Search results for "Mitochondrial matrix"

showing 6 items of 6 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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Sea Urchin Mitochondrial Matrix Contains a 56-kDa Chaperonine-like Protein

1997

Abstract Paracentrotus lividus mitochondrial matrix contains a constitutive hsp of 56-KDa which cross reacts with a serum anti-hsp-60 chaperonine from yeast mitochondria. The localization of hsps preexisting or newly synthesized in different subcellular fractions of gastrula embryos is also analyzed by two-dimensional electrophoresis.

animal structuresChaperoninsBlotting WesternBiophysicsMitochondrionBiochemistryParacentrotus lividusbiology.animalAnimalsElectrophoresis Gel Two-DimensionalImmunoelectrophoresisMolecular BiologySea urchinbiologyEmbryoCell Biologybiology.organism_classificationMolecular biologyYeastMitochondriaGastrulationBiochemistryMitochondrial matrixSea Urchinsbiological sciencesembryonic structuresBiochemical and Biophysical Research Communications
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Localization of mitochondrial Hsp56 chaperonin during sea urchin development.

2001

We have previously demonstrated that Paracentrotus lividus nuclear genome encodes for the heat shock inducible chaperonin homolog Hsp 56 (1) and that the mature protein is localized in the mitochondrial matrix (2). In this paper we report that constitutive Hsp56 is maternally inherited, in fact it is present in the in unfertilized eggs, and that it has a perinuclear specific localization during cleavage. In the later stages both the constitutive and the heat shock inducible chaperonin has a specific territorial distribution. Moreover following heat shock, the Hsp56 appears in the cytoplasm and in the postmitochondrial supernatant beside the mitochondrial fraction.

Nuclear geneEmbryo NonmammalianBlotting WesternBiophysicsMitochondrionCell FractionationBiochemistryParacentrotus lividusChaperoninTacrolimus Binding Proteinsbiology.animalAnimalsMolecular BiologySea urchinbiologyCell Biologybiology.organism_classificationMolecular biologyImmunohistochemistryCell biologyMitochondriaMitochondrial matrixCytoplasmSea UrchinsHSP60Molecular ChaperonesBiochemical and biophysical research communications
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Hsp10: Anatomic distribution, functions, and involvement in human disease

2013

There is growing evidence that molecular chaperones/heat shock proteins are involved in the pathogenesis of a number of human diseases, known as chaperonopathies. A better molecular understanding of the pathogenetic mechanisms is essential for addressing new strategies in diagnostics, therapeutics and clinical management of chaperonopathies, including those in which Hsp10 is involved. This chaperonin has been studied for a long time as a member of the mitochondrial protein-folding machine. However, although in normal cells Hsp10 is mainly localized in the mitochondrial matrix, it has also been found during and after stress in other subcellular compartments, such as cytosol, vesicles and sec…

InflammationAgingGeneral Immunology and MicrobiologySettore BIO/16 - Anatomia UmanaVesicleBiologyGeneral Biochemistry Genetics and Molecular BiologyChaperoninCell biologyAutoimmune DiseasesPathogenesisSettore MED/18 - Chirurgia GeneraleCytosolSettore MED/38 - Pediatria Generale E SpecialisticaBiochemistryMitochondrial matrixHeat shock proteinNeoplasmsCancer cellExtracellularChaperonin 10HumansHsp10chaperonopathies molecular chaperones human diseases cellular localization mitochondria
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Lon protease: a novel mitochondrial matrix protein in the interconnection between drug-induced mitochondrial dysfunction and endoplasmic reticulum st…

2017

Background and Purpose Mitochondria-associated membranes (MAMs) are specific endoplasmic reticulum (ER) domains that enable it to interact directly with mitochondria and mediate metabolic flow and Ca2+ transfer. A growing list of proteins have been identified as MAMs components, but how they are recruited and function during complex cell stress situations is still not understood, while the participation of mitochondrial matrix proteins is largely unrecognized. Experimental Approach This work compares mitochondrial/ER contact during combined ER stress/mitochondrial dysfunction using a model of human hepatoma cells (Hep3B cell line) treated for 24 h with classic pharmacological inducers of ER…

0301 basic medicinePharmacologyMitochondrial DNAChemistryEndoplasmic reticulumMitochondrionmedicine.diseaseCarbonyl cyanide m-chlorophenyl hydrazoneCell biology03 medical and health sciencesMitofusin-2chemistry.chemical_compound030104 developmental biology0302 clinical medicineMitochondrial matrixUnfolded protein responsemedicineOptic Atrophy 1030217 neurology & neurosurgeryBritish Journal of Pharmacology
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Intramitochondrial crystalloids in rat pinealocytes.

1982

In the present study the rare occurrence of intramitochondrial crystalloid inclusions in the rat pinealocytes is described. They lie within the mitochondrial matrix and consist of a lattice of moderately electron-dense lines. Intersections at regular intervals form rhomboid-like subunits. The significance of these inclusions is not known.

Inclusion BodiesMalemedicine.medical_specialtyHistologySubmitochondrial ParticlesRats Inbred StrainsCell BiologyMitochondrionBiologyPineal GlandInclusion bodiesPathology and Forensic MedicinePinealocyteMitochondriaRatsPineal glandMicroscopy ElectronEndocrinologymedicine.anatomical_structureMitochondrial matrixInternal medicinemedicineBiophysicsAnimalsCrystallizationCell and tissue research
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