Search results for "mitochondrion"

showing 10 items of 491 documents

Effects of a high-fat diet on energy metabolism and ROS production in rat liver.

2011

International audience; BACKGROUND & AIMS: A high-fat diet affects liver metabolism, leading to steatosis, a complex disorder related to insulin resistance and mitochondrial alterations. Steatosis is still poorly understood since diverse effects have been reported, depending on the different experimental models used. METHODS: We hereby report the effects of an 8 week high-fat diet on liver energy metabolism in a rat model, investigated in both isolated mitochondria and hepatocytes. RESULTS: Liver mass was unchanged but lipid content and composition were markedly affected. State-3 mitochondrial oxidative phosphorylation was inhibited, contrasting with unaffected cytochrome content. Oxidative…

Mitochondrial ROSMaleTranscription GeneticMESH : Reactive Oxygen SpeciesMitochondria LiverMESH : HepatocytesMitochondrionOxidative PhosphorylationMESH: Hepatocytes0302 clinical medicineMESH: Membrane Potential MitochondrialCitrate synthaseMESH: AnimalsBeta oxidationMESH : Electron Transport2. Zero hungerMembrane Potential Mitochondrial0303 health sciencesMESH : RatsAdenine nucleotide translocatorMESH: Energy MetabolismMESH: Reactive Oxygen SpeciesLipidsBiochemistryLiverMESH: Dietary FatsMitochondrial matrix030220 oncology & carcinogenesisBody CompositionMESH : Oxidative PhosphorylationATP–ADP translocaseMESH: Mitochondria LiverMESH: RatsMESH : Body CompositionMESH : MaleOxidative phosphorylationBiologyMESH : Rats WistarElectron Transport03 medical and health sciencesMESH: Oxidative Phosphorylation[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyAnimals[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyRats WistarMESH: Electron Transport[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular Biology030304 developmental biologyHepatologyMESH: Transcription GeneticMESH : Transcription GeneticMESH : LiverMESH : LipidsMESH: Body CompositionMESH: Rats WistarMESH: LipidsDietary FatsMESH: MaleRatsMESH : Energy MetabolismMESH : Membrane Potential MitochondrialMESH : Mitochondria Liverbiology.proteinHepatocytesMESH : AnimalsEnergy MetabolismReactive Oxygen SpeciesMESH : Dietary FatsMESH: Liver
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Nitroglycerine causes mitochondrial reactive oxygen species production: In vitro mechanistic insights

2007

Background Nitroglycerine (GTN) is an organic nitrate that has been used for more than 100 years. Despite its widespread clinical use, several aspects of the pharmacology of GTN remain elusive. In a recent study, the authors of the present study showed that GTN causes opening of the mitochondrial permeability transition pore (mPTP) and mitochondrial production of reactive oxygen species (ROS). Objective In the present study, it was tested whether GTN-induced ROS production depends on mitochondrial potassium ATP-dependent channel or mPTP opening, and/or GTN biotransformation. Methods and results Isolated rat heart mitochondria were incubated with succinate (a substrate for complex II) and GT…

Mitochondrial ROSPotassium ChannelsVasodilator AgentsRespiratory chainIn Vitro TechniquesPharmacologyMitochondrionMitochondrial Membrane Transport ProteinsMitochondria HeartToxicologyNitroglycerinchemistry.chemical_compoundMitochondrial membrane transport proteinKATP ChannelsAnimalsMedicineRats WistarBiotransformationchemistry.chemical_classificationReactive oxygen speciesbiologyMitochondrial Permeability Transition Porebusiness.industryMPTPPotassium channelRatsBasic ResearchchemistryMitochondrial permeability transition poreModels Animalcardiovascular systembiology.proteinReactive Oxygen SpeciesCardiology and Cardiovascular Medicinebusinesscirculatory and respiratory physiologyCanadian Journal of Cardiology
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Mitochondrial Alterations and Enhanced Human Leukocyte/Endothelial Cell Interactions in Type 1 Diabetes

2020

Type 1 diabetes has been associated with oxidative stress. This study evaluates the rates of oxidative stress, mitochondrial function, leukocyte&ndash

Mitochondrial ROScardiovascular riskmedicine.medical_specialtyendotheliumtype 1 diabeteslcsh:Medicine030209 endocrinology & metabolism030204 cardiovascular system & hematologyMitochondrionmedicine.disease_causeArticleProinflammatory cytokineSuperoxide dismutase03 medical and health sciences0302 clinical medicineInternal medicinemedicinechemistry.chemical_classificationReactive oxygen speciesbiologyCell adhesion moleculebusiness.industrylcsh:RGeneral MedicinemitochondriaEndocrinologychemistryinflammationMyeloperoxidasebiology.proteinbusinessOxidative stressJournal of Clinical Medicine
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Mitochondrial Oxidative Stress, Mitochondrial DNA Damage and Their Role in Age-Related Vascular Dysfunction

2015

The prevalence of cardiovascular diseases is significantly increased in the older population. Risk factors and predictors of future cardiovascular events such as hypertension, atherosclerosis, or diabetes are observed with higher frequency in elderly individuals. A major determinant of vascular aging is endothelial dysfunction, characterized by impaired endothelium-dependent signaling processes. Increased production of reactive oxygen species (ROS) leads to oxidative stress, loss of nitric oxide (•NO) signaling, loss of endothelial barrier function and infiltration of leukocytes to the vascular wall, explaining the low-grade inflammation characteristic for the aged vasculature. We here disc…

Mitochondrial ROSmedicine.medical_specialtyMitochondrial DNADNA RepairInflammationReviewBiologyMitochondrionmedicine.disease_causeDNA MitochondrialCatalysisAntioxidantsNitric oxideInorganic Chemistrylcsh:Chemistrychemistry.chemical_compoundInternal medicinemedicineAnimalsHumansPhysical and Theoretical ChemistryEndothelial dysfunctionMolecular Biologylcsh:QH301-705.5Spectroscopychemistry.chemical_classificationReactive oxygen speciesmitochondrial oxidative stressOrganic Chemistryagingmitochondrial DNA damageGeneral Medicinevascular dysfunctionmedicine.diseaseComputer Science ApplicationsMitochondriaOxidative StressEndocrinologyBiochemistrychemistrylcsh:Biology (General)lcsh:QD1-999Cardiovascular Diseasesmedicine.symptomReactive Oxygen SpeciesOxidative stressDNA DamageInternational Journal of Molecular Sciences
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Permeabilization of the Outer Mitochondrial Membrane by Bcl-2 Proteins

2010

The proteins of the Bcl-2 family regulate the release of the apoptotic factors from mitochondria during apoptosis, a key event in physiological cell death. Although their molecular mechanisms remain unclear, the Bcl-2 proteins have been proposed to directly control the permeability of the outer mitochondrial membrane by pore formation. Indeed, they share structural features with the pore forming domains of some bacterial toxins and they can give rise to proteolipidic pores in model membranes. The complex level of regulation needed to decide the fate of the cell is achieved by an intricate interaction network between different members of the family. Current models consider multiple parallel …

Mitochondrial membrane transport proteinMembranebiologyTranslocase of the outer membraneBcl-2 familyTranslocase of the inner membranebiology.proteinMitochondrionMitochondrial carrierBacterial outer membraneCell biology
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Lack of GDAP1 induces neuronal calcium and mitochondrial defects in a knockout mouse model of Charcot-Marie-tooth neuropathy

2015

27 páginas, 9 figuras.

Mitochondrial proteinCancer Researchlcsh:QH426-470Nerve Tissue ProteinsBiologyMitochondrionCharcot-Marie-Tooth diseaseGDAP1 geneMiceGeneticsAutophagyAnimalsCalcium SignalingMolecular BiologyGenetics (clinical)Ecology Evolution Behavior and SystematicsCytoskeletonCalcium signalingGeneticsVoltage-dependent calcium channelEndoplasmic reticulumAutophagyBiología y Biomedicina / BiologíaAxonsCell biologyMitochondriaMitochondrialMice Inbred C57BLAlpha tubulinlcsh:Geneticsmitochondrial fusionKnockout mouseMitochondrial fissionCalcium ChannelsAnimal cellGene DeletionResearch Article
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Yeast Translation Elongation Factor eIF5A Expression Is Regulated by Nutrient Availability through Different Signalling Pathways

2020

Translation elongation factor eIF5A binds to ribosomes to promote peptide bonds between problematic amino acids for the reaction like prolines. eIF5A is highly conserved and essential in eukaryotes, which usually contain two similar but differentially expressed paralogue genes. The human eIF5A-1 isoform is abundant and implicated in some cancer types

MitochondrionBiotecnologialcsh:ChemistryPeptide Initiation FactorsGene Expression Regulation Fungalmitochondrial respirationGene expressionExpressió genèticaHap1Protein Isoformshemelcsh:QH301-705.5SpectroscopyChemistryRNA-Binding ProteinsTranslation (biology)Iron DeficienciesGeneral MedicineTORAerobiosisUp-RegulationComputer Science ApplicationsCell biologySnf1EIF5ASignal TransductionGene isoformSaccharomyces cerevisiae ProteinsIronCitric Acid CycleDown-RegulationSaccharomyces cerevisiaeMechanistic Target of Rapamycin Complex 1Models BiologicalArticleCatalysisInorganic ChemistryeIF5APhysical and Theoretical ChemistryMolecular BiologyTranscription factorGeneLysineOrganic ChemistryNutrientsMetabolismCarbonMetabolic Flux AnalysisGlucoselcsh:Biology (General)lcsh:QD1-999Fermentationgene expressionInternational Journal of Molecular Sciences
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Astrocytes Protect Neurons from Aβ1-42 Peptide-Induced Neurotoxicity Increasing TFAM and PGC-1 and Decreasing PPAR-γ and SIRT-1

2015

One of the earliest neuropathological events in Alzheimer's disease is accumulation of astrocytes at sites of Aβ1-42 depositions. Our results indicate that Aβ1-42 toxic peptide increases lipid peroxidation, apoptosis and cell death in neurons but not in astrocytes in primary culture. Aβ1-42-induced deleterious neuronal effects are not present when neurons and astrocytes are mixed cultured. Stimulation of astrocytes with toxic Aβ1-42 peptide increased p-65 and decreased IκB resulting in inflammatory process. In astrocytes Aβ1-42 decreases protein expressions of sirtuin 1 (SIRT-1) and peroxisome proliferator-activated receptor γ (PPAR-γ) and over-expresses peroxisome proliferator-activated re…

MnSODProgrammed cell deathPPAR-γPeroxisome proliferator-activated receptorMitochondrionBiologyBioinformaticsmedicine.disease_causeAlzheimer's DiseaseNeurologiaPGC-1Sirtuin 1medicineAnimalsTFAMCells Culturedchemistry.chemical_classificationNeuronsAmyloid beta-PeptidesCell DeathSirtuin 1Caspase 3Superoxide DismutaseNeurotoxicityTranscription Factor RelAGeneral MedicineTFAMmedicine.diseasePeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaCoculture TechniquesPeptide FragmentsCell biologyMitochondriaPeroxidesRatsPPAR gammachemistryMitochondrial biogenesisNF-κB.Astrocytesbiology.proteinFisiologia humanaLipid PeroxidationOxidative stressResearch PaperTranscription FactorsInternational Journal of Medical Sciences
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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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Mitochondrially encoded cysteine predicts animal lifespan

2007

Summary The role of genetic factors in the determination of lifespan is undisputed. However, numerous successful efforts to identify individual genetic modulators of longevity have not yielded yet a quantitative measure to estimate the lifespan of a species from scratch, merely based on its genomic constitution. Here, we report on a meta-examination of genome sequences from 248 animal species with known maximum lifespan, including mammals, birds, fish, insects, and helminths. Our analysis reveals that the frequency with which cysteine is encoded by mitochondrial DNA is a specific and phylogenetically ubiquitous molecular indicator of aerobic longevity: long-lived species synthesize respirat…

Models MolecularGeneticsAgingMitochondrial DNAFree Radicalsmedia_common.quotation_subjectLongevityRespiratory chainLongevityComputational BiologyLocus (genetics)Cell BiologyMitochondrionBiologyProtein oxidationDNA MitochondrialGenomeMitochondriaMitochondrial ProteinsAnimalsHumansCysteineAnaerobic bacteriaPhylogenymedia_commonAging Cell
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