Search results for " cytochrome c"

showing 10 items of 22 documents

Bruce/apollon promotes hippocampal neuron survival and is downregulated by kainic acid

2005

Prolonged or excess stimulation of excitatory amino acid receptors leads to seizures and the induction of excitotoxic nerve cell injury. Kainic acid acting on glutamate receptors produces degeneration of vulnerable neurons in parts of the hippocampus and amygdala, but the exact mechanisms are not fully understood. We have here investigated whether the anti-apoptotic protein Bruce is involved in kainic acid-induced neurodegeneration. In the rat hippocampus and cortex, Bruce was exclusively expressed by neurons. The levels of Bruce were rapidly downregulated by kainic acid in hippocampal neurons as shown both in vivo and in cell culture. Caspase-3 was activated in neurons exhibiting low level…

MaleKainic acidCell SurvivalBiophysicsExcitotoxicityBruce/apollon Hippocampus Kainic acid Excitotoxicity Neuronal death Caspase-3 Cytochrome cDown-RegulationHippocampusStimulationBiologyHippocampal formationmedicine.disease_causeHippocampusBiochemistrychemistry.chemical_compoundDownregulation and upregulationmedicineAnimalsRats WistarMolecular BiologyCells CulturedNeuronsKainic AcidDose-Response Relationship DrugNeurodegenerationGlutamate receptorCell Biologymedicine.diseaseRatsCell biologynervous systemchemistryBiochemistryUbiquitin-Conjugating Enzymeshuman activitiescirculatory and respiratory physiology
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Imeglimin Normalizes Glucose Tolerance and Insulin Sensitivity and Improves Mitochondrial Function in Liver of a High-Fat, High-Sucrose Diet Mice Mod…

2015

International audience; Imeglimin is the first in a new class of oral glucose-lowering agents currently in phase 2b development. Although imeglimin improves insulin sensitivity in humans, the molecular mechanisms are unknown. This study used a model of 16-week high-fat, high-sucrose diet (HFHSD) mice to characterize its antidiabetic effects. Six-week imeglimin treatment significantly decreased glycemia, restored normal glucose tolerance, and improved insulin sensitivity without modifying organs, body weights, and food intake. This was associated with an increase in insulin-stimulated protein kinase B phosphorylation in the liver and muscle. In liver mitochondria, imeglimin redirects substra…

Malemedicine.medical_specialtyMale Animals Mice Inbred C57BL Insulin Resistance/*physiology Diet High-Fat/adverse effects Hypoglycemic Agents/*therapeutic use Liver/*drug effects/*metabolism Mitochondria/*drug effects/*metabolism Triazines/*therapeutic useImegliminMitochondria/*drug effects/*metabolismEndocrinology Diabetes and Metabolism[SDV]Life Sciences [q-bio]High-Fat/adverse effectsBiologyMitochondrionDiet High-Fatmedicine.disease_causeInbred C57BLchemistry.chemical_compoundMiceLipid oxidationInternal medicineInternal MedicinemedicineHypoglycemic Agents/*therapeutic useHypoglycemic AgentsAnimalsProtein kinase BBeta oxidationComputingMilieux_MISCELLANEOUS2. Zero hungerchemistry.chemical_classificationReactive oxygen speciesTriazines/*therapeutic useTriazinesMitochondria3. Good healthDietMice Inbred C57BL[SDV] Life Sciences [q-bio]EndocrinologyLiver/*drug effects/*metabolismLiverchemistryInsulin Resistance/*physiologyCoenzyme Q – cytochrome c reductaseInsulin ResistanceOxidative stress
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Mitochondrial myopathy with lactic acidosis and deficient activity of muscle succinate cytochrome-c-oxidoreductase

1984

A male infant had severe muscular hypotonia from birth. Recurrent vomiting with dehydration and severe metabolic acidosis complicated the course. Elevated lactate (up to 12.3 mmol/l; n less than 2), pyruvate (0.4 mmol/l; n less than 0.05) and alanine levels were found in serum with an abnormal lactate/pyruvate ratio (greater than 30; n less than 15). In urine the concentrations of lactate, pyruvate, alanine and of several intermediates of the citric acid cycle were increased. In muscle, numerous disseminated "ragged red fibres" were found by light microscopy; muscle fibres were found to contain subsarcolemmal aggregates of mitochondria, lipid droplets and glycogen by electromicroscopical me…

Malemedicine.medical_specialtySevere muscular hypotoniaRespiratory chainMitochondria Livermacromolecular substancesMitochondrionBiology03 medical and health scienceschemistry.chemical_compound0302 clinical medicineMuscular DiseasesMitochondrial myopathy030225 pediatricsInternal medicinemedicineHumansGlycogenMusclesInfantMetabolic acidosismedicine.diseaseMitochondriaMitochondria Muscle3. Good healthCitric acid cycleEndocrinologyBiochemistrychemistryLactic acidosisPediatrics Perinatology and Child HealthLactatesSuccinate Cytochrome c OxidoreductaseAcidosisOxidoreductases030217 neurology & neurosurgeryEuropean Journal of Pediatrics
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Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering

2008

We demonstrate tracking of protein structural changes with time-resolved wide-angle X-ray scattering (TR-WAXS) with nanosecond time resolution. We investigated the tertiary and quaternary conformational changes of human hemoglobin under nearly physiological conditions triggered by laser-induced ligand photolysis. We also report data on optically induced tertiary relaxations of myoglobin and refolding of cytochrome c to illustrate the wide applicability of the technique. By providing insights into the structural dynamics of proteins functioning in their natural environment, TR-WAXS complements and extends results obtained with time-resolved optical spectroscopy and X-ray crystallography.

Materials scienceProtein ConformationCrystallography X-RayBiochemistrySensitivity and SpecificityArticlechemistry.chemical_compoundHemoglobinsProtein structureScattering RadiationSpectroscopyWide-angle X-ray scatteringMolecular Biologyprotein dynamics conformational changes hemoglobin myoglobin cytochrome cScatteringMyoglobinX-RaysResolution (electron density)Cytochromes cCell BiologyNanosecondMyoglobinchemistryChemical physicsProtein quaternary structuresense organsBiotechnology
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Proteins participating to the post-transcriptional regulation of the mitochondrial cytochrome c oxidase subunit IV via elements located in the 3′UTR

2009

Abstract In developing rat brain cytochrome c oxidase subunit IV (COXIV) expression is also regulated at post-transcriptional level and two 3′UTR-COXIV RNA-binding factors have been identified. Here, we report the enrichment and identification of the factors from just born rat brains by affinity chromatography of biotinylated 3′UTR-COXIV RNA–protein complexes on streptavidin-conjugated paramagnetic particles. We successfully isolated two main proteins of about 86 and 42 kDa, whose sequences were highly attributable to Hsp90 and Actin. The purified proteins maintain RNA-binding ability and specificity for COXIV messenger and, interacting with the 3′UTR, then could negatively modulate mRNA tr…

Protein subunitRNA-binding proteinMitochondrionChromatography AffinityElectron Transport Complex IVMitochondrial ProteinsRats Sprague-DawleySequence Analysis ProteinSerineAnimalsCytochrome c oxidaseHSP90 Heat-Shock ProteinsPhosphorylationPost-transcriptional regulation RNA-binding proteins Mitochondria Cytochrome c oxidase COXIV 3'UTR3' Untranslated RegionsMolecular BiologyPost-transcriptional regulationMessenger RNAbiologyThree prime untranslated regionBrainRNA-Binding ProteinsTranslation (biology)Cell BiologyActinsRatsMolecular WeightAnimals NewbornGene Expression RegulationBiochemistrybiology.proteinMolecular MedicineProtein BindingMitochondrion
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Membrane D-lactate oxidase in Zymomonas mobilis: evidence for a branched respiratory chain.

1998

Respiratory chain composition of the ethanol-producing bacterium Zymomonas mobilis was studied. Its membrane D-lactate oxidase was characterised. With NADH, but not D-lactate as substrate, a cytochrome o-like component was seen in CO difference spectra. Chlorpromazine specifically inhibited reduction of cytochrome d, while myxothiazol eliminated the cytochrome o-like features in CO difference spectra. It is suggested that electrons from NADH are distributed between branches terminated by the cytochrome o-like component, cytochrome a, and cytochrome d. With D-lactate, electrons are transported to cytochrome a, or an unidentified CN(-)-sensitive oxidase, and cytochrome d.

StereochemistryChlorpromazineMicrobiologyMixed Function OxygenasesElectron Transportchemistry.chemical_compoundOxygen ConsumptionCytochrome C1Multienzyme ComplexesGeneticsCytochrome c oxidaseNADH NADPH OxidoreductasesLactic AcidMolecular BiologyZymomonasbiologyMyxothiazolCytochrome b6f complexCytochrome bCytochrome cCytochrome dNADAerobiosisThiazolesBiochemistrychemistrySpectrophotometryCoenzyme Q – cytochrome c reductasebiology.proteinCytochromesMethacrylatesOxidation-ReductionFEMS microbiology letters
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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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Effects of vitamin A deficiency on mitochondrial function in rat liver and heart.

2000

The aim of this study was to investigate comparative effects of vitamin A deficiency on respiratory activity and structural integrity in liver and heart mitochondria. Male rats were fed a liquid control diet (control rats) or a liquid vitamin A-deficient diet (vitamin A-deficient rats) for 50 days. One group of vitamin-A deficient rats was refed a control diet for 15 days (vitamin A-recovered rats). To assess the respiratory function of mitochondria the contents of coenzyme Q (ubiquinone, CoQ), cytochrome c and the activities of the whole electron transport chain and of each of its respiratory complexes were evaluated. Chronic vitamin A deficiency promoted a significant increase in the endo…

VitaminMalemedicine.medical_specialtyUbiquinoneRespiratory chainMedicine (miscellaneous)Cytochrome c GroupMitochondria LiverMitochondria HeartElectron Transportchemistry.chemical_compoundRetinoidsInternal medicinemedicineAnimalsVitamin ERespiratory functionNutrition and DieteticsbiologyVitamin A DeficiencyCytochrome cRetinolmedicine.diseaseRatsVitamin A deficiencyEndocrinologyMitochondrial respiratory chainchemistryCoenzyme Q – cytochrome c reductasebiology.proteinThe British journal of nutrition
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A Deficiency in Respiratory Complex I in Heart Mitochondria from Vitamin A-Deficient Rats Is Counteracted by an Increase in Coenzyme Q

1997

Defects of NADH:coenzyme Q oxidoreductase (complex I) of mitochondria have been described in many congenital and acquired diseases. Administration of coenzyme Q (CoQ, ubiquinone) has been shown to benefit patients with some of these diseases. However, the mechanisms by which CoQ exerts the therapeutic effects are not clearly understood. A reason could be the lack of saturation of CoQ, in kinetic terms, for complex I activity. However, this hypothesis has not been proved in vivo because of the difficulty to incorporate CoQ into the mitochondrial membranes. We have found a deficiency in respiratory complex I in heart mitochondria from vitamin A-deficient rats which was accompanied by high CoQ…

Vitaminmedicine.medical_specialtyAcquired diseasesUbiquinoneBiophysicsMitochondrionBiologyBiochemistryMitochondria Heartchemistry.chemical_compoundRespiratory Complex IOxidoreductaseInternal medicinemedicineAnimalsNADH NADPH OxidoreductasesMolecular Biologychemistry.chemical_classificationElectron Transport Complex IVitamin A Deficiencyfood and beveragesCell BiologyRatsElectron transfer rateKineticsEndocrinologychemistryCoenzyme Q – cytochrome c reductaseBiochemical and Biophysical Research Communications
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Structure of the Zymomonas mobilis respiratory chain: oxygen affinity of electron transport and the role of cytochrome c peroxidase

2014

The genome of the ethanol-producing bacterium Zymomonas mobilis encodes a bd-type terminal oxidase, cytochrome bc 1 complex and several c-type cytochromes, yet lacks sequences homologous to any of the known bacterial cytochrome c oxidase genes. Recently, it was suggested that a putative respiratory cytochrome c peroxidase, receiving electrons from the cytochrome bc 1 complex via cytochrome c 552, might function as a peroxidase and/or an alternative oxidase. The present study was designed to test this hypothesis, by construction of a cytochrome c peroxidase mutant (Zm6-perC), and comparison of its properties with those of a mutant defective in the cytochrome b subunit of the bc 1 complex (Zm…

ZymomonasbiologyCytochrome bc1Cytochrome c peroxidaseCytochrome cCytochrome dCytochrome-c PeroxidaseMicrobiologyMolecular biologyStandardElectron TransportOxygenBiochemistryCytochrome C1Coenzyme Q – cytochrome c reductasebiology.proteinCytochrome c oxidaseOxidoreductasesPhysiology and BiochemistryGene DeletionPeroxidaseMicrobiology
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