Search results for "PEROXISOME"

showing 10 items of 232 documents

Transcriptional induction of the fatty acid binding protein gene in mouse liver by bezafibrate

1993

AbstractThe mechanism by which hypolipidemic peroxisome proliferators of the fibrate family induce the liver fatty acid binding protein in liver of rodents is unknown. In order to delineate the level at which this protein is induced, the transcriptional activity of the specific gene encoding for liver fatty acid binding protein was measured in isolated hepatocyte nuclei obtained from male Swiss mice daily force-fed during 7 days with 400 mg/kg body weight bezafibrate. This treatment induced a 4-fold increase in the liver fatty acid binding protein transcription rate. Liver fatty acid binding protein mRNA level, measured by Northern blot analysis and cytosolic content of this protein, analyz…

MalePeroxisome proliferator activated receptorTranscription GeneticImmunoblottingBiophysicsPeroxisome proliferator-activated receptorNerve Tissue ProteinsFatty Acid-Binding ProteinsPeroxisome proliferator hypolipidemic drugBiochemistryFatty acid-binding proteinMiceStructural BiologyGeneticsmedicineAnimalsRNA Messengeradipocyte protein 2Molecular Biologychemistry.chemical_classificationLiver fatty acid binding proteinBezafibratebiologyBinding proteinBody WeightCell BiologyOrgan SizePeroxisomeBlotting NorthernMolecular biologyLipidsNeoplasm ProteinsGene regulationFatty acid synthasechemistryBiochemistryGene Expression RegulationLiverbiology.proteinElectrophoresis Polyacrylamide GelPeroxisome proliferator-activated receptor alphaBezafibrateCarrier ProteinsDNA ProbesFatty Acid-Binding Protein 7medicine.drugFEBS Letters
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Induction of the fatty acid transport protein 1 and acyl-CoA synthase genes by dimer-selective rexinoids suggests that the peroxisome proliferator-ac…

2000

The intracellular fatty acid content of insulin-sensitive target tissues determines in part their insulin sensitivity. Uptake of fatty acids into cells is a controlled process determined in part by a regulated import/export system that is controlled at least by two key groups of proteins, i.e. the fatty acid transport protein (FATP) and acyl-CoA synthetase (ACS), which facilitate, respectively, the transport of fatty acids across the cell membrane and catalyze their esterification to prevent their efflux. Previously it was shown that the expression of the FATP-1 and ACS genes was controlled by insulin and by peroxisome proliferator-activated receptor (PPAR) agonists in liver or in adipose t…

MalePeroxisome proliferator-activated receptor gammaTime FactorsReceptors Retinoic AcidRetinoic acidReceptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorTretinoinRetinoid X receptorBiologyFatty Acid-Binding ProteinsBiochemistryMicechemistry.chemical_compoundCoenzyme A LigasesTumor Cells CulturedAnimalsHumansTissue DistributionMolecular BiologyNucleic Acid Synthesis InhibitorsCell Nucleuschemistry.chemical_classificationDose-Response Relationship DrugFatty AcidsMembrane ProteinsFatty acidMembrane Transport ProteinsSerum Albumin Bovine3T3 CellsCell BiologyFatty Acid Transport ProteinsRatsRats ZuckerRetinoic acid receptorRetinoid X ReceptorschemistryBiochemistryDactinomycinFree fatty acid receptorRNAPeroxisome proliferator-activated receptor alphaCaco-2 CellsCarrier ProteinsTranscription Factors
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Transgenic expression and activation of PGC-1α protect dopaminergic neurons in the MPTP mouse model of Parkinson’s disease

2011

Mitochondrial dysfunction and oxidative stress occur in Parkinson’s disease (PD), but little is known about the molecular mechanisms controlling these events. Peroxisome proliferator-activated receptor-gamma coactivator-1α (PGC-1α) is a transcriptional coactivator that is a master regulator of oxidative stress and mitochondrial metabolism. We show here that transgenic mice overexpressing PGC-1α in dopaminergic neurons are resistant against cell degeneration induced by the neurotoxin MPTP. The increase in neuronal viability was accompanied by elevated levels of mitochondrial antioxidants SOD2 and Trx2 in the substantia nigra of transgenic mice. PGC-1α overexpression also protected against MP…

MaleSOD2Mice TransgenicSubstantia nigraMitochondrionBiologyNeuroprotectionCell LineMiceCellular and Molecular Neurosciencechemistry.chemical_compoundDopaminemedicineAnimalsNeurotoxinParkinson Disease SecondaryMolecular BiologyPGC-1α RSV SIRT1 MPTP Dopaminergic neurons Parkinson’s diseasePharmacologyMPTPDopaminergicBrainParkinson DiseaseCell BiologyPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaMitochondriaCell biologyDisease Models AnimalOxidative Stressnervous systemBiochemistrychemistry1-Methyl-4-phenyl-1236-tetrahydropyridineTrans-ActivatorsMolecular MedicineFemaleTranscription Factorsmedicine.drugCellular and Molecular Life Sciences
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An impaired peroxisomal targeting sequence leading to an unusual bicompartmental distribution of cytosolic epoxide hydrolase

1991

AbstractTo gain an understanding of the mechanism by which the subcellular distribution of cytosolic epoxide hydrolase (cEH) is directed, we have analyzed the carboxy terminal region of rat liver cEH by means of cDNA cloning to define the structure of its possible peroxisomal targeting sequence (PTS). Purified cEH was subjected to peptide analysis following endoproteinase Glu-C digestion and HPLC-separation of the fragments. The obtained sequence information was used to perform PCR experiments resulting in the isolation of a 680 bp cDNA clone encoding the carboxy terminus of cEH. The deduced amino acid sequence displays a terminal tripeptide Ser-Lys-Ile which is highly homologous to the PTS…

MaleSignal peptidePTSanimal structures1303 BiochemistryMolecular Sequence DataBiophysics10050 Institute of Pharmacology and Toxicology610 Medicine & healthTripeptideProtein Sorting SignalsBiologyMicrobodiesBiochemistryAmino acid sequence1307 Cell BiologyCytosol1315 Structural Biology1311 GeneticsStructural BiologyComplementary DNAGenetics1312 Molecular BiologyAnimalsCloning MolecularEpoxide hydrolaseMolecular BiologyPeptide sequenceEpoxide Hydrolaseschemistry.chemical_classificationBase SequencecDNA sequenceDNACell BiologyPeroxisomeMolecular biologyRatsIsoenzymesCytosolPCREnzymeLiverchemistryBiochemistrycEH570 Life sciences; biologyPeptide analysis1304 Biophysics
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Differential proto-oncogene mRNA induction from rats treated with peroxisome proliferators

1990

After experimental treatment of rats with clofibrate or ciprofibrate, two peroxisomes proliferators with hypolipidemic activity, RNAs were prepared from liver, kidney, heart and brain; hybridization was done with DNA probes for c-myc and c-Ha-ras oncogenes and for cyanide insensitive Acyl CoA oxidase, a peroxisomal protein. c-myc mRNA is highly abundant in liver and at a lower extent in kidney, especially after treatment with ciprofibrate; clofibrate also allows a c-myc mRNA increase, but at a lower extent. c-Ha-ras, which is already expressed in all tested tissues from control animals, is stimulated by clofibrate and ciprofibrate treatments. Comparatively these compounds stimulate the cyan…

MaleSomatic cellGenes mycBiophysicsBiologyKidneyMicrobodiesBiochemistryClofibric AcidProto-OncogenesmedicineAnimalsAcyl-CoA oxidaseClofibrateRNA MessengerMolecular BiologyHypolipidemic AgentsKidneyMessenger RNAClofibrateOncogeneFibric AcidsCell BiologyPeroxisomeMolecular biologyRats Inbred F344RatsGenes rasmedicine.anatomical_structureGene Expression RegulationLiverOrgan SpecificityAcyl-CoA OxidaseCiprofibrateOxidoreductasesmedicine.drugBiochemical and Biophysical Research Communications
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Obesity causes PGC‐1α deficiency in the pancreas leading to marked IL‐6 upregulation via NF‐κB in acute pancreatitis

2019

Obesity is associated with local and systemic complications in acute pancreatitis. PPARγ coactivator 1α (PGC-1α) is a transcriptional coactivator and master regulator of mitochondrial biogenesis that exhibits dysregulation in obese subjects. Our aims were: (1) to study PGC-1α levels in pancreas from lean or obese rats and mice with acute pancreatitis; and (2) to determine the role of PGC-1α in the inflammatory response during acute pancreatitis elucidating the signaling pathways regulated by PGC-1α. Lean and obese Zucker rats and lean and obese C57BL6 mice were used first; subsequently, wild-type and PGC-1α knockout (KO) mice with cerulein-induced pancreatitis were used to assess the inflam…

MaleTaurocholic Acid0301 basic medicinemedicine.medical_specialtyPGC-1αPathology and Forensic Medicine03 medical and health sciencesDownregulation and upregulationInternal medicineAnimalsMedicineObesityPhosphorylationInterleukin 6PancreasCeruletideMice KnockoutIL-6biologyp65Interleukin-6business.industryNF-kappa BTranscription Factor RelAmedicine.diseasePeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaRats ZuckerUp-Regulation3. Good healthMice Inbred C57BLDisease Models Animal030104 developmental biologyEndocrinologymedicine.anatomical_structureMitochondrial biogenesisPancreatitisbiology.proteinPancreatitisAcute pancreatitisPPARGC1AbusinessPancreasCeruletideSignal TransductionThe Journal of Pathology
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Incidence of Abcd1 level on the induction of cell death and organelle dysfunctions triggered by very long chain fatty acids and TNF-alpha on oligoden…

2012

X-linked adrenoleukodystrophy (X-ALD) is characterized by ABCD1 deficiency. This disease is associated with elevated concentrations of very long chain fatty acids (C24:0 and C26:0) in the plasma and tissues of patients. Under its severe form, brain demyelination and inflammation are observed. Therefore, we determined the effects of C24:0 and C26:0 on glial cells:oligodendrocytes, which synthesize myelin, and astrocytes, which participate in immune response. So, 158N murine oligodendrocytes, rat C6 glioma cells, rat primary cultures of neuronal-glial cells, and of oligodendrocytes were treated for various periods of time in the absence or presence of C24:0 and C26:0 used at plasmatic concent…

MaleTime FactorsVacuoleMitochondrionToxicologyATP Binding Cassette Transporter Subfamily D Member 1chemistry.chemical_compoundMice0302 clinical medicineRNA Small InterferingAdrenoleukodystrophyCells CulturedComputingMilieux_MISCELLANEOUSMembrane Potential MitochondrialNeurons0303 health sciencesGeneral NeuroscienceFatty AcidsBrainPeroxisomeCatalaseFlow Cytometry3. Good healthCell biologyMitochondriaOligodendrogliamedicine.anatomical_structureFemaleProgrammed cell deathChromatography GasBiologyGas Chromatography-Mass SpectrometryStatistics Nonparametric03 medical and health sciencesMicroscopy Electron TransmissionLysosomeOrganellemedicineAnimalsHumansPropidium iodideRNA MessengerRats Wistar030304 developmental biologyCell SizeChemokine CCL22OrganellesDose-Response Relationship DrugCell growthTumor Necrosis Factor-alphaRatschemistryAnimals NewbornAstrocytesATP-Binding Cassette Transporters[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition030217 neurology & neurosurgery
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Fibrate induction of the adrenoleukodystrophy-related gene (ABCD2)

2001

X-linked adrenoleukodystrophy (X-ALD) is a neurodegenerative disease due to a defect in the ABCD1 (ALD) gene. ABCD1, and the two close homologues ABCD2 (ALDR) and ABCD3 (PMP70), are genes encoding ATP-binding cassette half-transporters of the peroxisomal membrane. As overexpression of the ABCD2 or ABCD3 gene can reverse the biochemical phenotype of X-ALD (reduced beta-oxidation of very-long-chain fatty acids), pharmacological induction of these partially redundant genes may represent a therapeutic approach to X-ALD. We previously reported that the ABCD2 and ABCD3 genes could be strongly induced by fibrates, which are hypolipidaemic drugs and peroxisome-proliferators in rodents. We provide e…

MaleTranscription GeneticMolecular Sequence DataResponse elementReceptors Cytoplasmic and NuclearATP-binding cassette transporterATP Binding Cassette Transporter Subfamily DBiochemistryMiceFenofibrateABCD3Sequence Homology Nucleic AcidABCD2medicineAnimalsHumansRats WistarAdrenoleukodystrophyPromoter Regions GeneticGeneHypolipidemic AgentsMice KnockoutBase SequencebiologyDNATransfectionPeroxisomemedicine.diseaseMolecular biologyRatsGene Expression Regulationbiology.proteinATP-Binding Cassette TransportersAdrenoleukodystrophyTranscription FactorsEuropean Journal of Biochemistry
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Transcriptional activation of CYP2C9, CYP1A1, and CYP1A2 by hepatocyte nuclear factor 4alpha requires coactivators peroxisomal proliferator activated…

2006

Hepatocyte nuclear factor 4alpha (HNF4alpha) is a key transcription factor for the constitutive expression of cytochromes P450 (P450s) in the liver. However, human hepatoma HepG2 cells show a high level of HNF4alpha but express only marginal P450 levels. We found that the HNF4alpha-mediated P450 transcription in HepG2 is impaired by the low level of coactivators peroxisomal proliferator activated receptor-gamma coactivator 1alpha (PGC1alpha) and steroid receptor coactivator 1 (SRC1). Reporter assays with a chimeric CYP2C9-LUC construct demonstrated that the sole transfection of coactivators induced luciferase activity in HepG2 cells. In HeLa cells however, CYP2C9-LUC activity only significa…

MaleTranscriptional Activationendocrine systemBiologyResponse ElementsTransfectiondigestive systemAdenoviridaeNuclear Receptor Coactivator 1Cytochrome P-450 CYP1A2CoactivatorCytochrome P-450 CYP1A1HumansInsulinTranscription factorCells CulturedHeat-Shock ProteinsCytochrome P-450 CYP2C9Histone AcetyltransferasesPharmacologyTransfectionMiddle AgedMolecular biologyPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaNuclear receptor coactivator 1Hepatocyte nuclear factorsHepatocyte Nuclear Factor 4Nuclear receptor coactivator 3Nuclear receptor coactivator 2HepatocytesMolecular MedicineFemaleAryl Hydrocarbon HydroxylasesChromatin immunoprecipitationHeLa CellsProtein BindingTranscription FactorsMolecular pharmacology
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Suppression of the JNK Pathway by Induction of a Metabolic Stress Response Prevents Vascular Injury and Dysfunction

2008

Background— Oxidative injury and dysfunction of the vascular endothelium are early and causal features of many vascular diseases. Single antioxidant strategies to prevent vascular injury have met with mixed results. Methods and Results— Here, we report that induction of a metabolic stress response with adenosine monophosphate kinase (AMPK) prevents oxidative endothelial cell injury. This response is characterized by stabilization of the mitochondrion and increased mitochondrial biogenesis, resulting in attenuation of oxidative c-Jun N-terminal kinase (JNK) activation. We report that peroxisome proliferator coactivator 1α is a key downstream target of AMPK that is both necessary and suffici…

MaleUmbilical Veinsmedicine.medical_specialtyEndotheliumMitochondrionmedicine.disease_causeArticleMiceInternal medicinePhysiology (medical)Chlorocebus aethiopsmedicineAnimalsHumansVascular DiseasesRNA Small InterferingEndothelial dysfunctionHeat-Shock ProteinsMembrane Potential MitochondrialCell Deathbusiness.industryAdenylate KinaseJNK Mitogen-Activated Protein KinasesEndothelial CellsAMPKHydrogen PeroxideRibonucleotidesAminoimidazole CarboxamideOxidantsmedicine.diseaseAdaptation PhysiologicalPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaAngiotensin IICell biologyMice Inbred C57BLEndothelial stem cellOxidative Stressmedicine.anatomical_structureEndocrinologyMitochondrial biogenesisMutagenesisCOS CellsbusinessCardiology and Cardiovascular MedicineOxidative stressTranscription FactorsCirculation
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