Search results for "Electron Transport Complex II"

showing 10 items of 11 documents

Arabidopsis RCD1 coordinates chloroplast and mitochondrial functions through interaction with ANAC transcription factors

2019

Reactive oxygen species (ROS)-dependent signaling pathways from chloroplasts and mitochondria merge at the nuclear protein RADICAL-INDUCED CELL DEATH1 (RCD1). RCD1 interacts in vivo and suppresses the activity of the transcription factors ANAC013 and ANAC017, which mediate a ROS-related retrograde signal originating from mitochondrial complex III. Inactivation of RCD1 leads to increased expression of mitochondrial dysfunction stimulon (MDS) genes regulated by ANAC013 and ANAC017. Accumulating MDS gene products, including alternative oxidases (AOXs), affect redox status of the chloroplasts, leading to changes in chloroplast ROS processing and increased protection of photosynthetic apparatus.…

0106 biological sciences0301 basic medicineretrograde signalingChloroplastsArabidopsisPlant BiologyMitochondrion01 natural sciencesElectron Transport Complex IIIGene Expression Regulation PlantArabidopsisOXIDATIVE STRESS-RESPONSETranscriptional regulationCYCLIC ELECTRON FLOWBiology (General)Nuclear proteinANAC transcription factors1183 Plant biology microbiology virologyreactive oxygen speciesbiologyChemistryRETROGRADE REGULATIONGeneral NeuroscienceQRNuclear Proteinsfood and beveragesGeneral MedicinePlants Genetically Modified:Science::Biological sciences [DRNTU]Cell biologyMitochondriaChloroplastviherhiukkasetMedicineSignal transductionmitochondrial functionsResearch ArticleSignal TransductionQH301-705.5SciencemitokondriotGenetics and Molecular BiologyGeneral Biochemistry Genetics and Molecular BiologyPROTEIN COMPLEXESSIGNALING PATHWAYS03 medical and health scienceschloroplastStress PhysiologicalALTERNATIVE OXIDASESkasvitENZYME-ACTIVITIESredox signalingTranscription factorarabidopsis RCD1General Immunology and MicrobiologybiokemiaArabidopsis Proteinsta1182Biology and Life Sciencesbiology.organism_classification030104 developmental biologyCELL-DEATHPLANT-MITOCHONDRIAA. thalianaGeneral BiochemistryRetrograde signalingGENES-ENCODING MITOCHONDRIALproteiinit010606 plant biology & botanyTranscription Factors
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Evaluation of whole antioxidant defenses of human mononuclear cells by a new in vitro biological test: lack of correlation between erythrocyte and mo…

2009

1873-2933 (Electronic) Journal Article; OBJECTIVES: This work aims to evaluate the resistance of mononuclear cells to oxidative stress using a "KRL" test, formerly utilized to evaluate the resistance of erythrocyte to free radicals. METHODS: The "KRL" test evaluates the resistance to lysis of cells treated by free radicals generated under standardized conditions. RESULTS: We defined new analytical parameters (level of radical production, time course, number of cells) to obtain an accurate assay determining the resistance to oxidative stress of mononuclear cells, in comparison to that of erythrocytes. This test allows the evaluation of change in the redox state of mononuclear cells (improved…

AntioxidantLysisErythrocytesmedicine.medical_treatmentRadicalClinical BiochemistryStatistics as TopicCell Culture TechniquesAntimycin AInflammationImmunologic Testsmedicine.disease_causePeripheral blood mononuclear cellAntioxidantsAnti-Bacterial Agents/pharmacologyImmunologic Tests/*methodsElectron Transport Complex IIIReactive Oxygen Species/metabolismAntioxidants/*metabolism/pharmacologymedicineErythrocytes/*metabolismLeukocytesHumansDiagnosticOxidative Stress/*drug effectschemistry.chemical_classificationReactive oxygen speciesAntimycin A/pharmacologyElectron Transport Complex III/antagonists & inhibitorsChemistryMononuclear/drug effects/*metabolismReproducibility of ResultsGeneral MedicineIn vitroAnti-Bacterial AgentsOxidative StressBiochemistryLeukocytes MononuclearReagent KitsReagent Kits Diagnosticmedicine.symptomReactive Oxygen SpeciesOxidation-ReductionOxidative stress
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New molecular aspects of regulation of mitochondrial activity by fenofibrate and fasting

2000

Abstract Fenofibrate and fasting are known to regulate several genes involved in lipid metabolism in a similar way. In this study measuring several mitochondrial enzyme activities, we demonstrate that, in contrast to citrate synthase and complex II, cytochrome c oxidase (COX) is a specific target of these two treatments. In mouse liver organelles, Western blot experiments indicated that mitochondrial levels of p43, a mitochondrial T3 receptor, and mitochondrial peroxisome proliferator activated receptor (mt-PPAR), previously described as a dimeric partner of p43 in the organelle, are increased by both fenofibrate and fasting. In addition, in PPARα-deficient mice, this influence was abolishe…

[SDV]Life Sciences [q-bio]Receptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorMitochondria LiverMitochondrionBiochemistryMice0302 clinical medicineFenofibrateStructural BiologyBIOLOGIE CELLULAIRECitrate synthaseFibrateReceptorComputingMilieux_MISCELLANEOUSMice Knockoutchemistry.chemical_classification0303 health sciencesFenofibratebiologyElectron Transport Complex IIFastingPeroxisomeDNA-Binding ProteinsSuccinate Dehydrogenase[SDV] Life Sciences [q-bio]OxidoreductasesDimerizationmedicine.drugPeroxisome proliferator activated receptormedicine.medical_specialtyBiophysicsCitrate (si)-Synthase[INFO] Computer Science [cs]Mitochondrial T3 receptorElectron Transport Complex IV03 medical and health sciencesMultienzyme ComplexesInternal medicineGeneticsmedicineAnimalsCytochrome c oxidase[INFO]Computer Science [cs]MitochondrionMolecular BiologyCrosses Genetic030304 developmental biologyOrganellesLipid metabolismCell BiologyMice Inbred C57BLEndocrinologychemistrybiology.protein030217 neurology & neurosurgeryTranscription Factors
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Menaquinone-dependent succinate dehydrogenase of bacteria catalyzes reversed electron transport driven by the proton potential.

1998

Succinate dehydrogenases from bacteria and archaea using menaquinone (MK) as an electron acceptor (succinate/menaquinone oxidoreductases) contain, or are predicted to contain, two heme-B groups in the membrane-anchoring protein(s), located close to opposite sides of the membrane. All succinate/ubiquinone oxidoreductases, however, contain only one heme-B molecule. In Bacillus subtilis and other bacteria that use MK as the respiratory quinone, the succinate oxidase activity (succinate-->O2), and the succinate/menaquinone oxidoreductase activity were specifically inhibited by uncoupler (CCCP, carbonyl cyanide m-chlorophenylhydrazone) or by agents dissipating the membrane potential (valinomycin…

Carbonyl Cyanide m-Chlorophenyl HydrazoneVitamin KHemeBiochemistryCatalysisMembrane PotentialsElectron TransportValinomycinchemistry.chemical_compoundOxidoreductaseElectrochemistryEnzyme Inhibitorschemistry.chemical_classificationMembrane potentialBinding SitesbiologyBacteriaChemistryElectron Transport Complex IISuccinate dehydrogenaseElectron acceptorbiology.organism_classificationElectron transport chainSuccinate DehydrogenaseBiochemistrybiology.proteinProtonsBacteriaEuropean journal of biochemistry
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2-Methoxyestradiol Affects Mitochondrial Biogenesis Pathway and Succinate Dehydrogenase Complex Flavoprotein Subunit A in Osteosarcoma Cancer Cells.

2017

Background/aim Dysregulation of mitochondrial pathways is implicated in several diseases, including cancer. Notably, mitochondrial respiration and mitochondrial biogenesis are favored in some invasive cancer cells, such as osteosarcoma. Hence, the aim of the current work was to investigate the effects of 2-methoxyestradiol (2-ME), a potent anticancer agent, on the mitochondrial biogenesis of osteosarcoma cells. Materials and methods Highly metastatic osteosarcoma 143B cells were treated with 2-ME separately or in combination with L-lactate, or with the solvent (non-treated control cells). Protein levels of α-syntrophin and peroxisome proliferator-activated receptor gamma, coactivator 1 alph…

0301 basic medicineCancer ResearchSIRT3Protein subunitSDHAMuscle ProteinsAntineoplastic AgentsMolecular Dynamics SimulationBiochemistryElectron Transport Complex IV03 medical and health sciences0302 clinical medicineGeneticSettore BIO/10 - BiochimicaCell Line TumorSirtuin 3CoactivatorGeneticsHumansMolecular BiologyOsteosarcomaOrganelle BiogenesisbiologyEstradiolSettore BIO/16 - Anatomia UmanaChemistryElectron Transport Complex IICalcium-Binding ProteinsMembrane ProteinsPeroxisomeMitochondrial biogenesiPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaCell biology2-MethoxyestradiolMitochondriaSuccinate dehydrogenaseMolecular Docking Simulation030104 developmental biologyMitochondrial biogenesisSettore CHIM/03 - Chimica Generale E Inorganica030220 oncology & carcinogenesisSirtuinCancer cellbiology.proteinResearch ArticleCancer genomicsproteomics
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The oxidation of ubiquinol by the isolated rieske iron-sulfur protein in solution

1990

The pre-steady-state redox reactions of the Rieske iron-sulfur protein isolated from beef heart mitochondria have been characterized. The rates of oxidation by c-type cytochromes is much faster than the rate of reduction by ubiquinols. This enables the monitoring of the oxidation of ubiquinols by the Rieske protein through the steady-state electron transfer to cytochrome c in solution. The pH and ionic strength dependence of this reaction indicate that the ubiquinol anion is the direct reductant of the oxidized cluster of the iron-sulfur protein. The second electron from ubiquinol is diverted to oxygen by the isolated Rieske protein, and forms oxygen radicals that contribute to the steady-s…

Iron-Sulfur ProteinsUbiquinolCytochromeUbiquinoneBiophysicsmacromolecular substancesPhotochemistryBiochemistryRedoxMitochondria HeartElectron Transport Complex IIIElectron transferchemistry.chemical_compoundCytochrome C1AnimalsMolecular BiologybiologyChemistryCytochrome cHydrogen-Ion ConcentrationSolutionsKineticsCoenzyme Q – cytochrome c reductaseRieske proteinbiology.proteinCytochromesCattleOxidation-ReductionArchives of Biochemistry and Biophysics
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mRNA-binding protein tristetraprolin is essential for cardiac response to iron deficiency by regulating mitochondrial function

2018

Cells respond to iron deficiency by activating iron-regulatory proteins to increase cellular iron uptake and availability. However, it is not clear how cells adapt to conditions when cellular iron uptake does not fully match iron demand. Here, we show that the mRNA-binding protein tristetraprolin (TTP) is induced by iron deficiency and degrades mRNAs of mitochondrial Fe/S-cluster-containing proteins, specifically Ndufs1 in complex I and Uqcrfs1 in complex III, to match the decrease in Fe/S-cluster availability. In the absence of TTP, Uqcrfs1 levels are not decreased in iron deficiency, resulting in nonfunctional complex III, electron leakage, and oxidative damage. Mice with deletion of Ttp …

0301 basic medicineCardiac responseCardiac function curveIron-Sulfur ProteinsTristetraprolinMitochondria HeartCell Line03 medical and health sciencesElectron Transport Complex IIIMiceTristetraprolinmedicineAnimalschemistry.chemical_classificationMice KnockoutReactive oxygen speciesMultidisciplinaryNDUFS1MyocardiumNADH DehydrogenaseIron deficiencyIron Deficienciesmedicine.diseaseCell biology030104 developmental biologychemistryPNAS PlusCoenzyme Q – cytochrome c reductaseOxidation-ReductionFunction (biology)
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Altered Mitochondrial Function and Oxidative Stress in Leukocytes of Anorexia Nervosa Patients

2014

ContextAnorexia nervosa is a common illness among adolescents and is characterised by oxidative stress.ObjectiveThe effects of anorexia on mitochondrial function and redox state in leukocytes from anorexic subjects were evaluated.Design and settingA multi-centre, cross-sectional case-control study was performed.PatientsOur study population consisted of 20 anorexic patients and 20 age-matched controls, all of which were Caucasian women.Main outcome measuresAnthropometric and metabolic parameters were evaluated in the study population. To assess whether anorexia nervosa affects mitochondrial function and redox state in leukocytes of anorexic patients, we measured mitochondrial oxygen consumpt…

Anorexia NervosaEating DisordersMitochondrionmedicine.disease_causeBiochemistryElectron Transport Complex IIIchemistry.chemical_compoundLeukocytesMedicine and Health SciencesEnergy-Producing OrganellesMembrane Potential Mitochondrialchemistry.chemical_classificationeducation.field_of_studyMultidisciplinaryQRGlutathioneMitochondriaAnorexia nervosa (differential diagnoses)MedicineFemaleCellular Structures and Organellesmedicine.symptomResearch ArticleAdultmedicine.medical_specialtyAdolescentSciencePopulationContext (language use)AnorexiaBioenergeticsYoung AdultOxygen ConsumptionInternal medicineMental Health and PsychiatrymedicineHumanseducationReactive oxygen speciesElectron Transport Complex Ibusiness.industryBiology and Life SciencesCell BiologyGlutathioneOxidative StressEndocrinologychemistryMitochondrial SizeReactive Oxygen SpeciesbusinessOxidative stressPLoS ONE
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Novel inhibitors of mitochondrial respiratory chain: endoperoxides from the marine tunicate Stolonica socialis.

2001

The Mediterranean tunicate Stolonica socialis contains a new class of powerful cytotoxic acetogenins, generically named stolonoxides. In this paper, which also details the isolation and chemical characterization of a minor component (3a) of the tunicate extract, we report the potent inhibitory activity (IC(50) < 1 microM) of stolonoxides (1a and 3a) on mitochondrial electron transfer. The compounds affect specifically the functionality of complex II (succinate:ubiquinone oxidoreductase) and complex III (ubiquinol:cytochrome C oxidoreductase) in mammalian cells, thereby causing a rapid collapse of the whole energetic metabolism. This result, which differs from the properties of similar known…

UbiquinolMagnetic Resonance SpectroscopyStereochemistryIn Vitro TechniquesFunctional activityElectron Transportchemistry.chemical_compoundElectron Transport Complex IIIMarine Natural ProductOxidoreductaseMultienzyme ComplexesDrug DiscoveryMediterranean SeaAnimalsNADH NADPH OxidoreductasesUrochordataEnzyme InhibitorsFuranschemistry.chemical_classificationElectron Transport Complex IbiologyCytochrome cElectron Transport Complex IISuccinate dehydrogenaseElectron Transport Complex IIMyocardiumDioxolanesMitochondriaPeroxidesSuccinate DehydrogenaseMitochondrial respiratory chainchemistryBiochemistryElectron Transport Complex ICoenzyme Q – cytochrome c reductasebiology.proteinMolecular MedicineCattleStructure ElucidationOxidoreductasesJournal of medicinal chemistry
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Synthesis of N-diisopropyl phosphoryl benzyl-tetrahydroisoquinoline, a new class of mitochondrial complexes I and III inhibitors

2000

The synthesis of N-(O,O-diisopropylphosphoryl)-benzyltetrahydroisoquinoline (3) has been achieved in a 'one pot' procedure from imine (2) and diisopropyl-phosphorochloridate (1) generated in situ (POCl3 + iPrOH). Compound 3 is the first benzyltetrahydroisoquinoline derivative found to be a potent inhibitor of mitochondrial complexes I and III, and therefore it opens a new perspective with this series of compounds as they can be considered as new class of antitumor agents.

Magnetic Resonance SpectroscopyStereochemistryClinical BiochemistryImineRespiratory chainPharmaceutical ScienceBiochemistryChemical synthesisElectron TransportElectron Transport Complex IIIchemistry.chemical_compoundDrug DiscoveryAnimalsNADH NADPH OxidoreductasesEnzyme InhibitorsMolecular BiologyElectron Transport Complex IbiologyBicyclic moleculeTetrahydroisoquinolineOrganic ChemistryNuclear magnetic resonance spectroscopyIsoquinolinesMitochondriachemistryEnzyme inhibitorbiology.proteinMolecular MedicineCattleOxidation-ReductionDerivative (chemistry)Bioorganic &amp; Medicinal Chemistry Letters
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