Search results for "Mitochondrial apoptosis-induced channel"

showing 4 items of 4 documents

Induction of Mitochondrial Changes Associated with Oxidative Stress on Very Long Chain Fatty Acids (C22:0, C24:0, or C26:0)-Treated Human Neuronal Ce…

2012

In Alzheimer's disease, lipid alterations point towards peroxisomal dysfunctions. Indeed, a cortical accumulation of saturated very long chain fatty acids (VLCFAs: C22:0, C24:0, C26:0), substrates for peroxisomalβ-oxidation, has been found in Alzheimer patients. This study was realized to investigate the effects of VLCFAs at the mitochondrial level since mitochondrial dysfunctions play crucial roles in neurodegeneration. On human neuronal SK-NB-E cells treated with C22:0, C24:0, or C26:0 (0.1–20 μM; 48 h), an inhibition of cell growth and mitochondrial dysfunctions were observed by cell counting with trypan blue, MTT assay, and measurement of mitochondrial transmembrane potential (Δψm) with…

AgingArticle SubjectMitochondrionBiologymedicine.disease_causeBiochemistryMitochondrial apoptosis-induced channelchemistry.chemical_compoundSuperoxidesCell Line TumormedicineHumanslcsh:QH573-671Cell ShapeCell ProliferationMembrane Potential MitochondrialNeuronslcsh:CytologySuperoxideFatty AcidsNeurodegenerationCell BiologyGeneral MedicinePeroxisomeFlow Cytometrymedicine.diseaseMolecular biologyMitochondriaCell biologyOxidative StressProtein SubunitsMicroscopy FluorescencechemistryMultiprotein ComplexesDNAJA3ATP–ADP translocaseOxidative stressResearch ArticleOxidative Medicine and Cellular Longevity
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The thiol switch C684 in Mitofusin-2 mediates redox-induced alterations of mitochondrial shape and respiration

2017

Mitofusin-2 (MFN2) is a GTPase in the outer mitochondrial membrane involved in the regulation of mitochondrial fusion and bioenergetics. MFN2 also plays a role in mitochondrial fusion induced by changes in the intracellular redox state. Adding oxidized glutathione (GSSG), the core cellular stress indicator, to mitochondrial preparations stimulates mitochondrial fusion by inducing disulphide bond-mediated oligomer formation of MFN2 and its homolog MFN1 which involve cysteine 684 (C684) of MFN2. Mitochondrial hyperfusion represents an adaptive stress response that confers transient protection by increasing mitochondrial ATP production but how this depends on the thiol switch C684 in MFN2 has …

Mice Knockout0301 basic medicineCell RespirationMFN2Cell BiologyOxidative phosphorylationMitochondrionBiologyMitochondrial apoptosis-induced channelGTP PhosphohydrolasesMitochondriaCell biologyMice03 medical and health sciencesCellular and Molecular NeuroscienceMitofusin-2030104 developmental biologymitochondrial fusionAnimalsMFN1Sulfhydryl CompoundsATP–ADP translocaseCell ShapeOxidation-ReductionCells CulturedNeurochemistry International
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Redox signaling (cross-talk) from and to mitochondria involves mitochondrial pores and reactive oxygen species

2010

This review highlights the important role of redox signaling between mitochondria and NADPH oxidases. Besides the definition and general importance of redox signaling, the cross-talk between mitochondrial and Nox-derived reactive oxygen species (ROS) is discussed on the basis of 4 different examples. In the first model, angiotensin-II is discussed as a trigger for NADPH oxidase activation with subsequent ROS-dependent opening of mitochondrial ATP-sensitive potassium channels leading to depolarization of mitochondrial membrane potential followed by mitochondrial ROS formation and respiratory dysfunction. This concept was supported by observations that ethidium bromide-induced mitochondrial d…

Mitochondrial ROSAgingPotassium ChannelsMyocytes Smooth MuscleBiophysicsIn Vitro TechniquesMitochondrionmedicine.disease_causeMitochondrial Membrane Transport ProteinsModels BiologicalMitochondrial apoptosis-induced channelBiochemistryPeroxynitritechemistry.chemical_compoundmedicineAnimalsHumansMitochondrionFeedback PhysiologicalNADPH oxidasebiologyNADPH oxidaseMitochondrial Permeability Transition PoreSuperoxideAngiotensin IINADPH OxidasesSuperoxideNitric oxideCell BiologyReactive Nitrogen SpeciesMitochondriaCell biologyOxidative StressOxidative protein modificationchemistryMitochondrial permeability transition poreRedox regulationNOX1Hypertensionbiology.proteinReactive Oxygen SpeciesOxidation-ReductionOxidative stressSignal TransductionBiochimica et Biophysica Acta (BBA) - Bioenergetics
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Conformational control of Bax localization and apoptotic activity by Pro168.

2004

In healthy cells, Bax resides inactive in the cytosol because its COOH-terminal transmembrane region (TMB) is tucked into a hydrophobic pocket. During apoptosis, Bax undergoes a conformational change involving NH2-terminal exposure and translocates to mitochondria to release apoptogenic factors. How this process is regulated remains unknown. We show that the TMB of Bax is both necessary and sufficient for mitochondrial targeting. However, its availability for targeting depends on Pro168 located within the preceding loop region. Pro168 mutants of Bax lack apoptotic activity, cannot rescue the apoptosis-resistant phenotype of Bax/Bak double knockout cells, and are retained in the cytosol even…

Models MolecularConformational changeProlineCell SurvivalProtein ConformationMutantMolecular Sequence DataApoptosisMitochondrionMitochondrial apoptosis-induced channelArticleCell Line03 medical and health sciencesMice0302 clinical medicineBcl-2-associated X proteinProto-Oncogene ProteinsAnimalsHumansAmino Acid Sequence030304 developmental biologybcl-2-Associated X Proteinapoptosis; Bcl-2 family; NH2-terminal exposure; mitochondria; targeting0303 health sciencesbiologyMembrane ProteinsCell BiologyPeptide FragmentsCell biologyTransport proteinMitochondriaCytosolProtein Transportbcl-2 Homologous Antagonist-Killer ProteinProto-Oncogene Proteins c-bcl-2030220 oncology & carcinogenesisbiology.proteinBcl-2 Homologous Antagonist-Killer ProteinHeLa CellsThe Journal of cell biology
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