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[PMID]:29320825
[Au] Autor:Kim HJ; Yong TS; Shin MH; Lee KJ; Park GM; Suvonkulov U; Kovalenko D; Yu HS
[Ad] Endereço:Department of Parasitology and Tropical Medicine, School of Medicine, Pusan National University, Yangsan 50612, Korea.
[Ti] Título:Practical Algorisms for PCR-RFLP-Based Genotyping of Echinococcus granulosus Sensu Lato.
[So] Source:Korean J Parasitol;55(6):679-684, 2017 Dec.
[Is] ISSN:1738-0006
[Cp] País de publicação:Korea (South)
[La] Idioma:eng
[Ab] Resumo:Echinococcus granulosus sensu lato (s.l.) is a causative agent of cystic echinococcosis or cystic hydatid disease in humans and domestic and wild animals. The disease is a serious health problem in countries associated with poverty and poor hygiene practices, particularly in livestock raising. We introduced a practical algorism for genotyping the parasite, which may be useful to many developing countries. To evaluate the efficiency of the algorism, we genotyped 3 unknown strains isolated from human patients. We found that unknowns 1 and 3 were included in G1, G2, and G3 genotypes group and unknown 2 was included in G4 genotype (Echinococcus equinus) according to the algorisms. We confirmed these results by sequencing the 3 unknown isolates cox1 and nad1 PCR products. In conclusion, these new algorisms are very fast genotype identification tools that are suitable for evaluating E. granulosus s.l. isolated from livestock or livestock holders, particularly in developing countries.
[Mh] Termos MeSH primário: Algoritmos
Equinococose/parasitologia
Equinococose/veterinária
Echinococcus granulosus/genética
Genótipo
Técnicas de Genotipagem/métodos
Reação em Cadeia da Polimerase
Polimorfismo de Fragmento de Restrição
[Mh] Termos MeSH secundário: Animais
Animais Domésticos
Ciclo-Oxigenase 1/genética
Echinococcus granulosus/isolamento & purificação
Complexo I de Transporte de Elétrons/genética
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.14.99.1 (Cyclooxygenase 1); EC 1.6.5.3 (Electron Transport Complex I)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.3347/kjp.2017.55.6.679


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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


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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


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[PMID]:27770741
[Au] Autor:Frye MA; Ryu E; Nassan M; Jenkins GD; Andreazza AC; Evans JM; McElroy SL; Oglesbee D; Highsmith WE; Biernacka JM
[Ad] Endereço:Department of Psychiatry and Psychology, Mayo Clinic, Rochester, MN, USA. Electronic address: mfrye@mayo.edu.
[Ti] Título:Mitochondrial DNA sequence data reveals association of haplogroup U with psychosis in bipolar disorder.
[So] Source:J Psychiatr Res;84:221-226, 2017 01.
[Is] ISSN:1879-1379
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Converging genetic, postmortem gene-expression, cellular, and neuroimaging data implicate mitochondrial dysfunction in bipolar disorder. This study was conducted to investigate whether mitochondrial DNA (mtDNA) haplogroups and single nucleotide variants (SNVs) are associated with sub-phenotypes of bipolar disorder. MtDNA from 224 patients with Bipolar I disorder (BPI) was sequenced, and association of sequence variations with 3 sub-phenotypes (psychosis, rapid cycling, and adolescent illness onset) was evaluated. Gene-level tests were performed to evaluate overall burden of minor alleles for each phenotype. The haplogroup U was associated with a higher risk of psychosis. Secondary analyses of SNVs provided nominal evidence for association of psychosis with variants in the tRNA, ND4 and ND5 genes. The association of psychosis with ND4 (gene that encodes NADH dehydrogenase 4) was further supported by gene-level analysis. Preliminary analysis of mtDNA sequence data suggests a higher risk of psychosis with the U haplogroup and variation in the ND4 gene implicated in electron transport chain energy regulation. Further investigation of the functional consequences of this mtDNA variation is encouraged.
[Mh] Termos MeSH primário: Transtorno Bipolar/genética
Transtorno Bipolar/psicologia
DNA Mitocondrial
Predisposição Genética para Doença
Haplótipos
Transtornos Psicóticos/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Transtorno Bipolar/complicações
Estudos Transversais
Complexo I de Transporte de Elétrons/genética
Grupo com Ancestrais do Continente Europeu/genética
Feminino
Estudos de Associação Genética
Seres Humanos
Masculino
Meia-Idade
Proteínas Mitocondriais/genética
NADH Desidrogenase/genética
Fenótipo
Polimorfismo de Nucleotídeo Único
Transtornos Psicóticos/complicações
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Mitochondrial); 0 (Mitochondrial Proteins); EC 1.6.5.3 (Electron Transport Complex I); EC 1.6.5.3 (NADH dehydrogenase subunit 4); EC 1.6.99.3 (NADH Dehydrogenase); EC 1.6.99.3 (ND5 protein, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180111
[Lr] Data última revisão:
180111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161023
[St] Status:MEDLINE


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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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[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


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[PMID]:28985504
[Au] Autor:Lin R; Mo Y; Zha H; Qu Z; Xie P; Zhu ZJ; Xu Y; Xiong Y; Guan KL
[Ad] Endereço:State Key Laboratory of Genetic Engineering, Collaborative Innovation Center for Genetics and Development, School of Life Sciences, Molecular and Cell Biology Laboratory, Institute of Biomedical Sciences, Shanghai Medical College of Fudan University, Shanghai 200032, China. Electronic address: rlin@
[Ti] Título:CLOCK Acetylates ASS1 to Drive Circadian Rhythm of Ureagenesis.
[So] Source:Mol Cell;68(1):198-209.e6, 2017 Oct 05.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In addition to responding to environmental entrainment with diurnal variation, metabolism is also tightly controlled by cell-autonomous circadian clock. Extensive studies have revealed key roles of transcription in circadian control. Post-transcriptional regulation for the rhythmic gating of metabolic enzymes remains elusive. Here, we show that arginine biosynthesis and subsequent ureagenesis are collectively regulated by CLOCK (circadian locomotor output cycles kaput) in circadian rhythms. Facilitated by BMAL1 (brain and muscle Arnt-like protein), CLOCK directly acetylates K165 and K176 of argininosuccinate synthase (ASS1) to inactivate ASS1, which catalyzes the rate-limiting step of arginine biosynthesis. ASS1 acetylation by CLOCK exhibits circadian oscillation in human cells and mouse liver, possibly caused by rhythmic interaction between CLOCK and ASS1, leading to the circadian regulation of ASS1 and ureagenesis. Furthermore, we also identified NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9 (NDUFA9) and inosine-5'-monophosphate dehydrogenase 2 (IMPDH2) as acetylation substrates of CLOCK. Taken together, CLOCK modulates metabolic rhythmicity by acting as a rhythmic acetyl-transferase for metabolic enzymes.
[Mh] Termos MeSH primário: Fatores de Transcrição ARNTL/genética
Argininossuccinato Sintase/genética
Proteínas CLOCK/genética
Ritmo Circadiano/genética
Processamento de Proteína Pós-Traducional
Ureia/metabolismo
[Mh] Termos MeSH secundário: Fatores de Transcrição ARNTL/metabolismo
Acetilação
Animais
Arginina/biossíntese
Argininossuccinato Sintase/metabolismo
Proteínas CLOCK/metabolismo
Linhagem Celular Tumoral
Relógios Circadianos
Complexo I de Transporte de Elétrons/genética
Complexo I de Transporte de Elétrons/metabolismo
Células HEK293
Hepatócitos/citologia
Hepatócitos/metabolismo
Seres Humanos
IMP Desidrogenase/genética
IMP Desidrogenase/metabolismo
Masculino
Camundongos
Camundongos Knockout
Osteoblastos/metabolismo
Osteoblastos/patologia
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ARNTL Transcription Factors); 0 (Arntl protein, mouse); 8W8T17847W (Urea); 94ZLA3W45F (Arginine); EC 1.1.1.205 (IMP Dehydrogenase); EC 1.1.1.205 (IMPDH2 protein, human); EC 1.6.5.3 (Electron Transport Complex I); EC 1.6.5.3 (NDUFA9 protein, human); EC 2.3.1.48 (CLOCK Proteins); EC 2.3.1.48 (Clock protein, mouse); EC 6.3.4.5 (Argininosuccinate Synthase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171007
[St] Status:MEDLINE


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[PMID]:28960069
[Au] Autor:Belevich N; von Ballmoos C; Verkhovskaya M
[Ad] Endereço:Institute of Biotechnology, University of Helsinki , P.O. Box 65, Viikinkaari 1, FIN-00014 Helsinki, Finland.
[Ti] Título:Activation of Proton Translocation by Respiratory Complex I.
[So] Source:Biochemistry;56(42):5691-5697, 2017 Oct 24.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Activation of proton pumping by reconstituted and native membrane-bound Complex I was studied using optical electric potential- and pH-sensitive probes. We find that reconstituted Complex I has a delay in proton translocation, which is significantly longer than the delay in quinone reductase activity, indicating an initially decoupled state of Complex I. Studies of the amount of NADH required for the activation of pumping indicate the prerequisite of multiple turnovers. Proton pumping by Complex I was also activated by NADPH, excluding significant reduction of Complex I and a preexisting Δψ as activation factors. Co-reconstitution of Complex I and ATPase did not indicate an increased membrane permeability for protons in the uncoupled Complex I state. The delay in Complex I proton pumping activation was also observed in subbacterial vesicles. While it is negligible at room temperature, it strongly increases at a lower temperature. We conclude that Complex I undergoes a conversion from a decoupled state to a coupled state upon activation. The possible origins and importance of the observed phenomenon are discussed.
[Mh] Termos MeSH primário: Complexo I de Transporte de Elétrons/metabolismo
Proteínas de Escherichia coli/metabolismo
Escherichia coli/enzimologia
NAD/metabolismo
Prótons
[Mh] Termos MeSH secundário: Complexo I de Transporte de Elétrons/química
Proteínas de Escherichia coli/química
NAD/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Protons); 0U46U6E8UK (NAD); EC 1.6.5.3 (Electron Transport Complex I)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170930
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00727


  9 / 3135 MEDLINE  
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[PMID]:28910366
[Au] Autor:Chen Y; Meyer JN; Hill HZ; Lange G; Condon MR; Klein JC; Ndirangu D; Falvo MJ
[Ad] Endereço:War Related Illness and Injury Study Center, Veterans Affairs New Jersey Health Care System, East Orange, New Jersey, United States of America.
[Ti] Título:Role of mitochondrial DNA damage and dysfunction in veterans with Gulf War Illness.
[So] Source:PLoS One;12(9):e0184832, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Gulf War Illness (GWI) is a chronic multi-symptom illness not currently diagnosed by standard medical or laboratory test that affects 30% of veterans who served during the 1990-1991 Gulf War. The clinical presentation of GWI is comparable to that of patients with certain mitochondrial disorders-i.e., clinically heterogeneous multisystem symptoms. Therefore, we hypothesized that mitochondrial dysfunction may contribute to both the symptoms of GWI as well as its persistence over time. We recruited 21 cases of GWI (CDC and Kansas criteria) and 7 controls to participate in this study. Peripheral blood samples were obtained in all participants and a quantitative polymerase chain reaction (QPCR) based assay was performed to quantify mitochondrial and nuclear DNA lesion frequency and mitochondrial DNA (mtDNA) copy number (mtDNAcn) from peripheral blood mononuclear cells. Samples were also used to analyze nuclear DNA lesion frequency and enzyme activity for mitochondrial complexes I and IV. Both mtDNA lesion frequency (p = 0.015, d = 1.13) and mtDNAcn (p = 0.001; d = 1.69) were elevated in veterans with GWI relative to controls. Nuclear DNA lesion frequency was also elevated in veterans with GWI (p = 0.344; d = 1.41), but did not reach statistical significance. Complex I and IV activity (p > 0.05) were similar between groups and greater mtDNA lesion frequency was associated with reduced complex I (r2 = -0.35, p = 0.007) and IV (r2 = -0.28, p < 0.01) enzyme activity. In conclusion, veterans with GWI exhibit greater mtDNA damage which is consistent with mitochondrial dysfunction.
[Mh] Termos MeSH primário: Dano ao DNA
DNA Mitocondrial/genética
Doenças Mitocondriais/genética
Síndrome do Golfo Pérsico/genética
[Mh] Termos MeSH secundário: Estudos de Casos e Controles
Complexo I de Transporte de Elétrons/metabolismo
Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Feminino
Guerra do Golfo
Seres Humanos
Masculino
Meia-Idade
Veteranos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (DNA, Mitochondrial); EC 1.6.5.3 (Electron Transport Complex I); EC 1.9.3.1 (Electron Transport Complex IV)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170915
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184832


  10 / 3135 MEDLINE  
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[PMID]:28867181
[Au] Autor:Li YG; Dong ZF; Chen KK; He YP; Dai XY; Li S; Li JB; Zhu W; Wei M
[Ad] Endereço:Department of Cardiovascular Medicine, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai 200233, PR China. Electronic address: liyongguang222326@163.com.
[Ti] Título:Insulin upregulates GRIM-19 and protects cardiac mitochondrial morphology in type 1 diabetic rats partly through PI3K/AKT signaling pathway.
[So] Source:Biochem Biophys Res Commun;493(1):611-617, 2017 Nov 04.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Insulin is involved in the development of diabetic heart disease and is important in the activities of mitochondrial complex I. However, the effect of insulin on cardiac mitochondrial nicotinamide adenine dinucleotide dehydrogenase (ubiquinone) 1 subunit of retinoic-interferon-induced mortality 19 (GRIM-19) has not been characterized. The aim of this study was to investigate the effect of insulin on the mitochondrial GRIM-19 in the hearts of rats with streptozotocin (STZ)-induced type 1 diabetes. Protein changes of GRIM-19 were evaluated by western blotting and reverse transcription-quantitative polymerase chain reaction. Furthermore, the effects of insulin on mitochondrial complex I were detected in HeLa cells and H9C2 cardiac myocytes. During the development of diabetic heart disease, the cardiac function did not change within the 8 weeks, but the mitochondrial morphology was altered. The hearts from the rats with STZ-induced diabetes exhibited reduced expression of GRIM-19. Prior to the overt cardiac dilatation, mitochondrial alterations were already present. Following subcutaneous insulin injection, it was demonstrated that GRIM-19 protein was altered, as well as the mitochondrial morphology. The phosphoinositide 3-kinase inhibitor LY294002 had an effect on insulin signaling in H9C2 cardiacmyocytes, and decreased the level of GRIM-19 by half compared with that in the insulin group. The results indicate that insulin is essential for the control of cardiac mitochondrial morphology and the GRIM-19 expression partly via PI3K/AKT signaling pathways.
[Mh] Termos MeSH primário: Diabetes Mellitus Tipo 1/metabolismo
Diabetes Mellitus Tipo 1/patologia
Complexo I de Transporte de Elétrons/metabolismo
Insulina/administração & dosagem
Mitocôndrias Cardíacas/patologia
Chaperonas Moleculares/metabolismo
Fosfatidilinositol 3-Quinases/metabolismo
Proteínas Proto-Oncogênicas c-akt/metabolismo
[Mh] Termos MeSH secundário: Animais
Células HeLa
Seres Humanos
Masculino
Mitocôndrias Cardíacas/efeitos dos fármacos
Mitocôndrias Cardíacas/metabolismo
Ratos
Ratos Sprague-Dawley
Transdução de Sinais/efeitos dos fármacos
Estreptozocina
Regulação para Cima/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Insulin); 0 (Molecular Chaperones); 5W494URQ81 (Streptozocin); EC 1.6.5.3 (Electron Transport Complex I); EC 1.6.5.3 (GRIM-19 protein, rat); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170905
[St] Status:MEDLINE



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