Search results for "Peroxisome proliferator-activated receptor gamma"

showing 10 items of 39 documents

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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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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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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Pgc-1α and Nr4a1 Are Target Genes of Circadian Melatonin and Dopamine Release in Murine Retina

2015

Purpose The neurohormones melatonin and dopamine mediate clock-dependent/circadian regulation of inner retinal neurons and photoreceptor cells and in this way promote their functional adaptation to time of day and their survival. To fulfill this function they act on melatonin receptor type 1 (MT1 receptors) and dopamine D4 receptors (D4 receptors), respectively. The aim of the present study was to screen transcriptional regulators important for retinal physiology and/or pathology (Dbp, Egr-1, Fos, Nr1d1, Nr2e3, Nr4a1, Pgc-1α, Rorβ) for circadian regulation and dependence on melatonin signaling/MT1 receptors or dopamine signaling/D4 receptors. Methods This was done by gene profiling using qu…

Malemedicine.medical_specialtyDopamineDNA Mutational AnalysisBiologyMelatonin receptorRetinaMelatoninMiceDopamineInternal medicinemedicineNuclear Receptor Subfamily 4 Group A Member 1AnimalsCircadian rhythmReceptorMelatoninRegulation of gene expressionDNAAdaptation PhysiologicalPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaeye diseasesCircadian RhythmMice Inbred C57BLEndocrinologyGene Expression RegulationDopamine receptorMutationFemalesense organsSignal transductionhormones hormone substitutes and hormone antagonistsmedicine.drugSignal TransductionTranscription Factors
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La concentración sanguínea de PGC-1a predice miocardio salvado y remodelado ventricular tras infarto agudo de miocardio con elevación del segmento ST

2015

et al.

Malemedicine.medical_specialtyST-segment elevation acute myocardial infarctionMyocardial InfarctionIschemiaPGC-1αMagnetic Resonance Imaging CineInfarctionRemodelado ventricularElectrocardiographyCardiac magnetic resonance imagingVentricular remodelingInternal medicineEdemamedicineHumansST segmentProspective Studiescardiovascular diseasesMyocardial infarctionVentricular remodelingHeat-Shock ProteinsVentricular Remodelingmedicine.diagnostic_testbusiness.industryMyocardiumEstrés oxidativoStroke VolumeMagnetic resonance imagingGeneral MedicineMiddle AgedPrognosismedicine.diseasePeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaInfarto agudo de miocardio con elevación del segmento STMetabolismo oxidativoOxidative stresscardiovascular systemCardiologyOxidative metabolismFemalemedicine.symptombusinessFollow-Up StudiesTranscription FactorsRevista Española de Cardiología (English Edition)
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Identification of novel peroxisome proliferator-activated receptor alpha (PPARalpha) target genes in mouse liver using cDNA microarray analysis.

2001

Peroxisome proliferators, which function as peroxisome proliferator-activated receptor-alpha (PPARalpha) agonists, are a group of structurally diverse nongenotoxic hepatocarcinogens including the fibrate class of hypolipidemic drugs that induce peroxisome proliferation in liver parenchymal cells. Sustained activation of PPARalpha by these agents leads to the development of liver tumors in rats and mice. To understand the molecular mechanisms responsible for the pleiotropic effects of these agents, we have utilized the cDNA microarray to generate a molecular portrait of gene expression in the liver of mice treated for 2 weeks with Wy-14,643, a potent peroxisome proliferator. PPARalpha activa…

Mice KnockoutPeroxisome proliferator-activated receptor gammaDNA ComplementaryChemistryMicroarray analysis techniquesGene Expression ProfilingPeroxisome ProliferationReceptors Cytoplasmic and NuclearPeroxisomeArticleCell biologyGene expression profilingMice Inbred C57BLMicePyrimidinesLiverGene expressionGeneticsAnimalsPeroxisome proliferator-activated receptor deltaPeroxisome proliferator-activated receptor alphaMolecular BiologyOligonucleotide Array Sequence AnalysisTranscription FactorsGene expression
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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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Myoglobin, expressed in brown adipose tissue of mice, regulates the content and activity of mitochondria and lipid droplets

2021

Abstract The identification of novel physiological regulators that stimulate energy expenditure through brown adipose tissue (BAT) activity in substrate catalysis is of utmost importance to understand and treat metabolic diseases. Myoglobin (MB), known to store or transport oxygen in heart and skeletal muscles, has recently been found to bind fatty acids with physiological constants in its oxygenated form (i.e., MBO2). Here, we investigated the in vivo effect of MB expression on BAT activity. In particular, we studied mitochondrial function and lipid metabolism as essential determinants of energy expenditure in this tissue. We show in a MB-null (MBko) mouse model that MB expression in BAT i…

PalmitatesOxidative phosphorylationMitochondrion1307 Cell BiologyMiceAdipose Tissue BrownLipid dropletBrown adipose tissueRespiration1312 Molecular BiologymedicineAnimalsHumansPPAR alpha11434 Center for Clinical StudiesMuscle SkeletalMolecular BiologyUncoupling Protein 1Mice KnockoutMyoglobinChemistryProteinsThermogenesisLipid metabolismLipid DropletsCell BiologyMetabolism10081 Institute of Veterinary PhysiologyPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaMitochondriaCell biologyOxygenDisease Models AnimalAdipocytes Brownmedicine.anatomical_structure10076 Center for Integrative Human Physiology570 Life sciences; biologyApoptosis Regulatory ProteinsEnergy MetabolismThermogenesisBiochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
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Phosphorylation of peroxisome proliferator-activated receptor α in rat Fao cells and stimulation by ciprofibrate

1999

The basic mechanism(s) by which peroxisome proliferators activate peroxisome proliferator-activated receptors (PPARs) is (are) not yet fully understood. Given the diversity of peroxisome proliferators, several hypotheses of activation have been proposed. Among them is the notion that peroxisome proliferators could activate PPARs by changing their phosphorylation status. In fact, it is well known that several members of the nuclear hormone receptor superfamily are regulated by phosphorylation. In this report, we show that the rat Fao hepatic-derived cell line, known to respond to peroxisome proliferators, exhibited a high content of PPARalpha. Alkaline phosphatase treatment of Fao cell lysat…

Peroxisome proliferator-activated receptor gammaPhosphataseReceptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorBiologyMicrobodiesBiochemistryCell LineClofibric AcidmedicineAnimalsEnzyme InhibitorsPhosphorylationPharmacologychemistry.chemical_classificationFibric Acidsfood and beveragesPeroxisomePhosphoric Monoester HydrolasesRatsGene Expression RegulationBiochemistryNuclear receptorchemistryPhosphorylationPeroxisome Proliferatorslipids (amino acids peptides and proteins)Acyl-CoA OxidasePeroxisome proliferator-activated receptor alphaCiprofibrateOxidoreductasesTranscription Factorsmedicine.drugBiochemical Pharmacology
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