Search results for "Peroxisome proliferator"

showing 10 items of 132 documents

Induction of the peroxisome proliferator activated receptor by fenofibrate in rat liver

1992

AbstractThe process of peroxisome proliferation in rodent liver by hypolipidemic compounds and related substances has recently been shown to be receptor-madiated. In the present study, we have examined the effect of oral administration of the strong peroxisome proliferator fenofibrate on the hepatic expression level of the peroxisome proliferator activated receptor (PPAR) in rats. Immunoblots of rat liver cytosols and nuclear extracs using antibodies raised against recombinant PPAR/β-galactosidase fusion proteins revealed a pronounced increase in the amount of PPAR protein in response to fenofibrate treatment. This induction could also be confirmed at the level or RNA by Northern blotting. …

Male1303 BiochemistryReceptors Cytoplasmic and Nuclear10050 Institute of Pharmacology and ToxicologyPeroxisome proliferator-activated receptorPPARMicrobodiesPolymerase Chain ReactionBiochemistryPPAR agonist1307 Cell BiologyMiceCytosol1315 Structural BiologyFenofibrateStructural Biologychemistry.chemical_classificationMice Inbred BALB CFenofibrateOligodeoxyribonucleotidesPeroxisome proliferator-activated receptor alphaFusion proteinmedicine.drugmedicine.medical_specialtyPeroxisome proliferator-activated receptor gammamRNAMolecular Sequence DataBiophysicsPeroxisome ProliferationReceptors Cell Surface610 Medicine & healthBiology1311 GeneticsInternal medicine1312 Molecular BiologyGeneticsmedicineAnimalsNorthern blotMolecular BiologyAntibodyHypolipidemic compoundCell NucleusMessenger RNABase SequenceImmune SeraCell BiologyBlotting NorthernRatsMice Inbred C57BLEndocrinologychemistry570 Life sciences; biologyTranscription Factors1304 BiophysicsFEBS Letters
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Differential expression of PGC-1α and metabolic sensors suggest age-dependent induction of mitochondrial biogenesis in Friedreich ataxia fibroblasts.

2011

11 pages, 6 figures. PMID:21687738[PubMed] PMCID: PMC3110204

MaleAgingMitochondrial DiseasesMitochondrial MyopathyUbiquinoneCardiomyopathylcsh:MedicineMitochondrionAMP-Activated Protein Kinasesp38 Mitogen-Activated Protein KinasesAntioxidantsAdenosine TriphosphateAMP-activated protein kinaseTrinucleotide RepeatsFibrosisMolecular Cell BiologyChildlcsh:ScienceHeat-Shock ProteinsRegulation of gene expressionMultidisciplinaryMovement DisordersbiologyNeuromuscular DiseasesMiddle AgedCatalasePeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaCell biologyMitochondriaDNA-Binding ProteinsNeurologyDisease ProgressionMedicineFemalemedicine.symptomSignal TransductionResearch ArticleAdultcongenital hereditary and neonatal diseases and abnormalitiesAtaxiaAdolescentMitochondrial ProteinsmedicineGeneticsHumansBiologyAllelesGlutathione PeroxidaseSuperoxide Dismutaselcsh:RHuman GeneticsFibroblastsmedicine.diseaseMolecular biologyOxidative StressMitochondrial biogenesisGene Expression RegulationFriedreich Ataxiabiology.proteinFrataxinlcsh:QEnergy MetabolismReactive Oxygen SpeciesTranscription FactorsPLoS ONE
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Effects of peroxisome proliferator-activated receptor alpha activation on pathways contributing to cholesterol homeostasis in rat hepatocytes

2004

International audience; Peroxisome proliferator-activated receptor alpha (PPARa) activation by fibrates controls expression of several genes involved in hepatic cholesterol metabolism. Other genes could be indirectly controlled in response to changes in cellular cholesterol availability. To further understand how fibrates may affect cholesterol synthesis, we investigated in parallel the changes in the metabolic pathways contributing to cholesterol homeostasis in liver. Ciprofibrate increased HMG-CoA reductase and FPP synthase mRNA levels in rat hepatocytes, together with cholesterogenesis from [14C] acetate and [3H] mevalonate. The up-regulation observed in fenofibrate- and WY-14,643-treate…

MaleCarboxy-Lyases[SDV]Life Sciences [q-bio]Receptors Cytoplasmic and NuclearAcetatesClofibric AcidMicechemistry.chemical_compound0302 clinical medicineMice KnockoutCarbon Isotopes0303 health sciencesFenofibrateFibric AcidsPeroxisomeUp-RegulationHMG-COA REDUCTASEDNA-Binding ProteinsCholesterolCHOLESTEROL METABOLISM030220 oncology & carcinogenesisHMG-CoA reductaseCholesteryl esterPeroxisome Proliferatorslipids (amino acids peptides and proteins)Peroxisome proliferator-activated receptor alphaSterol Regulatory Element Binding Protein 1Cell DivisionSignal Transductionmedicine.drugmedicine.medical_specialtyMevalonic AcidPeroxisome ProliferationBiologyCholesterol 7 alpha-hydroxylaseBile Acids and Salts03 medical and health sciencesInternal medicinemedicineAnimalsRNA MessengerMolecular Biology030304 developmental biologyCell BiologyRAT HEPATOCYTEPPARA-NULL MOUSERatsSterol regulatory element-binding proteinMice Inbred C57BLPyrimidinesEndocrinologychemistryFIBRATECCAAT-Enhancer-Binding ProteinsHepatocytesbiology.proteinHydroxymethylglutaryl CoA ReductasesTranscription Factors
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Effects of Conjugated Linoleic Acid Associated With Endurance Exercise on Muscle Fibres and Peroxisome Proliferator-Activated Receptor γ Coactivator …

2016

Conjugated linoleic acid (CLA) has been reported to improve muscle hypertrophy, steroidogenesis, physical activity, and endurance capacity in mice, although the molecular mechanisms of its actions are not completely understood. The aim of the present study was to identify whether CLA alters the expression of any of the peroxisome proliferator-activated receptor γ coactivator 1α (PGC1α) isoforms, and to evaluate the possible existence of fibre-type-specific hypertrophy in the gastrocnemius and plantaris muscles. Mice were randomly assigned to one of four groups: placebo sedentary, CLA sedentary, placebo trained, or CLA trained. The CLA groups were gavaged with 35 μl per day of Tonalin® FFA 8…

MaleConjugatedPhysiologyClinical BiochemistryMuscle Fibers SkeletalMuscle FibersMiceLectinsPhysical Conditioning AnimalAnimalsProtein IsoformsLinoleic Acids ConjugatedInbred BALB CMice Inbred BALB CAnimalSettore BIO/16 - Anatomia UmanaAdenylate KinaseSkeletalCell BiologyPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaPhysical ConditioningHindlimbMitochondriaLinoleic AcidsAdenylate Kinase; Animals; Dietary Supplements; Hindlimb; Lectins; Linoleic Acids Conjugated; Male; Mice Inbred BALB C; Mitochondria; Muscle Fibers Skeletal; Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha; Protein Isoforms; Physical Conditioning Animal; Physiology; Clinical Biochemistry; Cell BiologyDietary SupplementsFat supplements
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PPAR-alpha L162V and PGC-1 G482S gene polymorphisms, but not PPAR-gamma P12A, are associated with alcohol consumption in a Spanish Mediterranean popu…

2008

Abstract Background Peroxisome Proliferator-Activated Receptors (PPARs) and its co-activators are regulatory elements of the cellular lipid homeostasis and have been associated with feeding behavior modulation. Animal models suggest that these genes may be involved in alcohol consumption regulation. However, no studies in humans exist. Our aim is to estimate the possible association between polymorphisms in the PPAR-α , PPAR-γ and PPAR-γ co-activator 1A ( PGC-1A ) genes and alcohol consumption in humans. Methods We have conducted a cross-sectional study between the PPAR-α L162V, PPAR-γ P12A and PGC-1A G482S polymorphisms, and alcohol consumption in a general Mediterranean Spanish population…

MaleCross-sectional studyClinical BiochemistryPeroxisome Proliferator-Activated ReceptorsPeroxisome proliferator-activated receptorAlcoholBiochemistryGenechemistry.chemical_compoundGene FrequencyPolymorphism (computer science)Heat-Shock ProteinsGeneticschemistry.chemical_classificationAged 80 and overeducation.field_of_studyMediterranean RegionGeneral MedicineMiddle AgedPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaFemaleAdultmedicine.medical_specialtyAdolescentAlcohol DrinkingGenotypePopulationSingle-nucleotide polymorphismBiologyPolymorphism Single NucleotideYoung AdultInternal medicinemedicineHumansPPAR alphaeducationAllele frequencyAllelesAgedEthanolPolymorphism GeneticEthanolBiochemistry (medical)DNASingle nucleotide polymorphismEndocrinologyCross-Sectional StudieschemistrySocioeconomic FactorsSpainAlcoholic beveragesTranscription FactorsClinica chimica acta; international journal of clinical chemistry
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A role for the peroxisomal 3-ketoacyl-CoA thiolase B enzyme in the control of PPARα-mediated upregulation of SREBP-2 target genes in the liver.: ThB …

2011

International audience; Peroxisomal 3-ketoacyl-CoA thiolase B (Thb) catalyzes the final step in the peroxisomal β-oxidation of straight-chain acyl-CoAs and is under the transcription control of the nuclear hormone receptor PPARα. PPARα binds to and is activated by the synthetic compound Wy14,643 (Wy). Here, we show that the magnitude of Wy-mediated induction of peroxisomal β-oxidation of radiolabeled (1-(14)C) palmitate was significantly reduced in mice deficient for Thb. In contrast, mitochondrial β-oxidation was unaltered in Thb(-/-) mice. Given that Wy-treatment induced Acox1 and MFP-1/-2 activity at a similar level in both genotypes, we concluded that the thiolase step alone was respons…

MaleMESH: HepatomegalyPalmitatesMESH : PyrimidinesMESH : Gene DeletionBiochemistryelement-binding proteinsMESH : Acetyl-CoA C-AcyltransferaseMiceMESH: Up-RegulationMESH: AnimalsMESH : Up-RegulationMESH: Lipid Metabolism0303 health sciencesMESH : Gene Expression RegulationThiolase030302 biochemistry & molecular biologyGeneral MedicineMESH : HepatomegalyUp-Regulationzellweger-syndromePeroxisome ProliferatorsMESH: Peroxisome ProliferatorsHepatomegalySterol Regulatory Element Binding Protein 2peroxisomal 3-ketoacyl-CoA thiolase BMESH: Mitochondria3-oxoacyl-coa thiolaseLathosterolfatty-acid oxidationrat-liverMESH: Sterol Regulatory Element Binding Protein 203 medical and health sciencesMESH : Sterol Regulatory Element Binding Protein 2HumansPPAR alphaMESH : Peroxisome Proliferators[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyPPARaVLAGMESH : Oxidation-ReductionFatty Acid Oxidation.MESH: HumansCholesterolMESH : HumanscholesterolLipid MetabolismMESH: PeroxisomesSterol regulatory element-binding proteinchemistryMESH: PyrimidinesCholesterol; Micro-array analysis; Peroxisomal 3-ketoacyl-CoA thiolase B; PPARα and SREBP-2; Wy14643Fatty Acid OxidationGene DeletionMESH: LiverMESH: Oxidation-ReductionMESH: Signal TransductionMESH: Mice KnockoutVoeding Metabolisme en Genomicachemistry.chemical_compoundMESH: CholesterolMESH : Lipid MetabolismWy14MESH : PalmitatesMESH: PPAR alphaMESH : CholesterolMice Knockoutneuronal migration643PeroxisomeAcetyl-CoA C-AcyltransferaseMESH: Gene Expression RegulationMetabolism and GenomicsMitochondriaLiverBiochemistryMicro-array analysisMetabolisme en GenomicaACOX1Nutrition Metabolism and GenomicsMESH : MitochondriaOxidation-ReductionSignal Transductionacyl-coa oxidasecholesterol-synthesisMESH : MaleMESH : PPAR alphaPeroxisome ProliferationPPARα and SREBP-2Biologybeta-oxidationVoedingproliferator-activated receptorsMESH : MicePeroxisomesAnimals[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: Mice030304 developmental biologySCP2NutritionMESH : Signal TransductionMESH : LiverMESH: PalmitatesMESH: MalePyrimidinesMESH: Acetyl-CoA C-AcyltransferaseGene Expression RegulationMESH: Gene DeletionMESH : Mice KnockoutMESH : AnimalsMESH : Peroxisomes
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Free [NADH]/[NAD+] regulates sirtuin expression

2011

Sirtuins are deacetylases involved in metabolic regulation and longevity. Our aim was to test the hypothesis that they are subjected to redox regulation by the [NADH]/[NAD(+)] ratio. We used NIH3T3 fibroblasts in culture, Drosophila fed with or without ethanol and exercising rats. In all three models an increase in [NADH]/[NAD(+)] came up with an increased expression of sirtuin mRNA and protein. PGC-1α (a substrate of sirtuins) protein level was significantly increased in fibroblasts incubated with lactate and pyruvate but this effect was lost in fibroblasts obtained from sirtuin-deficient mice. We conclude that the expression of sirtuins is subject to tight redox regulation by the [NADH]/[…

MaleMetaboliteBiophysicsBiochemistryMicechemistry.chemical_compoundPhysical Conditioning AnimalPyruvic AcidAnimalsSirtuinsLactic AcidRNA MessengerRats WistarEthanol metabolismMolecular BiologyCells CulturedGlyceraldehyde 3-phosphate dehydrogenaseRegulation of gene expressionMessenger RNAEthanolbiologyFibroblastsNADPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaRatsCell biologyDrosophila melanogasterGlycerol-3-phosphate dehydrogenaseGene Expression RegulationchemistryBiochemistrySirtuinNIH 3T3 CellsTrans-Activatorsbiology.proteinNAD+ kinaseOxidation-ReductionTranscription FactorsArchives of Biochemistry and Biophysics
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Mitochondrial biogenesis fails in secondary biliary cirrhosis in rats leading to mitochondrial DNA depletion and deletions

2011

Chronic cholestasis is characterizedby mitochondrial dysfunction, associated with loss of mitochondrialmembrane potential, decreased activities of respiratory chaincomplexes, and ATP production. Our aim was to determine themolecular mechanisms that link long-term cholestasis to mitochondrialdysfunction. We studied a model of chronic cholestasis inducedby bile duct ligation in rats. Key sensors and regulators of theenergetic state and mitochondrial biogenesis, mitochondrial DNA(mtDNA)-to-nuclear DNA (nDNA) ratio (mtDNA/nDNA) relativecopy number, mtDNA deletions, and indexes of apoptosis (BAX,BCL-2, and cleaved caspase 3) and cell proliferation (PCNA) wereevaluated. Our results show that long…

MaleMitochondrial DNAPhysiologyMitochondrial TurnoverMitochondrial HepatopathyNF-E2-Related Factor 1Respiratory chainMitochondria LiverProtein Serine-Threonine KinasesMitochondrionBiologyDNA MitochondrialSirtuin 1CholestasisProliferating Cell Nuclear AntigenPhysiology (medical)medicineAnimalsRats Wistarbcl-2-Associated X ProteinCholestasisHepatologyCaspase 3Liver Cirrhosis BiliaryGastroenterologyPyruvate Dehydrogenase Acetyl-Transferring KinaseRNA-Binding ProteinsTFAMmedicine.diseaseGA-Binding Protein Transcription FactorPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaMolecular biologyRatsGenes MitochondrialProto-Oncogene Proteins c-bcl-2Mitochondrial biogenesisChronic DiseaseBile DuctsGene DeletionTranscription FactorsAmerican Journal of Physiology-Gastrointestinal and Liver Physiology
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Dehydroepiandrosterone up-regulates the Adrenoleukodystrophy-related gene (ABCD2) independently of PPAR alpha in rodents

2007

International audience; X-linked adrenoleukodystrophy (X-ALD) is a neurodegenerative disease caused by mutations in the ABCD1 gene, which encodes a peroxisomal ABC transporter, ALDP, supposed to participate in the transport of very long chain fatty acids (VLCFA). The adrenoleukodystrophyrelated protein (ALDRP), which is encoded by the ABCD2 gene, is the closest homolog of ALDP and is considered as a potential therapeutic target since functional redundancy has been demonstrated between the two proteins. Pharmacological induction of Abcd2 by fibrates through the activation of PPARa has been demonstrated in rodent liver. DHEA, the most abundant steroid in human, is described as a PPARa activat…

MalePEROXISOMEProhormonePeroxisome proliferator-activated receptorATP-binding cassette transporterBiochemistryMice0302 clinical medicineABC TRANSPORTERSPPAR-ALPHAAdrenal GlandsTestisDHEACells Culturedchemistry.chemical_classification0303 health sciencesSex CharacteristicsbiologyBrainGeneral MedicineOrgan SizePeroxisome3. Good healthUp-RegulationLiverAdrenoleukodystrophyFemalemedicine.drugAndrostenediolmedicine.medical_specialtyADRENOLEUKODYSTROPHYATP Binding Cassette Transporter Subfamily D03 medical and health sciencesABCD3Internal medicinemedicineABCD2AnimalsPPAR alpha[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyRats Wistar030304 developmental biologyActivator (genetics)Body Weightnutritional and metabolic diseasesMembrane ProteinsDehydroepiandrosteronemedicine.diseaseRatsMice Inbred C57BLEndocrinologychemistrybiology.proteinHepatocytesATP-Binding Cassette TransportersAcyl-CoA Oxidase030217 neurology & neurosurgery
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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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