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[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 / 2411 MEDLINE  
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[PMID]:29227076
[Au] Autor:Danylovych HV
[Ti] Título:Evaluation of functioning of mitochondrial electron transport chain with NADH and FAD autofluorescence
[So] Source:Ukr Biochem J;88(1):31-43, 2016 Jan-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:We prove the feasibility of evaluation of mitochondrial electron transport chain function in isolated mitochondria of smooth muscle cells of rats from uterus using fluorescence of NADH and FAD coenzymes. We found the inversely directed changes in FAD and NADH fluorescence intensity under normal functioning of mitochondrial electron transport chain. The targeted effect of inhibitors of complex I, III and IV changed fluorescence of adenine nucleotides. Rotenone (5 µM) induced rapid increase in NADH fluorescence due to inhibition of complex I, without changing in dynamics of FAD fluorescence increase. Antimycin A, a complex III inhibitor, in concentration of 1 µg/ml caused sharp increase in NADH fluorescence and moderate increase in FAD fluorescence in comparison to control. NaN3 (5 mM), a complex IV inhibitor, and CCCP (10 µM), a protonophore, caused decrease in NADH and FAD fluorescence. Moreover, all the inhibitors caused mitochondria swelling. NO donors, e.g. 0.1 mM sodium nitroprusside and sodium nitrite similarly to the effects of sodium azide. Energy-dependent Ca2+ accumulation in mitochondrial matrix (in presence of oxidation substrates and Mg-ATP2- complex) is associated with pronounced drop in NADH and FAD fluorescence followed by increased fluorescence of adenine nucleotides, which may be primarily due to Ca2+- dependent activation of dehydrogenases of citric acid cycle. Therefore, the fluorescent signal of FAD and NADH indicates changes in oxidation state of these nucleotides in isolated mitochondria, which may be used to assay the potential of effectors of electron transport chain.
[Mh] Termos MeSH primário: Complexo III da Cadeia de Transporte de Elétrons/metabolismo
Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Complexo I de Transporte de Elétrons/metabolismo
Flavina-Adenina Dinucleotídeo/química
Mitocôndrias/metabolismo
NAD/química
[Mh] Termos MeSH secundário: Animais
Antimicina A/farmacologia
Cálcio/metabolismo
Carbonil Cianeto m-Clorofenil Hidrazona/farmacologia
Fracionamento Celular
Transporte de Elétrons/efeitos dos fármacos
Complexo I de Transporte de Elétrons/antagonistas & inibidores
Complexo III da Cadeia de Transporte de Elétrons/antagonistas & inibidores
Complexo IV da Cadeia de Transporte de Elétrons/antagonistas & inibidores
Inibidores Enzimáticos/farmacologia
Feminino
Flavina-Adenina Dinucleotídeo/metabolismo
Mitocôndrias/efeitos dos fármacos
Miócitos de Músculo Liso/efeitos dos fármacos
Miócitos de Músculo Liso/metabolismo
Miométrio/efeitos dos fármacos
Miométrio/metabolismo
NAD/metabolismo
Nitroprussiato/farmacologia
Imagem Óptica
Ratos
Rotenona/farmacologia
Azida Sódica/farmacologia
Nitrito de Sódio/farmacologia
Desacopladores/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Uncoupling Agents); 03L9OT429T (Rotenone); 0U46U6E8UK (NAD); 146-14-5 (Flavin-Adenine Dinucleotide); 169D1260KM (Nitroprusside); 555-60-2 (Carbonyl Cyanide m-Chlorophenyl Hydrazone); 642-15-9 (Antimycin A); 968JJ8C9DV (Sodium Azide); EC 1.10.2.2 (Electron Transport Complex III); EC 1.6.5.3 (Electron Transport Complex I); EC 1.9.3.1 (Electron Transport Complex IV); M0KG633D4F (Sodium Nitrite); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.01.031


  3 / 2411 MEDLINE  
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[PMID]:28450391
[Au] Autor:Korge P; Calmettes G; John SA; Weiss JN
[Ad] Endereço:From the UCLA Cardiovascular Research Laboratory and the Departments of Medicine (Cardiology) and Physiology, David Geffen School of Medicine at UCLA, Los Angeles, California 90095.
[Ti] Título:Reactive oxygen species production induced by pore opening in cardiac mitochondria: The role of complex III.
[So] Source:J Biol Chem;292(24):9882-9895, 2017 06 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recent evidence has implicated succinate-driven reverse electron transport (RET) through complex I as a major source of damaging reactive oxygen species (ROS) underlying reperfusion injury after prolonged cardiac ischemia. However, this explanation may be incomplete, because RET on reperfusion is self-limiting and therefore transient. RET can only generate ROS when mitochondria are well polarized, and it ceases when permeability transition pores (PTP) open during reperfusion. Because prolonged ischemia/reperfusion also damages electron transport complexes, we investigated whether such damage could lead to ROS production after PTP opening has occurred. Using isolated cardiac mitochondria, we demonstrate a novel mechanism by which antimycin-inhibited complex III generates significant amounts of ROS in the presence of Mg and NAD and the absence of exogenous substrates upon inner membrane pore formation by alamethicin or Ca -induced PTP opening. We show that H O production under these conditions is related to Mg -dependent NADH generation by malic enzyme. H O production is blocked by stigmatellin, indicating its origin from complex III, and by piericidin, demonstrating the importance of NADH-related ubiquinone reduction for ROS production under these conditions. For maximal ROS production, the rate of NADH generation has to be equal or below that of NADH oxidation, as further increases in [NADH] elevate ubiquinol-related complex III reduction beyond the optimal range for ROS generation. These results suggest that if complex III is damaged during ischemia, PTP opening may result in succinate/malate-fueled ROS production from complex III due to activation of malic enzyme by increases in matrix [Mg ], [NAD ], and [ADP].
[Mh] Termos MeSH primário: Complexo III da Cadeia de Transporte de Elétrons/metabolismo
Malato Desidrogenase/metabolismo
Mitocôndrias Cardíacas/metabolismo
Espécies Reativas de Oxigênio/agonistas
[Mh] Termos MeSH secundário: Difosfato de Adenosina/metabolismo
Alameticina/farmacologia
Animais
Antimicina A/análogos & derivados
Antimicina A/farmacologia
Biocatálise/efeitos dos fármacos
Sinalização do Cálcio/efeitos dos fármacos
Complexo III da Cadeia de Transporte de Elétrons/antagonistas & inibidores
Ativação Enzimática/efeitos dos fármacos
Inibidores Enzimáticos/farmacologia
Peróxido de Hidrogênio/metabolismo
Ionóforos/farmacologia
Magnésio/metabolismo
Malato Desidrogenase/química
Mitocôndrias Cardíacas/química
Mitocôndrias Cardíacas/efeitos dos fármacos
NAD/metabolismo
Oxirredução
Polienos/farmacologia
Porosidade/efeitos dos fármacos
Piridinas/farmacologia
Coelhos
Espécies Reativas de Oxigênio/metabolismo
Ubiquinona/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Ionophores); 0 (Polyenes); 0 (Pyridines); 0 (Reactive Oxygen Species); 0U46U6E8UK (NAD); 11118-72-2 (antimycin); 1339-63-5 (Ubiquinone); 27061-78-5 (Alamethicin); 61D2G4IYVH (Adenosine Diphosphate); 642-15-9 (Antimycin A); 8VT513UJ9R (piericidin A); 91682-96-1 (stigmatellin); BBX060AN9V (Hydrogen Peroxide); EC 1.1.1.37 (Malate Dehydrogenase); EC 1.10.2.2 (Electron Transport Complex III); I38ZP9992A (Magnesium)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171228
[Lr] Data última revisão:
171228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.768317


  4 / 2411 MEDLINE  
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[PMID]:29053833
[Au] Autor:Manole A; Jaunmuktane Z; Hargreaves I; Ludtmann MHR; Salpietro V; Bello OD; Pope S; Pandraud A; Horga A; Scalco RS; Li A; Ashokkumar B; Lourenço CM; Heales S; Horvath R; Chinnery PF; Toro C; Singleton AB; Jacques TS; Abramov AY; Muntoni F; Hanna MG; Reilly MM; Revesz T; Kullmann DM; Jepson JEC; Houlden H
[Ad] Endereço:Department of Molecular Neuroscience and Neurogenetics Laboratory, UCL Institute of Neurology, Queen Square, London, WC1N 3BG, UK.
[Ti] Título:Clinical, pathological and functional characterization of riboflavin-responsive neuropathy.
[So] Source:Brain;140(11):2820-2837, 2017 11 01.
[Is] ISSN:1460-2156
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Brown-Vialetto-Van Laere syndrome represents a phenotypic spectrum of motor, sensory, and cranial nerve neuropathy, often with ataxia, optic atrophy and respiratory problems leading to ventilator-dependence. Loss-of-function mutations in two riboflavin transporter genes, SLC52A2 and SLC52A3, have recently been linked to Brown-Vialetto-Van Laere syndrome. However, the genetic frequency, neuropathology and downstream consequences of riboflavin transporter mutations are unclear. By screening a large cohort of 132 patients with early-onset severe sensory, motor and cranial nerve neuropathy we confirmed the strong genetic link between riboflavin transporter mutations and Brown-Vialetto-Van Laere syndrome, identifying 22 pathogenic mutations in SLC52A2 and SLC52A3, 14 of which were novel. Brain and spinal cord neuropathological examination of two cases with SLC52A3 mutations showed classical symmetrical brainstem lesions resembling pathology seen in mitochondrial disease, including severe neuronal loss in the lower cranial nerve nuclei, anterior horns and corresponding nerves, atrophy of the spinothalamic and spinocerebellar tracts and posterior column-medial lemniscus pathways. Mitochondrial dysfunction has previously been implicated in an array of neurodegenerative disorders. Since riboflavin metabolites are critical components of the mitochondrial electron transport chain, we hypothesized that reduced riboflavin transport would result in impaired mitochondrial activity, and confirmed this using in vitro and in vivo models. Electron transport chain complex I and complex II activity were decreased in SLC52A2 patient fibroblasts, while global knockdown of the single Drosophila melanogaster riboflavin transporter homologue revealed reduced levels of riboflavin, downstream metabolites, and electron transport chain complex I activity. This in turn led to abnormal mitochondrial membrane potential, respiratory chain activity and morphology. Riboflavin transporter knockdown in Drosophila also resulted in severely impaired locomotor activity and reduced lifespan, mirroring patient pathology, and these phenotypes could be partially rescued using a novel esterified derivative of riboflavin. Our findings expand the genetic, clinical and neuropathological features of Brown-Vialetto-Van Laere syndrome, implicate mitochondrial dysfunction as a downstream consequence of riboflavin transporter gene defects, and validate riboflavin esters as a potential therapeutic strategy.
[Mh] Termos MeSH primário: Encéfalo/patologia
Paralisia Bulbar Progressiva/genética
Perda Auditiva Neurossensorial/genética
Proteínas de Membrana Transportadoras/genética
Receptores Acoplados a Proteínas-G/genética
Medula Espinal/patologia
[Mh] Termos MeSH secundário: Adolescente
Animais
Atrofia
Encéfalo/ultraestrutura
Paralisia Bulbar Progressiva/metabolismo
Paralisia Bulbar Progressiva/patologia
Criança
Pré-Escolar
Citrato (si)-Sintase/metabolismo
Drosophila melanogaster
Complexo I de Transporte de Elétrons/metabolismo
Complexo II de Transporte de Elétrons/metabolismo
Complexo III da Cadeia de Transporte de Elétrons/metabolismo
Feminino
Fibroblastos/metabolismo
Técnicas de Silenciamento de Genes
Perda Auditiva Neurossensorial/metabolismo
Perda Auditiva Neurossensorial/patologia
Seres Humanos
Técnicas In Vitro
Lactente
Locomoção/genética
Longevidade/genética
Masculino
Microscopia Eletrônica
Vias Neurais
Riboflavina
Tratos Espinocerebelares/patologia
Tratos Espinotalâmicos/patologia
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Transport Proteins); 0 (Receptors, G-Protein-Coupled); 0 (SLC52A2 protein, human); 0 (SLC52A3 protein, human); EC 1.10.2.2 (Electron Transport Complex III); EC 1.3.5.1 (Electron Transport Complex II); EC 1.6.5.3 (Electron Transport Complex I); EC 2.3.3.1 (Citrate (si)-Synthase); TLM2976OFR (Riboflavin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171021
[St] Status:MEDLINE
[do] DOI:10.1093/brain/awx231


  5 / 2411 MEDLINE  
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[PMID]:28750029
[Au] Autor:Long Z; Duan G; Li H; Yi T; Wu X; Chen F; Wu Z; Gao Y
[Ad] Endereço:Department of Anesthesiology, Xinqiao Hospital, Third Military Medical University, Chongqing, China.
[Ti] Título:Ubiquinol-cytochrome c reductase core protein 1 may be involved in delayed cardioprotection from preconditioning induced by diazoxide.
[So] Source:PLoS One;12(7):e0181903, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:This study aimed to use long-term diazoxide treatment to establish a loss-of-cardioprotection model and then perform proteomics analysis to explore which proteins of mitochondrial inner membrane (MIM) are potentially involved in delayed cardioprotection. Rats received 1 to 8 weeks of diazoxide treatments (20 mg•kg-1•d-1) to establish a loss-of-cardioprotection model in different groups. Detection of serum cTnI levels and cell apoptosis assays in heart tissue were performed. Then, rats MIM after 0, 4 and 6 weeks of diazoxide treatment was isolated and proteomics analysis was performed. An invitro model of H9C2 cells was performed to explore the effects of targeted protein on delayed cardioprotection. The effect of delayed cardioprotection by diazoxide preconditioning disappeared when diazoxide treatments were given for six weeks or longer. Ubiquinol-cytochrome c reductase core protein 1 (UQCRC1) was identified in the proteomics analysis. UQCRC1 expression was upregulated by diazoxide treatment in H9C2 cells, and UQCRC1 down-regulation could increase the lactate dehydrogenase release and apoptosis rate after injury induced by oxygen glucose deprivation. These results showed that UQCRC1 might contribute to the loss-of-cardioprotection model induced by long-term diazoxide treatment and play a role in delayed cardioprotection.
[Mh] Termos MeSH primário: Cardiotônicos/farmacologia
Diazóxido/farmacologia
Complexo III da Cadeia de Transporte de Elétrons/metabolismo
Precondicionamento Isquêmico Miocárdico
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos dos fármacos
Linhagem Celular
Regulação para Baixo/efeitos dos fármacos
Glucose/deficiência
Marcação In Situ das Extremidades Cortadas
Masculino
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Membranas Mitocondriais/efeitos dos fármacos
Membranas Mitocondriais/metabolismo
Miocárdio/patologia
Oxigênio
Proteômica
Ratos
Troponina I/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cardiotonic Agents); 0 (Troponin I); EC 1.10.2.2 (Electron Transport Complex III); EC 1.10.2.2 (Uqcrc1 protein, rat); IY9XDZ35W2 (Glucose); O5CB12L4FN (Diazoxide); S88TT14065 (Oxygen)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181903


  6 / 2411 MEDLINE  
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[PMID]:28736227
[Au] Autor:Jang S; Javadov S
[Ad] Endereço:Department of Physiology, University of Puerto Rico School of Medicine, San Juan, Puerto Rico.
[Ti] Título:Association between ROS production, swelling and the respirasome integrity in cardiac mitochondria.
[So] Source:Arch Biochem Biophys;630:1-8, 2017 Sep 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Although mitochondrial Ca overload and ROS production play a critical role in mitochondria-mediated cell death, a cause-effect relationship between them remains elusive. This study elucidated the crosstalk between mitochondrial swelling, ROS production, and electron transfer chain (ETC) supercomplexes in rat heart mitochondria in response to Ca and tert-butyl hydroperoxide (TBH), a lipid-soluble organic peroxide. Results showed that ROS production induced by TBH was significantly increased in the presence of Ca in a dose-dependent manner. TBH markedly inhibited the state 3 respiration rate with no effect on the mitochondrial swelling. Ca exerted a slight effect on mitochondrial respiration that was greatly aggravated by TBH. Analysis of supercomplexes revealed a minor difference in the presence of TBH and/or Ca . However, incubation of mitochondria in the presence of high Ca (1 mM) or inhibitors of ETC complexes (rotenone and antimycin A) induced disintegration of the main supercomplex, respirasome. Thus, PTP-dependent swelling of mitochondria solely depends on Ca but not ROS. TBH has no effect on the respirasome while Ca induces disintegration of the supercomplex only at a high concentration. Intactness of individual ETC complexes I and III is important for maintenance of the structural integrity of the respirasome.
[Mh] Termos MeSH primário: Sinalização do Cálcio/fisiologia
Cálcio/metabolismo
Complexo III da Cadeia de Transporte de Elétrons/metabolismo
Complexo I de Transporte de Elétrons/metabolismo
Mitocôndrias Cardíacas/metabolismo
Espécies Reativas de Oxigênio/metabolismo
[Mh] Termos MeSH secundário: Animais
Masculino
Ratos
Ratos Sprague-Dawley
terc-Butil Hidroperóxido/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Reactive Oxygen Species); 955VYL842B (tert-Butylhydroperoxide); EC 1.10.2.2 (Electron Transport Complex III); EC 1.6.5.3 (Electron Transport Complex I); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE


  7 / 2411 MEDLINE  
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[PMID]:28688734
[Au] Autor:Altamura E; Fiorentino R; Milano F; Trotta M; Palazzo G; Stano P; Mavelli F
[Ad] Endereço:Chemistry Department, University "Aldo Moro", Via Orabona 4, I-70126 Bari, Italy.
[Ti] Título:First moves towards photoautotrophic synthetic cells: In vitro study of photosynthetic reaction centre and cytochrome bc1 complex interactions.
[So] Source:Biophys Chem;229:46-56, 2017 Oct.
[Is] ISSN:1873-4200
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Following a bottom-up synthetic biology approach it is shown that vesicle-based cell-like systems (shortly "synthetic cells") can be designed and assembled to perform specific function (for biotechnological applications) and for studies in the origin-of-life field. We recently focused on the construction of synthetic cells capable to converting light into chemical energy. Here we first present our approach, which has been realized so far by the reconstitution of photosynthetic reaction centre in the membrane of giant lipid vesicles. Next, the details of our ongoing research program are presented. It involves the use of the reaction centre, the coenzyme Q-cytochrome c oxidoreductase, and the ATP synthase for creating an autonomous synthetic cell. We show experimental results on the chemistry of the first two proteins showing that they can efficiently sustain light-driven chemical oscillations. Moreover, the cyclic pattern has been reproduced in silico by a minimal kinetic model.
[Mh] Termos MeSH primário: Complexo III da Cadeia de Transporte de Elétrons/metabolismo
Complexo de Proteínas do Centro de Reação Fotossintética/metabolismo
[Mh] Termos MeSH secundário: Sistema Livre de Células
Difusão Dinâmica da Luz
Transporte de Elétrons
Complexo III da Cadeia de Transporte de Elétrons/química
Cinética
Lipossomos/química
Lipossomos/metabolismo
Oxirredução
Fotossíntese
Complexo de Proteínas do Centro de Reação Fotossintética/química
Rhodobacter sphaeroides/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Liposomes); 0 (Photosynthetic Reaction Center Complex Proteins); EC 1.10.2.2 (Electron Transport Complex III)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170710
[St] Status:MEDLINE


  8 / 2411 MEDLINE  
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[PMID]:28673964
[Au] Autor:Zhang C; Liu Z; Bunker E; Ramirez A; Lee S; Peng Y; Tan AC; Eckhardt SG; Chapnick DA; Liu X
[Ad] Endereço:From the Department of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, Colorado 80303 and.
[Ti] Título:Sorafenib targets the mitochondrial electron transport chain complexes and ATP synthase to activate the PINK1-Parkin pathway and modulate cellular drug response.
[So] Source:J Biol Chem;292(36):15105-15120, 2017 Sep 08.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sorafenib (Nexavar) is a broad-spectrum multikinase inhibitor that proves effective in treating advanced renal-cell carcinoma and liver cancer. Despite its well-characterized mechanism of action on several established cancer-related protein kinases, sorafenib causes variable responses among human tumors, although the cause for this variation is unknown. In an unbiased screening of an oncology drug library, we found that sorafenib activates recruitment of the ubiquitin E3 ligase Parkin to damaged mitochondria. We show that sorafenib inhibits the activity of both complex II/III of the electron transport chain and ATP synthase. Dual inhibition of these complexes, but not inhibition of each individual complex, stabilizes the serine-threonine protein kinase PINK1 on the mitochondrial outer membrane and activates Parkin. Unlike the protonophore carbonyl cyanide -chlorophenylhydrazone, which activates the mitophagy response, sorafenib treatment triggers PINK1/Parkin-dependent cellular apoptosis, which is attenuated upon Bcl-2 overexpression. In summary, our results reveal a new mechanism of action for sorafenib as a mitocan and suggest that high Parkin activity levels could make tumor cells more sensitive to sorafenib's actions, providing one possible explanation why Parkin may be a tumor suppressor gene. These insights could be useful in developing new rationally designed combination therapies with sorafenib.
[Mh] Termos MeSH primário: Complexo III da Cadeia de Transporte de Elétrons/antagonistas & inibidores
Complexo II de Transporte de Elétrons/antagonistas & inibidores
Mitocôndrias/efeitos dos fármacos
ATPases Mitocondriais Próton-Translocadoras/antagonistas & inibidores
Niacinamida/análogos & derivados
Compostos de Fenilureia/farmacologia
Proteínas Quinases/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
[Mh] Termos MeSH secundário: Células Cultivadas
Transporte de Elétrons/efeitos dos fármacos
Complexo II de Transporte de Elétrons/metabolismo
Complexo III da Cadeia de Transporte de Elétrons/metabolismo
Células HEK293
Seres Humanos
Mitocôndrias/enzimologia
Mitocôndrias/metabolismo
ATPases Mitocondriais Próton-Translocadoras/metabolismo
Niacinamida/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phenylurea Compounds); 25X51I8RD4 (Niacinamide); 9ZOQ3TZI87 (sorafenib); EC 1.10.2.2 (Electron Transport Complex III); EC 1.3.5.1 (Electron Transport Complex II); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.3.2.27 (parkin protein); EC 2.7.- (Protein Kinases); EC 2.7.11.1 (PTEN-induced putative kinase); EC 3.6.3.- (Mitochondrial Proton-Translocating ATPases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170705
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.783175


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[PMID]:28673544
[Au] Autor:Bottani E; Cerutti R; Harbour ME; Ravaglia S; Dogan SA; Giordano C; Fearnley IM; D'Amati G; Viscomi C; Fernandez-Vizarra E; Zeviani M
[Ad] Endereço:MRC Mitochondrial Biology Unit, University of Cambridge, Wellcome Trust/MRC Building Hills Road, Cambridge CB2 0XY, UK.
[Ti] Título:TTC19 Plays a Husbandry Role on UQCRFS1 Turnover in the Biogenesis of Mitochondrial Respiratory Complex III.
[So] Source:Mol Cell;67(1):96-105.e4, 2017 Jul 06.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Loss-of-function mutations in TTC19 (tetra-tricopeptide repeat domain 19) have been associated with severe neurological phenotypes and mitochondrial respiratory chain complex III deficiency. We previously demonstrated the mitochondrial localization of TTC19 and its link with complex III biogenesis. Here we provide detailed insight into the mechanistic role of TTC19, by investigating a Ttc19 mouse model that shows progressive neurological and metabolic decline, decreased complex III activity, and increased production of reactive oxygen species. By using both the Ttc19 mouse model and a range of human cell lines, we demonstrate that TTC19 binds to the fully assembled complex III dimer, i.e., after the incorporation of the iron-sulfur Rieske protein (UQCRFS1). The in situ maturation of UQCRFS1 produces N-terminal polypeptides, which remain bound to holocomplex III. We show that, in normal conditions, these UQCRFS1 fragments are rapidly removed, but when TTC19 is absent they accumulate within complex III, causing its structural and functional impairment.
[Mh] Termos MeSH primário: Complexo III da Cadeia de Transporte de Elétrons/metabolismo
Proteínas com Ferro-Enxofre/metabolismo
Proteínas de Membrana/metabolismo
Mitocôndrias/enzimologia
Proteínas Mitocondriais/metabolismo
[Mh] Termos MeSH secundário: Animais
Comportamento Animal
Modelos Animais de Doenças
Complexo III da Cadeia de Transporte de Elétrons/deficiência
Complexo III da Cadeia de Transporte de Elétrons/genética
Feminino
Genótipo
Células HeLa
Seres Humanos
Proteínas com Ferro-Enxofre/genética
Cinética
Masculino
Proteínas de Membrana/genética
Camundongos Endogâmicos C57BL
Camundongos Knockout
Doenças Mitocondriais
Proteínas Mitocondriais/genética
Atividade Motora
Degeneração Neural
Sistema Nervoso/metabolismo
Sistema Nervoso/patologia
Sistema Nervoso/fisiopatologia
Fenótipo
Ligação Proteica
Estabilidade Proteica
Proteólise
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Iron-Sulfur Proteins); 0 (Membrane Proteins); 0 (Mitochondrial Proteins); 0 (Reactive Oxygen Species); 0 (Rieske iron-sulfur protein); 0 (UQCRFS1 protein, human); 0 (UQCRFS1 protein, mouse); 0 (tetratricopeptide 19 protein, human); 0 (tetratricopeptide 19 protein, mouse); EC 1.10.2.2 (Electron Transport Complex III)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170705
[St] Status:MEDLINE


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[PMID]:28604960
[Au] Autor:Zhang T; Hong F; Qian G; Tong F; Zhou X; Huang X; Yang R; Huang X
[Ad] Endereço:Department of Genetics and Metabolism, Children's Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310052, China. xinwenhuang@126.com.
[Ti] Título:[Analysis of UQCRB gene mutation in a child with mitochondrial complex III deficiency].
[So] Source:Zhonghua Yi Xue Yi Chuan Xue Za Zhi;34(3):382-386, 2017 Jun 10.
[Is] ISSN:1003-9406
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVE: To delineate the clinical, biochemical and genetic mutational characteristics of a child with mitochondrial complex III deficiency. METHODS: Clinical information and results of auxiliary examination of the patient were analyzed. Next-generation sequencing of the mitochondrial genome and related nuclear genes was carried out. Suspected mutation was confirmed in both parents with Sanger sequencing. Heterozygous deletion was mapped with chromosomal microarray analysis and confirmed with real-time PCR. RESULTS: The patient presented with vomiting, polypnea, fever, metabolic acidosis, hyperlactatemia, hypoglycemia, dysfunction of coagulation and immune system, in addition with increased lactate dehydrogenase and creatine kinase isoenzyme. Elevation of blood alanine and acylcarnitines as well as urinary ketotic dicarboxylic acid were also noted. The patient also presented development delay, mental retardation and hypotonia. Sequence analysis revealed two mutations in the nuclear gene UQCRB, which included a previously reported frameshift mutation c.306_309delAAAA(p.Arg105Lysfs*22) and a novel large deletion encompassing the entire UQCRB gene. CONCLUSION: The clinical, biochemical and gene mutation characteristics of a child with mitochondrial complex III deficiency caused by mutations of the UQCRB gene have been delineated.
[Mh] Termos MeSH primário: Proteínas de Transporte/genética
Complexo III da Cadeia de Transporte de Elétrons/deficiência
Doenças Mitocondriais/genética
Mutação
[Mh] Termos MeSH secundário: Adulto
Sequência de Bases
Complexo III da Cadeia de Transporte de Elétrons/genética
Feminino
Seres Humanos
Lactente
Masculino
Dados de Sequência Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (ubiquinone-binding proteins); EC 1.10.2.2 (Electron Transport Complex III)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170914
[Lr] Data última revisão:
170914
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170613
[St] Status:MEDLINE
[do] DOI:10.3760/cma.j.issn.1003-9406.2017.03.015



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