Search results for "cytochrome c"

showing 10 items of 129 documents

µ-Calpain conversion of antiapoptotic Bfl-1 (BCL2A1) into a prodeath factor reveals two distinct alpha-helices inducing mitochondria-mediated apoptos…

2011

Anti-apoptotic Bfl-1 and pro-apoptotic Bax, two members of the Bcl-2 family sharing a similar structural fold, are classically viewed as antagonist regulators of apoptosis. However, both proteins were reported to be death inducers following cleavage by the cysteine protease µ-calpain. Here we demonstrate that calpain-mediated cleavage of full-length Bfl-1 induces the release of C-terminal membrane active α-helices that are responsible for its conversion into a pro-apoptotic factor. A careful comparison of the different membrane-active regions present in the Bfl-1 truncated fragments with homologous domains of Bax show that helix α5, but not α6, of Bfl-1 induces cell death and cytochrome c r…

Programmed cell deathProtein StructureCancer Treatmentlcsh:MedicineApoptosisMitochondrionCleavage (embryo)BiochemistryProtein Structure SecondaryMinor Histocompatibility AntigensMiceCell Line TumorMolecular Cell BiologyAnimalsHumanslcsh:ScienceProtein InteractionsBiologyMultidisciplinaryMicroscopy ConfocalbiologyCell DeathCalpainCytochrome clcsh:RCytochromes cProteinsCalpainCysteine proteaseCell biologyMitochondriaProto-Oncogene Proteins c-bcl-2OncologyApoptosisbiology.proteinMedicinelcsh:QElectrophoresis Polyacrylamide GelGlobular ProteinsBCL2-related protein A1Research ArticlePloS one
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Coupling Endoplasmic Reticulum Stress to the Cell Death Program

2002

Accumulation of misfolded proteins and alterations in Ca2+ homeostasis in the endoplasmic reticulum (ER) causes ER stress and leads to cell death. However, the signal-transducing events that connect ER stress to cell death pathways are incompletely understood. To discern the pathway by which ER stress-induced cell death proceeds, we performed studies on Apaf-1−/− (null) fibroblasts that are known to be relatively resistant to apoptotic insults that induce the intrinsic apoptotic pathway. While these cells were resistant to cell death initiated by proapoptotic stimuli such as tamoxifen, they were susceptible to apoptosis induced by thapsigargin and brefeldin-A, both of which induce ER stress…

Programmed cell deathThapsigarginbiologyEndoplasmic reticulumCytochrome cIntrinsic apoptosisCell BiologyBiochemistryCell biologychemistry.chemical_compoundchemistryApoptosisbiology.proteinUnfolded protein responseMolecular BiologyCaspaseJournal of Biological Chemistry
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The apoptotic effects and synergistic interaction of sodium butyrate and MG132 in human retinoblastoma Y79 cells

1999

This study deals with the apoptotic effect exerted on human retinoblastoma Y79 cells by both sodium butyrate and an inhibitor of 26S proteasome [z-Leu-Leu-Leu-CHO (MG132)] and their synergistic effect. Exposure to sodium butyrate (1-4 mM) induced an accumulation of cells in the G2-M phase that was already visible after 24 h of treatment, when morphological and biochemical signs of apoptosis appeared only in a small number of cells (5-10%). Thereafter, the apoptotic effects increased progressively with slow kinetics, reaching a maximum after 72 h of exposure, when they concerned a large fraction of cells (>75% with 4 mM sodium butyrate). Sodium butyrate stimulated the conversion of procaspas…

Proteasome Endopeptidase ComplexTime FactorsLeupeptinsApoptosisCytochrome c GroupCysteine Proteinase InhibitorsProto-Oncogene Proteins c-mycTumor Cells CulturedHumanssodium butyrateLamin Type BCaspase 3Cell CycleNF-kappa BRetinoblastomaNuclear ProteinsFlow CytometryLaminsMitochondriaButyratesKineticsCaspasesI-kappa B ProteinsPoly(ADP-ribose) PolymerasesTumor Suppressor Protein p53Peptide Hydrolases
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Peptides Derived from the Transmembrane Domain of Bcl-2 Proteins as Potential Mitochondrial Priming Tools

2014

The Bcl-2 family of proteins is crucial for apoptosis regulation. Members of this family insert through a specific C-terminal anchoring trans membrane domain (TMD) in the mitochondrial outer membrane where they hierarchically interact to determine cell fate. While the mitochondrial membrane has been proposed to actively participate in these protein protein interactions, the influence of the TMD in the membrane-mediated interaction is poorly understood. Synthetic peptides (TMD-pepts) corresponding to the putative TMD of antiapoptotic (Bcl-2, Bcl-xL, Bcl-w, and Mcl-1) and pro-apoptotic (Bax, Bak) members were synthesized and characterized. TMD-pepts bound more efficiently to mitochondria-like…

Protein ConformationMolecular Sequence DataCell fate determinationBiochemistryHumansCell LineageAmino Acid SequenceInner mitochondrial membranebiologyChemistryCircular DichroismCytochrome cGeneral MedicineMolecular biologyMitochondriaCell biologystomatognathic diseasesTransmembrane domainMembraneProto-Oncogene Proteins c-bcl-2Cell cultureApoptosisbiology.proteinMolecular MedicinePeptidesBacterial outer membranehuman activitiesHeLa Cells
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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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Regional differences of substrate oxidation capacity in rat hearts: effects of extra load and endurance training.

1990

Male rats, aged 17 weeks at the end of experiments, were divided into four groups. Two groups lived in normal cage conditions with or without extra load (20% of the body weight) and two groups were trained by running with or without extra load for 8 weeks. Oxidation rates of succinate, glutamate + malate, palmitoylcarnitine, and pyruvate, and the activities of lactate dehydrogenase, citrate synthase, isocitrate dehydrogenase and cytochrome oxidase were measured in homogenates of the right ventricle and in those of the subendocardial and subepicardial layers of the left ventricle. Oxidation rates of succinate and palmitoylcarnitine tended to be higher in the subendocardium than in the subepi…

Pyruvate decarboxylationMalemedicine.medical_specialtyPhysiologyPhysical exerciseCitrate (si)-Synthasechemistry.chemical_compoundEndurance trainingPhysiology (medical)Lactate dehydrogenaseInternal medicinePhysical Conditioning AnimalmedicineCitrate synthaseCytochrome c oxidaseAnimalsPalmitoylcarnitinebiologyMusclesMyocardiumBody WeightRats Inbred StrainsRatsmedicine.anatomical_structureEndocrinologychemistryVentriclebiology.proteinPhysical EnduranceCardiology and Cardiovascular MedicineEnergy MetabolismOxidation-ReductionBasic research in cardiology
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Red wine extract prevents neuronal apoptosis in vitro and reduces mortality of transgenic mice.

2007

In this work, we have investigated the effects of nutritional antioxidants as antidegenerative agents on glutamate-induced apoptosis in primary cultures of cerebellar granule neurons (CGNs). Glutamate-induced apoptosis is also associated with intracellular [Ca(2+)]i overload, generation of reactive oxygen species (ROS), depression of cell energy metabolism, cytochrome c release, and increase in caspase-3 activity. Pretreatment (3 h) with red wine extract (5 microg/mL) and ascorbic acid (30 microM) blocks glutamate-induced apoptosis in CGNs. In vivo experiments carried out on transgenic mice expressing the human mutated Cu, Zn superoxide dismutase (SOD1) G93A (mSOD1(G93A)) show that mice fed…

SOD1Glutamic AcidApoptosisMice TransgenicWinePharmacologyBiologycerebellar granule cells • apoptosis • lyophilized red wine • ASL • mSOD1G93AGeneral Biochemistry Genetics and Molecular BiologyMiceSuperoxide Dismutase-1History and Philosophy of ScienceIn vivoAnimalsHumansCells Culturedchemistry.chemical_classificationWineNeuronsReactive oxygen speciesCaspase 3Superoxide DismutaseGeneral NeuroscienceCytochrome cCytochromes cAscorbic acidSurvival AnalysisNeuroprotective AgentschemistryBiochemistryApoptosisbiology.proteinCalciumReactive Oxygen SpeciesIntracellular
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Solid-phase extraction based on ground methacrylate monolith modified with gold nanoparticles for isolation of proteins

2015

In this study, a novel polymeric material functionalized with gold nanoparticles (AuNPs) was prepared as solid-phase extraction (SPE) sorbent for isolation of proteins. The sorbent was synthesized from a powdered poly(glycidyl-co-ethylene dimethacrylate) monolith, and modified with ammonia, followed by immobilization of AuNPs on the pore surface of the material. To evaluate the performance of this SPE support, proteins were selected as test solutes, being the extraction conditions and other parameters (loading capacity and regenerative ability of sorbent) established. The results indicated that this sorbent could be employed to selectively capture proteins according to their pI, on the basi…

SorbentMetal Nanoparticles02 engineering and technologyMethacrylate01 natural sciencesBiochemistryAnalytical ChemistryEnvironmental ChemistrySolid phase extractionMonolithBovine serum albuminSpectroscopygeographyChromatographygeography.geographical_feature_categorybiologyChemistryCytochrome cSolid Phase Extraction010401 analytical chemistryExtraction (chemistry)Proteins021001 nanoscience & nanotechnology0104 chemical sciencesColloidal goldMicroscopy Electron Scanningbiology.proteinMethacrylatesElectrophoresis Polyacrylamide GelGold0210 nano-technologyAnalytica Chimica Acta
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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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Ferricytochrome c encapsulated in silica hydrogels: correlation between active site dynamics and solvent structure.

2003

Ferricytochrome c encapsulated in silica hydrogels has been prepared by the sol-gel technique following, with some modifications, the procedure originally developed by Ellerby et al. (Science 255 1113 (1992)). A suitable preparation of hydrogels enables having both 'wet' and 'dry' samples. Wet samples have a high water content: as the temperature is lowered below approximately 260 K, water freezes and the samples crack. On the contrary, dry samples have a low water content (hydration h approximately equal 0.35): in these conditions water does not freeze even at cryogenic temperatures and the samples remain transparent and non-cracking. The dynamics of ferricytochrome c and its dependence on…

Time FactorsAbsorption spectroscopySilicon dioxideDrug CompoundingAnalytical chemistryBiophysicsSilica GelCapsulesCytochrome c GroupSpectrum Analysis RamanBiochemistrychemistry.chemical_compoundDrug StabilityFreezingAnimalsHorsesWater contentBinding SitesbiologySilica gelSpectrum AnalysisOrganic ChemistryTemperatureActive siteWaterHydrogelsAtmospheric temperature rangeSilicon DioxideSolventKineticschemistrySelf-healing hydrogelsbiology.proteinSolventsBiophysical chemistry
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