos fármacos
Fibras Musculares Esqueléticas/efeitos dos fármacos
Fibras Musculares Esqueléticas/metabolismo
Oligomicinas/farmacologia
Cultura Primária de Células
Ionóforos de Próton/farmacologia
Rotenona/farmacologia
Células Satélites de Músculo Esquelético/efeitos dos fármacos
Células Satélites de Músculo Esquelético/metabolismo
Desacopladores/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oligomycins); 0 (Proton Ionophores); 0 (Uncoupling Agents); 03L9OT429T (Rotenone); 370-86-5 (Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone); 642-15-9 (Antimycin A); 8L70Q75FXE (Adenosine Triphosphate); EC 1.10.2.2 (Electron Transport Complex III); EC 1.6.5.3 (Electron Transport Complex I)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180219
[Lr] Data última revisão:
180219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6960-9_7


  2 / 2828 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:29368834
[Au] Autor:Vatlin AA; Bekker OB; Lysenkova LN; Korolev AM; Shchekotikhin AE; Danilenko VN
[Ti] Título:[Sequencing and analysis of the resistome of Streptomyces fradiae ATCC19609 in order to develop a test system for screening of new antimicrobial agents].
[So] Source:Genetika;52(6):723-7, 2016 Jun.
[Is] ISSN:0016-6758
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:The paper provides the annotation and data on sequencing the antibiotic resistance genes in Streptomyces fradiae strain ATCC19609, highly sensitive to different antibiotics. Genome analysis revealed four groups of genes that determined the resistome of the tested strain. These included classical antibiotic resistance genes (nine aminoglycoside phosphotransferase genes, two beta-lactamase genes, and the genes of puromycin N-acetyltransferase, phosphinothricin N-acetyltransferase, and aminoglycoside acetyltransferase); the genes of ATP-dependent ABC transporters, involved in the efflux of antibiotics from the cell (MacB-2, BcrA, two-subunit MDR1); the genes of positive and negative regulation of transcription (whiB and padR families); and the genes of post-translational modification (serine-threonine protein kinases). A comparative characteristic of aminoglycoside phosphotransferase genes in S. fradiae ATCC19609, S. lividans TK24, and S. albus J1074, the causative agent of actinomycosis, is provided. The possibility of using the S. fradiae strain ATCC19609 as the test system for selection of the macrolide antibiotic oligomycin A derivatives with different levels of activity is demonstrated. Analysis of more than 20 semisynthetic oligomycin A derivatives made it possible to divide them into three groups according to the level of activity: inactive (>1 nmol/disk), 10 substances; with medium activity level (0.05­1 nmol/disk), 12 substances; and more active (0.01­0.05 nmol/disk), 2 substances. Important for the activity of semisynthetic derivatives is the change in the position of the 33rd carbon atom in the oligomycin A molecule.
[Mh] Termos MeSH primário: Proteínas de Bactérias
Farmacorresistência Bacteriana
Genoma Bacteriano
Oligomicinas/farmacologia
Streptomyces
Sequenciamento Completo do Genoma
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Farmacorresistência Bacteriana/efeitos dos fármacos
Farmacorresistência Bacteriana/genética
Testes de Sensibilidade Microbiana
Streptomyces/genética
Streptomyces/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Oligomycins); 05HQS4AI99 (oligomycin A)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180126
[St] Status:MEDLINE


  3 / 2828 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29054413
[Au] Autor:Mordel P; Schaeffer S; Dupas Q; Laville MA; Gérard M; Chapon F; Allouche S
[Ad] Endereço:Normandie Univ, UNICAEN, CHU Caen, Signalisation, électrophysiologie et imagerie des lésions d'ischémie-reperfusion myocardique, Caen, F-14032, France.
[Ti] Título:A 2 bp deletion in the mitochondrial ATP 6 gene responsible for the NARP (neuropathy, ataxia, and retinitis pigmentosa) syndrome.
[So] Source:Biochem Biophys Res Commun;494(1-2):133-137, 2017 Dec 09.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondrial (mt) DNA-associated NARP (neurogenic muscle weakness, ataxia, and retinitis pigmentosa) syndrome is due to mutation in the MT-ATP6 gene. We report the case of a 18-year-old man who presented with deafness, a myoclonic epilepsy, muscle weakness since the age of 10 and further developed a retinitis pigmentosa and ataxia. The whole mtDNA analysis by next-generation sequencing revealed the presence of the 2 bp microdeletion m.9127-9128 del AT in the ATP6 gene at 82% heteroplasmy in muscle and to a lower load in blood (10-20%) and fibroblasts (50%). Using the patient's fibroblasts, we demonstrated a 60% reduction of the oligomycin-sensitive ATPase hydrolytic activity, a 40% decrease in the ATP synthesis and determination of the mitochondrial membrane potential using the fluorescent probe tetramethylrhodamine, ethyl ester indicated a significant reduction in oligomycin sensitivity. In conclusion, we demonstrated that this novel AT deletion in the ATP6 gene is pathogenic and responsible for the NARP syndrome.
[Mh] Termos MeSH primário: Miopatias Mitocondriais/enzimologia
Miopatias Mitocondriais/genética
ATPases Mitocondriais Próton-Translocadoras/genética
Retinite Pigmentosa/enzimologia
Retinite Pigmentosa/genética
Deleção de Sequência
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/genética
Adenosina Trifosfatases/metabolismo
Trifosfato de Adenosina/metabolismo
Sequência de Bases
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Células Cultivadas
Análise Mutacional de DNA
DNA Mitocondrial/genética
Sequenciamento de Nucleotídeos em Larga Escala
Seres Humanos
Masculino
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
ATPases Mitocondriais Próton-Translocadoras/metabolismo
Oligomicinas/farmacologia
Síndrome
Adulto Jovem
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (DNA, Mitochondrial); 0 (Membrane Proteins); 0 (Oligomycins); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.3.- (Mitochondrial Proton-Translocating ATPases); EC 3.6.3.14 (MT-ATP6 protein, human); EC 3.6.3.14 (oligomycin sensitivity-conferring protein)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171022
[St] Status:MEDLINE


  4 / 2828 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[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


  5 / 2828 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[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


  6 / 2828 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28441462
[Au] Autor:Meyer L; Leymarie O; Chevalier C; Esnault E; Moroldo M; Da Costa B; Georgeault S; Roingeard P; Delmas B; Quéré P; Le Goffic R
[Ad] Endereço:VIM, INRA, Université Paris-Saclay, Jouy-en-Josas, France.
[Ti] Título:Transcriptomic profiling of a chicken lung epithelial cell line (CLEC213) reveals a mitochondrial respiratory chain activity boost during influenza virus infection.
[So] Source:PLoS One;12(4):e0176355, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Avian Influenza virus (AIV) is a major concern for the global poultry industry. Since 2012, several countries have reported AIV outbreaks among domestic poultry. These outbreaks had tremendous impact on poultry production and socio-economic repercussion on farmers. In addition, the constant emergence of highly pathogenic AIV also poses a significant risk to human health. In this study, we used a chicken lung epithelial cell line (CLEC213) to gain a better understanding of the molecular consequences of low pathogenic AIV infection in their natural host. Using a transcriptome profiling approach based on microarrays, we identified a cluster of mitochondrial genes highly induced during the infection. Interestingly, most of the regulated genes are encoded by the mitochondrial genome and are involved in the oxidative phosphorylation metabolic pathway. The biological consequences of this transcriptomic induction result in a 2.5- to 4-fold increase of the ATP concentration within the infected cells. PB1-F2, a viral protein that targets the mitochondria was not found associated to the boost of activity of the respiratory chain. We next explored the possibility that ATP may act as a host-derived danger signal (through production of extracellular ATP) or as a boost to increase AIV replication. We observed that, despite the activation of the P2X7 purinergic receptor pathway, a 1mM ATP addition in the cell culture medium had no effect on the virus replication in our epithelial cell model. Finally, we found that oligomycin, a drug that inhibits the oxidative phosphorylation process, drastically reduced the AIV replication in CLEC213 cells, without apparent cellular toxicity. Collectively, our results suggest that AIV is able to boost the metabolic capacities of its avian host in order to provide the important energy needs required to produce progeny virus.
[Mh] Termos MeSH primário: Transporte de Elétrons/genética
Células Epiteliais/virologia
Influenza Aviária/metabolismo
Pulmão/virologia
Mitocôndrias/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Galinhas
Transporte de Elétrons/efeitos dos fármacos
Inibidores Enzimáticos/farmacologia
Células Epiteliais/efeitos dos fármacos
Células Epiteliais/metabolismo
Perfilação da Expressão Gênica
Vírus da Influenza A
Influenza Aviária/virologia
Pulmão/efeitos dos fármacos
Pulmão/metabolismo
Mitocôndrias/genética
Oligomicinas/farmacologia
Fosforilação Oxidativa/efeitos dos fármacos
Transcriptoma
Replicação Viral/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Oligomycins)
[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:170426
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0176355


  7 / 2828 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28420869
[Au] Autor:Lysenkova LN; Saveljev OY; Grammatikova NE; Tsvetkov VB; Bekker OB; Danilenko VN; Dezhenkova LG; Bykov EE; Omelchuk OA; Korolev AM; Shchekotikhin AE
[Ad] Endereço:G. F. Gause Institute of New Antibiotics, Moscow, Russian Federation.
[Ti] Título:Verification of oligomycin A structure: synthesis and biological evaluation of 33-dehydrooligomycin A.
[So] Source:J Antibiot (Tokyo);70(8):871-877, 2017 Jul.
[Is] ISSN:0021-8820
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Although, the structure of oligomycin A (1) was confirmed by spectroscopic and chemical evaluations, some crystallographic data cast doubt on the originally adopted structure of the side 2-hydroxypropyl moiety of this antibiotic. It was suggested that the side chain of the oligomycin is enol-related (2-hydroxy-1-propenyl). To clarify this matter we synthesized and evaluated 33-dehydrooligomycin A (2) prepared by the Kornblum oxidation of 33-O-mesyloligomycin A (3) by dimethyl sulfoxide. NMR data for 33-dehydrooligomycin (2) and results of quantum chemical calculations have shown that this derivative exists in the keto rather than in the enol tautomer 2a. The in vitro antimicrobial activity of 2 was approximately two times weaker in comparison with oligomycin A against Streptomyces fradiae ATCC-19609 and reference Candida spp. strains and similar activity against certain filamentous fungi. The docking binding estimate of 2 with F F ATP synthase showed a slight decrease in binding affinity for 2 when compared with oligomycin A; that correlated with its activity against S. fradiae ATCC 19609 that is supersensitive to oligomycin A. The in vitro antiproliferative activities of 2 are also discussed.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Antifúngicos/farmacologia
Antineoplásicos/farmacologia
Oligomicinas/farmacologia
[Mh] Termos MeSH secundário: Antibacterianos/química
Antifúngicos/química
Antineoplásicos/química
Candida/efeitos dos fármacos
Linhagem Celular Tumoral
Seres Humanos
Espectroscopia de Ressonância Magnética
Oligomicinas/química
Streptomyces/efeitos dos fármacos
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (33-dehydrooligomycin A); 0 (Anti-Bacterial Agents); 0 (Antifungal Agents); 0 (Antineoplastic Agents); 0 (Oligomycins); 05HQS4AI99 (oligomycin A)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE
[do] DOI:10.1038/ja.2017.48


  8 / 2828 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28103219
[Au] Autor:Georgakopoulos ND; Wells G; Campanella M
[Ad] Endereço:Department of Comparative Biomedical Sciences, The Royal Veterinary College, University of London, London, UK.
[Ti] Título:The pharmacological regulation of cellular mitophagy.
[So] Source:Nat Chem Biol;13(2):136-146, 2017 Jan 19.
[Is] ISSN:1552-4469
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Small molecules are pharmacological tools of considerable value for dissecting complex biological processes and identifying potential therapeutic interventions. Recently, the cellular quality-control process of mitophagy has attracted considerable research interest; however, the limited availability of suitable chemical probes has restricted our understanding of the molecular mechanisms involved. Current approaches to initiate mitophagy include acute dissipation of the mitochondrial membrane potential (ΔΨ ) by mitochondrial uncouplers (for example, FCCP/CCCP) and the use of antimycin A and oligomycin to impair respiration. Both approaches impair mitochondrial homeostasis and therefore limit the scope for dissection of subtle, bioenergy-related regulatory phenomena. Recently, novel mitophagy activators acting independently of the respiration collapse have been reported, offering new opportunities to understand the process and potential for therapeutic exploitation. We have summarized the current status of mitophagy modulators and analyzed the available chemical tools, commenting on their advantages, limitations and current applications.
[Mh] Termos MeSH primário: Antimicina A/farmacologia
Mitocôndrias/efeitos dos fármacos
Degradação Mitocondrial/efeitos dos fármacos
Oligomicinas/farmacologia
[Mh] Termos MeSH secundário: Antimicina A/química
Seres Humanos
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Mitocôndrias/metabolismo
Mitocôndrias/patologia
Estrutura Molecular
Oligomicinas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Oligomycins); 642-15-9 (Antimycin A)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170504
[Lr] Data última revisão:
170504
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170120
[St] Status:MEDLINE
[do] DOI:10.1038/nchembio.2287


  9 / 2828 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27927723
[Au] Autor:Santo-Domingo J; Chareyron I; Dayon L; Núñez Galindo A; Cominetti O; Pilar Giner Giménez M; De Marchi U; Canto C; Kussmann M; Wiederkehr A
[Ad] Endereço:Mitochondrial Function, Nestlé Institute of Health Sciences, Lausanne, Switzerland.
[Ti] Título:Coordinated activation of mitochondrial respiration and exocytosis mediated by PKC signaling in pancreatic ß cells.
[So] Source:FASEB J;31(3):1028-1045, 2017 Mar.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondria play a central role in pancreatic ß-cell nutrient sensing by coupling their metabolism to plasma membrane excitability and insulin granule exocytosis. Whether non-nutrient secretagogues stimulate mitochondria as part of the molecular mechanism to promote insulin secretion is not known. Here, we show that PKC signaling, which is employed by many non-nutrient secretagogues, augments mitochondrial respiration in INS-1E (rat insulinoma cell line clone 1E) and human pancreatic ß cells. The phorbol ester, phorbol 12-myristate 13-acetate, accelerates mitochondrial respiration at both resting and stimulatory glucose concentrations. A range of inhibitors of novel PKC isoforms prevent phorbol ester-induced respiration. Respiratory response was blocked by oligomycin that demonstrated PKC-dependent acceleration of mitochondrial ATP synthesis. Enhanced respiration was observed even when glycolysis was bypassed or fatty acid transport was blocked, which suggested that PKC regulates mitochondrial processes rather than upstream catabolic fluxes. A phosphoproteome study of phorbol ester-stimulated INS-1E cells maintained under resting (2.5 mM) glucose revealed a large number of phosphorylation sites that were altered during short-term activation of PKC signaling. The data set was enriched for proteins that are involved in gene expression, cytoskeleton remodeling, secretory vesicle transport, and exocytosis. Interactome analysis identified PKC, C-Raf, and ERK1/2 as the central phosphointeraction cluster. Prevention of ERK1/2 signaling by using a MEK1 inhibitor caused a marked decreased in phorbol 12-myristate 13-acetate-induced mitochondrial respiration. ERK1/2 signaling module therefore links PKC activation to downstream mitochondrial activation. We conclude that non-nutrient secretagogues act, in part, PKC and downstream ERK1/2 signaling to stimulate mitochondrial energy production to compensate for energy expenditure that is linked to ß-cell activation.-Santo-Domingo, J., Chareyron, I., Dayon, L., Galindo, A. N., Cominetti, O., Giménez, M. P. G., De Marchi, U., Canto, C., Kussmann, M., Wiederkehr, A. Coordinated activation of mitochondrial respiration and exocytosis mediated by PKC signaling in pancreatic ß cells.
[Mh] Termos MeSH primário: Exocitose
Células Secretoras de Insulina/metabolismo
Mitocôndrias/metabolismo
Proteína Quinase C/metabolismo
Explosão Respiratória
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Células Cultivadas
Glucose/metabolismo
Seres Humanos
Isoenzimas/metabolismo
Sistema de Sinalização das MAP Quinases
Proteína Quinase 1 Ativada por Mitógeno/metabolismo
Proteína Quinase 3 Ativada por Mitógeno/metabolismo
Oligomicinas/farmacologia
Proteínas Proto-Oncogênicas c-raf/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Isoenzymes); 0 (Oligomycins); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.11.1 (Proto-Oncogene Proteins c-raf); EC 2.7.11.13 (Protein Kinase C); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3); IY9XDZ35W2 (Glucose)
[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:161209
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201600837R


  10 / 2828 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27818165
[Au] Autor:Zhdanov AV; Aviello G; Knaus UG; Papkovsky DB
[Ad] Endereço:School of Biochemistry & Cell Biology, University College Cork, Cork, Ireland. Electronic address: a.zhdanov@ucc.ie.
[Ti] Título:Cellular ROS imaging with hydro-Cy3 dye is strongly influenced by mitochondrial membrane potential.
[So] Source:Biochim Biophys Acta;1861(2):198-204, 2017 02.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Hydrocyanines are widely used as fluorogenic probes to monitor reactive oxygen species (ROS) generation in cells. Their brightness, stability to autoxidation and photobleaching, large signal change upon oxidation, pH independence and red/near infrared emission are particularly attractive for imaging ROS in live tissue. METHODS: Using confocal fluorescence microscopy we have examined an interference of mitochondrial membrane potential (ΔΨm) with fluorescence intensity and localisation of a commercial hydro-Cy3 probe in respiring and non-respiring colon carcinoma HCT116 cells. RESULTS: We found that the oxidised (fluorescent) form of hydro-Cy3 is highly homologous to the common ΔΨm-sensitive probe JC-1, which accumulates and aggregates only in 'energised' negatively charged mitochondrial matrix. Therefore, hydro-Cy3 oxidised by hydroxyl and superoxide radicals tends to accumulate in mitochondrial matrix, but dissipates and loses brightness as soon as ΔΨm is compromised. Experiments with mitochondrial inhibitor oligomycin and uncoupler FCCP, as well as a common ROS producer paraquat demonstrated that signals of the oxidised hydro-Cy3 probe rapidly and strongly decrease upon mitochondrial depolarisation, regardless of the rate of cellular ROS production. CONCLUSIONS: While analysing ROS-derived fluorescence of commercial hydrocyanine probes, an accurate control of ΔΨm is required. GENERAL SIGNIFICANCE: If not accounted for, non-specific effect of mitochondrial polarisation state on the behaviour of oxidised hydrocyanines can cause artefacts and data misinterpretation in ROS studies.
[Mh] Termos MeSH primário: Carbocianinas/metabolismo
Potencial da Membrana Mitocondrial/fisiologia
Mitocôndrias/metabolismo
Mitocôndrias/fisiologia
Espécies Reativas de Oxigênio/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Fluorescência
Células HCT116
Seres Humanos
Camundongos
Camundongos Endogâmicos C57BL
Oligomicinas/metabolismo
Oxirredução
Superóxidos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Carbocyanines); 0 (Oligomycins); 0 (Reactive Oxygen Species); 0 (cyanine dye 3); 11062-77-4 (Superoxides)
[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:161108
[St] Status:MEDLINE



página 1 de 283 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde