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Pesquisa : A11.284.149.450.349 [Categoria DeCS]
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[PMID]:28746987
[Au] Autor:Cardenas-Rodriguez M; Tokatlidis K
[Ad] Endereço:Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, UK.
[Ti] Título:Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space.
[So] Source:FEBS Lett;591(17):2661-2670, 2017 09.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Oxidative protein folding is confined to the bacterial periplasm, endoplasmic reticulum and the mitochondrial intermembrane space. Maintaining a redox balance requires the presence of reductive pathways. The major thiol-reducing pathways engage the thioredoxin and the glutaredoxin systems which are involved in removal of oxidants, protein proofreading and folding. Alterations in redox balance likely affect the flux of these redox pathways and are related to ageing and diseases such as neurodegenerative disorders and cancer. Here, we first review the well-studied oxidative and reductive processes in the bacterial periplasm and the endoplasmic reticulum, and then discuss the less understood process in the mitochondrial intermembrane space, highlighting its importance for the proper function of the cell.
[Mh] Termos MeSH primário: Citosol/metabolismo
Membranas Mitocondriais/metabolismo
Proteínas/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Oxirredução
Dobramento de Proteína
Transporte Proteico
Proteínas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12766


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[PMID]:29307826
[Au] Autor:Wu G; Li S; Zong G; Liu X; Fei S; Shen L; Guan X; Yang X; Shen Y
[Ad] Endereço:State Key Laboratory of Medicinal Chemical Biology and College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China.
[Ti] Título:Single channel recording of a mitochondrial calcium uniporter.
[So] Source:Biochem Biophys Res Commun;496(1):127-132, 2018 01 29.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondrial calcium uniporter (MCU) is the pore-forming subunit of the entire uniporter complex and plays an important role in mitochondrial calcium uptake. However, the single channel recording of MCU remains controversial. Here, we expressed and purified different MCU proteins and then reconstituted them into planar lipid bilayers for single channel recording. We showed that MCU alone from Pyronema omphalodes (pMCU) is active with prominent single channel Ca currents. In sharp contrast, MCU alone from Homo sapiens (hMCU) is inactive. The essential MCU regulator (EMRE) activates hMCU, and therefore, the complex (hMCU-hEMRE) shows prominent single channel Ca currents. These single channel currents are sensitive to the specific MCU inhibitor Ruthenium Red. Our results clearly demonstrate that active MCU can conduct large amounts of calcium into the mitochondria.
[Mh] Termos MeSH primário: Canais de Cálcio/química
Sinalização do Cálcio
Cálcio/química
Ativação do Canal Iônico
Bicamadas Lipídicas/química
Potencial da Membrana Mitocondrial
Membranas Mitocondriais/química
[Mh] Termos MeSH secundário: Seres Humanos
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Calcium Channels); 0 (Lipid Bilayers); 0 (mitochondrial calcium uniporter); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE


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[PMID]:29223393
[Au] Autor:Korotkov SM; Konovalova SA; Nesterov VP; Brailovskaya IV
[Ad] Endereço:Sechenov Institute of Evolutionary Physiology and Biochemistry, The Russian Academy of Sciences, Thorez pr. 44, 194223 St. Petersburg, Russia. Electronic address: korotkov@SK1645.spb.edu.
[Ti] Título:Mersalyl prevents the Tl -induced permeability transition pore opening in the inner membrane of Ca -loaded rat liver mitochondria.
[So] Source:Biochem Biophys Res Commun;495(2):1716-1721, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It was earlier shown that the calcium load of rat liver mitochondria in medium containing TlNO and KNO resulted in the Tl -induced mitochondrial permeability transition pore (MPTP) opening in the inner membrane. This opening was accompanied by an increase in swelling and membrane potential dissipation and a decrease in state 3, state 4, and 2,4-dinitrophenol-uncoupled respiration. This respiratory decrease was markedly leveled by mersalyl (MSL), the phosphate symporter (PiC) inhibitor which poorly stimulated the calcium-induced swelling, but further increased the potential dissipation. All of these effects of Ca and MSL were visibly reduced in the presence of the MPTP inhibitors (ADP, N-ethylmaleimide, and cyclosporine A). High MSL concentrations attenuated the ability of ADP to inhibit the MPTP. Our data suggest that the PiC can participate in the Tl -induced MPTP opening in the inner membrane of Ca -loaded rat liver mitochondria.
[Mh] Termos MeSH primário: Mersalil/farmacologia
Mitocôndrias Hepáticas/efeitos dos fármacos
Mitocôndrias Hepáticas/metabolismo
Proteínas de Transporte da Membrana Mitocondrial/efeitos dos fármacos
Proteínas de Transporte da Membrana Mitocondrial/metabolismo
Tálio/farmacologia
[Mh] Termos MeSH secundário: Animais
Cálcio/metabolismo
Técnicas In Vitro
Transporte de Íons/efeitos dos fármacos
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Membranas Mitocondriais/efeitos dos fármacos
Membranas Mitocondriais/metabolismo
Dilatação Mitocondrial/efeitos dos fármacos
Consumo de Oxigênio/efeitos dos fármacos
Ratos
Ratos Wistar
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Mitochondrial Membrane Transport Proteins); 0 (mitochondrial permeability transition pore); 5X1IO031V8 (Mersalyl); AD84R52XLF (Thallium); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171211
[St] Status:MEDLINE


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[PMID]:29217137
[Au] Autor:Broniarek I; Jarmuszkiewicz W
[Ad] Endereço:Department of Bioenergetics, Institute of Molecular Biology and Biotechnology, Adam Mickiewicz University in Poznan, Poland.
[Ti] Título:Atorvastatin affects negatively respiratory function of isolated endothelial mitochondria.
[So] Source:Arch Biochem Biophys;637:64-72, 2018 01 01.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The purpose of this research was to elucidate the direct effects of two popular blood cholesterol-lowering drugs used to treat cardiovascular diseases, atorvastatin and pravastatin, on respiratory function, membrane potential, and reactive oxygen species formation in mitochondria isolated from human umbilical vein endothelial cells (EA.hy926 cell line). Hydrophilic pravastatin did not significantly affect endothelial mitochondria function. In contrast, hydrophobic calcium-containing atorvastatin induced a loss of outer mitochondrial membrane integrity, an increase in hydrogen peroxide formation, and reductions in maximal (phosphorylating or uncoupled) respiratory rate, membrane potential and oxidative phosphorylation efficiency. The atorvastatin-induced changes indicate an impairment of mitochondrial function at the level of ATP synthesis and at the level of the respiratory chain, likely at complex I and complex III. The atorvastatin action on endothelial mitochondria was highly dependent on calcium ions and led to a disturbance in mitochondrial calcium homeostasis. Uptake of calcium ions included in atorvastatin molecule induced mitochondrial uncoupling that enhanced the inhibition of the mitochondrial respiratory chain by atorvastatin. Our results indicate that hydrophobic calcium-containing atorvastatin, widely used as anti-atherosclerotic agent, has a direct negative action on isolated endothelial mitochondria.
[Mh] Termos MeSH primário: Atorvastatina Cálcica/toxicidade
Inibidores de Hidroximetilglutaril-CoA Redutases/toxicidade
Mitocôndrias/efeitos dos fármacos
Mitocôndrias/metabolismo
Respiração/efeitos dos fármacos
[Mh] Termos MeSH secundário: Cálcio/metabolismo
Transporte de Elétrons/efeitos dos fármacos
Células Endoteliais da Veia Umbilical Humana
Seres Humanos
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Membranas Mitocondriais/efeitos dos fármacos
Membranas Mitocondriais/metabolismo
Fosforilação Oxidativa/efeitos dos fármacos
Consumo de Oxigênio/efeitos dos fármacos
Pravastatina/toxicidade
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Hydroxymethylglutaryl-CoA Reductase Inhibitors); 0 (Reactive Oxygen Species); 48A5M73Z4Q (Atorvastatin Calcium); KXO2KT9N0G (Pravastatin); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE


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[PMID]:28456637
[Au] Autor:Vienne JC; Cimetta C; Dubois M; Duburcq T; Favory R; Dessein AF; Fontaine M; Joncquel-Chevalier Curt M; Cuisset JM; Douillard C; Mention-Mulliez K; Dobbelaere D; Vamecq J
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Laboratory of Hormonology, Metabolism-Nutrition & Oncology (HMNO), Center of Biology and Pathology (CBP) Pierre-Marie Degand, CHRU Lille, France.
[Ti] Título:A fast method for high resolution oxymetry study of skeletal muscle mitochondrial respiratory chain complexes.
[So] Source:Anal Biochem;528:57-62, 2017 07 01.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:High resolution oxymetry study (HROS) of skeletal muscle usually requires 90-120 min preparative phase (dissection, permeabilization and washing). This work reports on the suitability of a rapid muscle preparation which by-passes this long preparation. For a few seconds only, muscle biopsy from pigs is submitted to gentle homogenization at 8000 rotations per minute using an ultra-dispersor apparatus. Subsequent HROS is performed using FCCP instead of ADP, compounds crossing and not plasma membrane, respectively. This simplified procedure compares favorably with classical (permeabilized fibers) HROS in terms of respiratory chain complex activities. Mitochondria from cells undergoing ultradispersion were functionally preserved as attested by relative inefficacy of added cytochrome C (not crossing intact mitochondrial outer membrane) to stimulate mitochondrial respiration. Responsiveness of respiration to ADP (in the absence of FCCP) suggested that these intact mitochondria were outside cells disrupted by ultradispersion or within cells permeated by this procedure.
[Mh] Termos MeSH primário: Respiração Celular
Mitocôndrias Musculares/metabolismo
Músculo Esquelético/metabolismo
Consumo de Oxigênio
[Mh] Termos MeSH secundário: Animais
Biópsia
Transporte de Elétrons
Complexo de Proteínas da Cadeia de Transporte de Elétrons/metabolismo
Feminino
Membranas Mitocondriais/metabolismo
Fibras Musculares Esqueléticas/metabolismo
Permeabilidade
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Electron Transport Chain Complex Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE


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[PMID]:29235339
[Au] Autor:Babich LG; Shlykov SG; Kushnarova AM; Kosterin SO
[Ti] Título:Ca(2+)-dependent regulation of the Ca(2+) concentration in the myometrium mitochondria. I. Trifluoperazine effects on mitochondria membranes polarization and [Ca(2+)](m).
[So] Source:Ukr Biochem J;88(4):5-11, 2016 Jul-Aug.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:Са2+-dependent regulation of Ca2+ exchange in mitochondria is carried out with participation of calmodulin. We have shown previously that calmodulin antagonists reduced the level of mitochondrial membrane polarization and induced increase of the ionized Са concentration in both the mitochondrial matrix and cell cytoplasm. The concentration-dependent influence of trifluoperazine on the level of polarization of mitochondrial membranes has been shown in this work. The coordinates of the Hill graphs were used to calculate the constant K0.5 and the Hill coefficient. K0.5 was 24.4 ± 5 µM (n = 10). The Hill coefficient was 2.0 ± 0.2, indicating the presence of two centers of the trifluoperazine binding. We have also studied [Ca2+]m changes, when incubating mitochondria in mediums of different composition: without ATP and ions of Mg (0-medium), in the presence of 3 mM Mg (Mg-medium) and 3 mM Mg + 3 mM ATP (Mg,ATP-medium). It was shown that the composition of the incubation medium affected the [Ca2+]m values in the absence of exogenous Ca2+ and did not affect them in the presence of the latter. Preincubation of mitochondria in mediums of different composition with 25 µM trifluoperazine did not affect the [Ca2+]m values both before and after the addition of 100 µÐœ Са2+ to the incubation medium. It was concluded, that trifluoperazine depolarized myometrial mitochondria membranes in concentration-dependent manner. However, mitochondria preincubation with 25 µM trifluope­razine accompanied by 50% decrease in membrane polarization did not affect the [Ca2+]m values.
[Mh] Termos MeSH primário: Cálcio/metabolismo
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Mitocôndrias/efeitos dos fármacos
Membranas Mitocondriais/efeitos dos fármacos
Trifluoperazina/farmacologia
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Animais
Calmodulina/antagonistas & inibidores
Calmodulina/metabolismo
Meios de Cultura/química
Relação Dose-Resposta a Droga
Feminino
Transporte de Íons/efeitos dos fármacos
Cinética
Magnésio/metabolismo
Mitocôndrias/metabolismo
Membranas Mitocondriais/metabolismo
Miométrio/química
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calmodulin); 0 (Culture Media); 214IZI85K3 (Trifluoperazine); 8L70Q75FXE (Adenosine Triphosphate); I38ZP9992A (Magnesium); 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:171214
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.04.005


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[PMID]:29235334
[Au] Autor:Khyzhnyak SV; Midyk SV; Sysoliatin SV; Voitsitsky VM
[Ti] Título:Fatty acids composition of inner mitochondrial membrane of rat cardiomyocytes and hepatocytes during hypoxia-hypercapnia.
[So] Source:Ukr Biochem J;88(3):92-8, 2016 May-Jun.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:We studied the influence of hypoxic-hypercapnic environment under the effect of hypothermia (artificial hibernation) on fatty acids spectrum of inner mitochondrial membrane (IMM) lipids of rat cardiomyocytes and hepatocytes. Specific for cellular organelles redistribution of IMM fatty acids was determined. It led to the reduction of total amount of saturated fatty acids (SFAs) and increase of unsaturated fatty acids (UFAs) in cardiomyocytes and to the increase of SFAs and decrease of UFAs in hepatocytes. The decrease in the content of oleic acid and increased content of arachidonic and docosahexaenoic acids in IMM were shown. This may be due to their role in the regulatory systems during hibernation, as well as following exit therefrom. It is assumed that artificial hibernation state is characterized by the stress reaction leading to optimal readjustment of fatty acids composition of membrane lipids, which supports functional activity of mitochondria in hepatocytes and cardiomyocytes.
[Mh] Termos MeSH primário: Ácidos Graxos Insaturados/química
Ácidos Graxos/química
Hepatócitos/metabolismo
Hipercapnia/metabolismo
Hipóxia/metabolismo
Membranas Mitocondriais/metabolismo
Miócitos Cardíacos/metabolismo
[Mh] Termos MeSH secundário: Animais
Animais não Endogâmicos
Ácidos Graxos/classificação
Ácidos Graxos/isolamento & purificação
Ácidos Graxos Insaturados/classificação
Ácidos Graxos Insaturados/isolamento & purificação
Hibernação
Masculino
Lipídeos de Membrana/química
Lipídeos de Membrana/classificação
Lipídeos de Membrana/isolamento & purificação
Mitocôndrias/química
Mitocôndrias/metabolismo
Membranas Mitocondriais/química
Ratos
Estresse Fisiológico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Fatty Acids, Unsaturated); 0 (Membrane Lipids)
[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:171214
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.03.092


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[PMID]:29203148
[Au] Autor:Dehdashtian E; Mehrzadi S; Yousefi B; Hosseinzadeh A; Reiter RJ; Safa M; Ghaznavi H; Naseripour M
[Ad] Endereço:School of Medicine, Iran University of Medical Sciences, Tehran, Iran.
[Ti] Título:Diabetic retinopathy pathogenesis and the ameliorating effects of melatonin; involvement of autophagy, inflammation and oxidative stress.
[So] Source:Life Sci;193:20-33, 2018 Jan 15.
[Is] ISSN:1879-0631
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Diabetic retinopathy (DR), a microvascular complication of diabetes mellitus (DM), remains as one of the major causes of vision loss worldwide. The release of pro-inflammatory cytokines and the adhesion of leukocytes to retinal capillaries are initial events in DR development. Inflammation, ER stress, oxidative stress and autophagy are major causative factors involved in the pathogenesis of DR. Diabetes associated hyperglycemia leads to mitochondrial electron transport chain dysfunction culminating in a rise in ROS generation. Since mitochondria are the major source of ROS production, oxidative stress induced by mitochondrial dysfunction also contributes to the development of diabetic retinopathy. Autophagy increases in the retina of diabetic patients and is regulated by ER stress, oxidative stress and inflammation-related pathways. Autophagy functions as a double-edged sword in DR. Under mild stress, autophagic activity can lead to cell survival while during severe stress, dysregulated autophagy results in massive cell death and may have a role in initiation and exacerbation of DR. Melatonin and its metabolites play protective roles against inflammation, ER stress and oxidative stress due to their direct free radical scavenger activities and indirect antioxidant activity via the stimulation antioxidant enzymes including glutathione reductase, glutathione peroxidase, superoxide dismutase and catalase. Melatonin also acts as a cell survival agent by modulating autophagy in various cell types and under different conditions through amelioration of oxidative stress, ER stress and inflammation. Herein, we review the possible effects of melatonin on diabetic retinopathy, focusing on its ability to regulate autophagy processes.
[Mh] Termos MeSH primário: Complicações do Diabetes/metabolismo
Retinopatia Diabética/metabolismo
Melatonina/metabolismo
[Mh] Termos MeSH secundário: Apoptose
Autofagia/efeitos dos fármacos
Sobrevivência Celular
Retinopatia Diabética/tratamento farmacológico
Retinopatia Diabética/genética
Seres Humanos
Inflamação/metabolismo
Melatonina/farmacologia
Melatonina/uso terapêutico
Mitocôndrias/metabolismo
Membranas Mitocondriais/metabolismo
Estresse Oxidativo/efeitos dos fármacos
Retina/patologia
Superóxido Dismutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 1.15.1.1 (Superoxide Dismutase); JL5DK93RCL (Melatonin)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180108
[Lr] Data última revisão:
180108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171206
[St] Status:MEDLINE


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[PMID]:28461337
[Au] Autor:Wang Y; Landry AP; Ding H
[Ad] Endereço:From the Department of Biological Sciences, Louisiana State University, Baton Rouge, Louisiana 70803.
[Ti] Título:The mitochondrial outer membrane protein mitoNEET is a redox enzyme catalyzing electron transfer from FMNH to oxygen or ubiquinone.
[So] Source:J Biol Chem;292(24):10061-10067, 2017 06 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Increasing evidence suggests that mitoNEET, a target of the type II diabetes drug pioglitazone, is a key regulator of energy metabolism in mitochondria. MitoNEET is anchored to the mitochondrial outer membrane via its N-terminal α helix domain and hosts a redox-active [2Fe-2S] cluster in its C-terminal cytosolic region. The mechanism by which mitoNEET regulates energy metabolism in mitochondria, however, is not fully understood. Previous studies have shown that mitoNEET specifically interacts with the reduced flavin mononucleotide (FMNH ) and that FMNH can quickly reduce the mitoNEET [2Fe-2S] clusters. Here we report that the reduced mitoNEET [2Fe-2S] clusters can be readily oxidized by oxygen. In the presence of FMN, NADH, and flavin reductase, which reduces FMN to FMNH using NADH as the electron donor, mitoNEET mediates oxidation of NADH with a concomitant reduction of oxygen. Ubiquinone-2, an analog of ubiquinone-10, can also oxidize the reduced mitoNEET [2Fe-2S] clusters under anaerobic or aerobic conditions. Compared with oxygen, ubiquinone-2 is more efficient in oxidizing the mitoNEET [2Fe-2S] clusters, suggesting that ubiquinone could be an intrinsic electron acceptor of the reduced mitoNEET [2Fe-2S] clusters in mitochondria. Pioglitazone or its analog NL-1 appears to inhibit the electron transfer activity of mitoNEET by forming a unique complex with mitoNEET and FMNH The results suggest that mitoNEET is a redox enzyme that may promote oxidation of NADH to facilitate enhanced glycolysis in the cytosol and that pioglitazone may regulate energy metabolism in mitochondria by inhibiting the electron transfer activity of mitoNEET.
[Mh] Termos MeSH primário: Mononucleotídeo de Flavina/metabolismo
Hidroquinonas/metabolismo
Membranas Mitocondriais/enzimologia
Proteínas Mitocondriais/metabolismo
Ubiquinona/metabolismo
[Mh] Termos MeSH secundário: Espectroscopia de Ressonância de Spin Eletrônica
Transporte de Elétrons/efeitos dos fármacos
Metabolismo Energético/efeitos dos fármacos
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
FMN Redutase/genética
FMN Redutase/metabolismo
Seres Humanos
Hipoglicemiantes/farmacologia
Cinética
Membranas Mitocondriais/efeitos dos fármacos
Membranas Mitocondriais/metabolismo
Proteínas Mitocondriais/química
Proteínas Mitocondriais/genética
Oxirredução
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Tiazóis/farmacologia
Tiazolidinedionas/farmacologia
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (5-(3,5-di-tert-butyl-4-hydroxybenzyl)-4-hydroxythiazol-2(5H)-one); 0 (CISD1 protein, human); 0 (Escherichia coli Proteins); 0 (Hydroquinones); 0 (Hypoglycemic Agents); 0 (Mitochondrial Proteins); 0 (Peptide Fragments); 0 (Recombinant Proteins); 0 (Thiazoles); 0 (Thiazolidinediones); 0 (flavin mononucleotide hydroquinone); 1339-63-5 (Ubiquinone); 7N464URE7E (Flavin Mononucleotide); EC 1.5.1.38 (FMN Reductase); EC 1.5.1.41 (Fre protein, E coli); I7T5V2W47R (Ubiquinone Q2); X4OV71U42S (pioglitazone)
[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:170503
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.789800


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[PMID]:28458255
[Au] Autor:Zhang Y; Bharathi SS; Rardin MJ; Lu J; Maringer KV; Sims-Lucas S; Prochownik EV; Gibson BW; Goetzman ES
[Ad] Endereço:From the Department of Pediatrics, University of Pittsburgh School of Medicine, University of Pittsburgh, Children's Hospital of Pittsburgh of University of Pittsburgh Medical Center, Pittsburgh, Pennsylvania 15224 and.
[Ti] Título:Lysine desuccinylase SIRT5 binds to cardiolipin and regulates the electron transport chain.
[So] Source:J Biol Chem;292(24):10239-10249, 2017 06 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:SIRT5 is a lysine desuccinylase known to regulate mitochondrial fatty acid oxidation and the urea cycle. Here, SIRT5 was observed to bind to cardiolipin via an amphipathic helix on its N terminus. , succinyl-CoA was used to succinylate liver mitochondrial membrane proteins. SIRT5 largely reversed the succinyl-CoA-driven lysine succinylation. Quantitative mass spectrometry of SIRT5-treated membrane proteins pointed to the electron transport chain, particularly Complex I, as being highly targeted for desuccinylation by SIRT5. Correspondingly, SIRT5 HEK293 cells showed defects in both Complex I- and Complex II-driven respiration. In mouse liver, SIRT5 expression was observed to localize strictly to the periportal hepatocytes. However, homogenates prepared from whole SIRT5 liver did show reduced Complex II-driven respiration. The enzymatic activities of Complex II and ATP synthase were also significantly reduced. Three-dimensional modeling of Complex II suggested that several SIRT5-targeted lysine residues lie at the protein-lipid interface of succinate dehydrogenase subunit B. We postulate that succinylation at these sites may disrupt Complex II subunit-subunit interactions and electron transfer. Lastly, SIRT5 mice, like humans with Complex II deficiency, were found to have mild lactic acidosis. Our findings suggest that SIRT5 is targeted to protein complexes on the inner mitochondrial membrane via affinity for cardiolipin to promote respiratory chain function.
[Mh] Termos MeSH primário: Cardiolipinas/metabolismo
Complexo de Proteínas da Cadeia de Transporte de Elétrons/metabolismo
Hepatócitos/enzimologia
Modelos Moleculares
Processamento de Proteína Pós-Traducional
Sirtuínas/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Animais
Cardiolipinas/química
Complexo I de Transporte de Elétrons/metabolismo
Complexo II de Transporte de Elétrons/metabolismo
Células HEK293
Hepatócitos/metabolismo
Seres Humanos
Lisina/metabolismo
Camundongos
Camundongos Knockout
Mitocôndrias Hepáticas/enzimologia
Mitocôndrias Hepáticas/metabolismo
Membranas Mitocondriais/enzimologia
Membranas Mitocondriais/metabolismo
Mutação
Transporte Proteico
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Sirtuínas/química
Sirtuínas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Cardiolipins); 0 (Electron Transport Chain Complex Proteins); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 0 (SIRT5 protein, mouse); EC 1.3.5.1 (Electron Transport Complex II); EC 1.6.5.3 (Electron Transport Complex I); EC 3.5.1.- (SIRT5 protein, human); EC 3.5.1.- (Sirtuins); K3Z4F929H6 (Lysine)
[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:170502
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.785022



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