Search results for "PEROXISOME"

showing 10 items of 232 documents

Peroxisome-proliferator-activated receptors as physiological sensors of fatty acid metabolism: molecular regulation in peroxisomes

2001

The enzymes required for the beta-oxidation of fatty acyl-CoA are present in peroxisomes and mitochondria. Administration of hypolipidaemic compounds such as clofibrate to rodents leads to an increase in the volume and density of peroxisomes in liver cells. These proliferators also induce simultaneously the expression of genes encoding acyl-CoA oxidase, enoyl-CoA hydratase-hydroxyacyl-CoA dehydrogenase (multifunctional enzyme) and thiolase (3-ketoacyl-CoA thiolase). All these enzymes are responsible for long-chain and very-long-chain fatty acid beta-oxidation in peroxisomes. Similar results were observed when rat hepatocytes, or liver-derived cell lines, were cultured with a peroxisome prol…

Transcriptional ActivationGuinea PigsResponse elementReceptors Cytoplasmic and NuclearBiologyBiochemistryGene Expression Regulation EnzymologicMicechemistry.chemical_compoundPeroxisomesAnimalsAcetyl-CoA C-AcetyltransferasePhosphorylationTranscription factorProtein Kinase Cchemistry.chemical_classificationFatty acid metabolismThiolaseFatty AcidsFatty acidPeroxisomeRatsLiverchemistryBiochemistryAcetyl-CoA C-acetyltransferasePeroxisome proliferator-activated receptor alphaSignal TransductionTranscription FactorsBiochemical Society Transactions
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Peroxisome proliferators and peroxisome proliferator activated receptors (PPARs) as regulators of lipid metabolism.

1997

Peroxisome proliferation (PP) in mammalian cells, first described 30 years ago, represents a fascinating field of modern research. Major improvements made in its understanding were obtained through basic advances that have opened up new areas in cell biology, biochemistry and genetics. A decade after the first report on PP, a new metabolic pathway (peroxisomal beta-oxidation) and its inducibility by peroxisome proliferators were discovered. More recently, a new type of nuclear receptor, the peroxisome proliferator-activated receptor (PPAR), has been described. The first PPAR was discovered in 1990. Since then, many other PPARs have been characterized. This original class of nuclear receptor…

Transcriptional ActivationPeroxisome ProliferationPeroxisome proliferator-activated receptorReceptors Cytoplasmic and NuclearBiologyLigandsBiochemistryMicrobodiesGene Expression Regulation EnzymologicMicrosomesAnimalsHumansReceptorHypolipidemic Agentschemistry.chemical_classificationFatty AcidsLipid metabolismGeneral MedicinePeroxisomeLipid MetabolismCell biologyMitochondriaBiochemistrychemistryNuclear receptorLiverlipids (amino acids peptides and proteins)Peroxisome proliferator-activated receptor alphaAcyl-CoA OxidaseSignal transductionOxidoreductasesOxidation-ReductionSignal TransductionTranscription FactorsBiochimie
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Regulation of the peroxisomal β-oxidation-dependent pathway by peroxisome proliferator-activated receptor α and kinases

2000

The first PPAR (peroxisome proliferator-activated receptor) was cloned in 1990 by Issemann and Green (Nature 347:645-650). This nuclear receptor was so named since it is activated by peroxisome proliferators including several drugs of the fibrate family, plasticizers, and herbicides. This receptor belongs to the steroid receptor superfamily. After activation by a specific ligand, it binds to a DNA response element, PPRE (peroxisome proliferator response element), which is a DR-1 direct repeat of the consensus sequence TGACCT x TGACCT. This mechanism leads to the transcriptional activation of target genes (Motojima et al., J Biol Chem 273:16710-16714, 1998). After the first discovery, severa…

Transcriptional ActivationPeroxisome proliferator-activated receptor gammamedicine.drug_classReceptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorFibrateBiologyBiochemistryPhosphatidylinositol 3-KinasesmedicineAnimalsHumansPhosphorylationProtein kinase AProtein Kinase CPharmacologychemistry.chemical_classificationPeroxisomeNuclear receptorchemistryBiochemistryPeroxisome Proliferatorslipids (amino acids peptides and proteins)Peroxisome proliferator-activated receptor alphaSignal transductionSignal TransductionTranscription FactorsBiochemical Pharmacology
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The POT1 gene for yeast peroxisomal thiolase is subject to three different mechanisms of regulation

1992

The Saccharomyces cerevisiae POT1 gene is, as are other yeast peroxisomal protein genes, inducible by fatty acids and repressible by glucose. We have now found that it is also induced during the stationary phase of the culture. To investigate these three regulatory circuits, we have studied the mRNA levels of regulatory mutants as well as the changes in chromatin structure upon gene activation. We conclude that the regulation of transcriptional activity in glucose repression, oleate induction, and stationary phase induction follow different molecular mechanisms. We suggest that this multiplicity of regulatory mechanisms may represent a general rule for the yeast peroxisomal protein genes.

Transcriptional ActivationTranscription GeneticGenes FungalSaccharomyces cerevisiaeMutantOleic AcidsSaccharomyces cerevisiaeMicrobodiesMicrobiologyGene Expression Regulation FungalGene expressionRNA MessengerAcetyl-CoA C-AcetyltransferaseMolecular BiologyGeneRegulation of gene expressionbiologyCell CycleFungal geneticsRNA FungalPeroxisomebiology.organism_classificationChromatinChromatinGlucoseBiochemistryOleic AcidMolecular Microbiology
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A Molecular Dynamics-Shared Pharmacophore Approach to Boost Early-Enrichment Virtual Screening: A Case Study on Peroxisome Proliferator-Activated Rec…

2016

Molecular dynamics (MD) simulations can be used, prior to virtual screening, to add flexibility to proteins and study them in a dynamic way. Furthermore, the use of multiple crystal structures of the same protein containing different co-crystallized ligands can help elucidate the role of the ligand on a protein's active conformation, and then explore the most common interactions between small molecules and the receptor. In this work, we evaluated the contribution of the combined use of MD on crystal structures containing the same protein but different ligands to examine the crucial ligand-protein interactions within the complexes. The study was carried out on peroxisome proliferator-activat…

Virtual screening0301 basic medicinePeroxisome proliferator-activated receptorComputational biologyMolecular Dynamics SimulationCrystallography X-RayLigandsPPARα01 natural sciencesBiochemistryDrug design03 medical and health sciencesMolecular dynamics0103 physical sciencesDrug DiscoveryHumansPPAR alphaGeneral Pharmacology Toxicology and PharmaceuticsPharmacologychemistry.chemical_classificationVirtual screeningBinding Sites010304 chemical physicsLigandOrganic ChemistryDynamic pharmacophoreSmall moleculeProtein Structure TertiaryMolecular Docking Simulation030104 developmental biologyROC CurvechemistryDocking (molecular)Area Under CurvePharmacology Toxicology and Pharmaceutics (all)Molecular dockingMolecular MedicinePeroxisome proliferator-activated receptor alphaPharmacophoreProtein BindingChemMedChem
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Oral administration of vitamin C decreases muscle mitochondrial biogenesis and hampers training-induced adaptations in endurance performance

2008

Background Exercise practitioners often take vitamin C supplements because intense muscular contractile activity can result in oxidative stress, as indicated by altered muscle and blood glutathione concentrations and increases in protein, DNA, and lipid peroxidation. There is, however, considerable debate regarding the beneficial health effects of vitamin C supplementation. Objective This study was designed to study the effect of vitamin C on training efficiency in rats and in humans. Design The human study was double-blind and randomized. Fourteen men (27-36 y old) were trained for 8 wk. Five of the men were supplemented daily with an oral dose of 1 g vitamin C. In the animal study, 24 mal…

VitaminAdultMalemedicine.medical_specialtyAntioxidantmedicine.medical_treatmentPeroxisome Proliferator-Activated ReceptorsMedicine (miscellaneous)Administration OralAscorbic AcidBiologymedicine.disease_causeAntioxidantsLipid peroxidationMitochondrial Proteinschemistry.chemical_compoundOxygen ConsumptionDouble-Blind MethodInternal medicinemedicineAnimalsHumansRats Wistarchemistry.chemical_classificationNutrition and DieteticsCross-Over StudiesVitamin CNuclear Respiratory Factor 1Glutathione peroxidaseAscorbic acidAdaptation PhysiologicalMitochondria MuscleRatsDNA-Binding ProteinsOxidative StressEndocrinologychemistryMitochondrial biogenesisDietary SupplementsPhysical EnduranceReactive Oxygen SpeciesOxidative stressTranscription Factors
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Etude structure/fonction du demi-transporteur ABCD2 dans le contexte de l'Adrénoleucodystrophie liée à l'X

2013

X-linked Adrenoleukodystrophy (X-ALD) is a rare neurodegenerative disease caused by deficiency of the peroxisomal half-transporter ABCD1, implicated in very long chain fatty acids import. Two additional half-transporters are located in the peroxisomal membrane: ABCD2 and ABCD3. Over-expression of ABCD2 is known to compensate for ABCD1 deficiency, making ABCD2 a therapeutic target for X-ALD treatment. In this context, the main objective of my thesis was to investigate the function and the structure of ABCD2, and more broadly, of peroxisomal ABC transporters.Half-transporters must at least dimerize to form a functional transporter. Alternative dimerization could modulate substrate specificity…

X-ALD[ SDV.BC ] Life Sciences [q-bio]/Cellular BiologyOligomérisation[SDV.BC]Life Sciences [q-bio]/Cellular BiologyPeroxisomeFunctional redundancyTransporteurs ABCABC transportersRedondance fonctionnelle[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyOligomerization[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyDimères ABC chimériquesPeroxysome[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyChimeric ABC dimers[SDV.BC] Life Sciences [q-bio]/Cellular Biology
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Structure-function analysis of peroxisomal ATP-binding cassette transporters using chimeric dimers

2014

Background: Peroxisomal ABC transporters are predicted to function as homodimers in mammals. [br/] Results: ABCD1 interacts with ABCD2. Chimeric proteins mimicking full-length dimers represent novel tools for functional study. Artificial homodimers and heterodimers are functional. [br/] Conclusion: Interchangeability between ABCD1 and ABCD2 is confirmed, but PUFA transport depends on ABCD2. [br/] Significance: For the first time, heterodimers in mammals are proven to be functional.[br/] ABCD1 and ABCD2 are two closely related ATP-binding cassette half-transporters predicted to homodimerize and form peroxisomal importers for fatty acyl-CoAs. Available evidence has shown that ABCD1 and ABCD2 …

[SDV.BA] Life Sciences [q-bio]/Animal biologyprotéine chimereanimal diseasesATP-binding cassette transporterProximity ligation assayProtein Chimerabiochimie structurale[ SDV.BA ] Life Sciences [q-bio]/Animal biologyPolymerase Chain ReactionBiochemistryGreen fluorescent proteininteraction moléculaireMice[ CHIM.OTHE ] Chemical Sciences/Otherhomodimèrereproductive and urinary physiologyAnimal biologyhétérodimèrechemistry.chemical_classification[SDV.BA]Life Sciences [q-bio]/Animal biologymammifèreTransfectionPeroxisomeprotéine de fusionBiochemistry[CHIM.OTHE] Chemical Sciences/OtherDimerizationPlasmidsABC Transporter;Fatty Acid;Peroxisome;Protein Chimera;Protein-Protein Interactiontransporteur abcBiologyPeroxisomeCell LineProtein–protein interactionStructure-Activity RelationshipMembrane BiologyBiologie animaleparasitic diseasesAutre (Chimie)PeroxisomesAnimalsHumansMolecular BiologyDNA PrimersBase SequenceABCD2fungiABCD1Fatty acidCell BiologyFusion proteinRatsProtein-Protein InteractionABC TransporterchemistryATP-Binding Cassette TransportersOther[CHIM.OTHE]Chemical Sciences/OtherFatty Acid
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New molecular aspects of regulation of mitochondrial activity by fenofibrate and fasting

2000

Abstract Fenofibrate and fasting are known to regulate several genes involved in lipid metabolism in a similar way. In this study measuring several mitochondrial enzyme activities, we demonstrate that, in contrast to citrate synthase and complex II, cytochrome c oxidase (COX) is a specific target of these two treatments. In mouse liver organelles, Western blot experiments indicated that mitochondrial levels of p43, a mitochondrial T3 receptor, and mitochondrial peroxisome proliferator activated receptor (mt-PPAR), previously described as a dimeric partner of p43 in the organelle, are increased by both fenofibrate and fasting. In addition, in PPARα-deficient mice, this influence was abolishe…

[SDV]Life Sciences [q-bio]Receptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorMitochondria LiverMitochondrionBiochemistryMice0302 clinical medicineFenofibrateStructural BiologyBIOLOGIE CELLULAIRECitrate synthaseFibrateReceptorComputingMilieux_MISCELLANEOUSMice Knockoutchemistry.chemical_classification0303 health sciencesFenofibratebiologyElectron Transport Complex IIFastingPeroxisomeDNA-Binding ProteinsSuccinate Dehydrogenase[SDV] Life Sciences [q-bio]OxidoreductasesDimerizationmedicine.drugPeroxisome proliferator activated receptormedicine.medical_specialtyBiophysicsCitrate (si)-Synthase[INFO] Computer Science [cs]Mitochondrial T3 receptorElectron Transport Complex IV03 medical and health sciencesMultienzyme ComplexesInternal medicineGeneticsmedicineAnimalsCytochrome c oxidase[INFO]Computer Science [cs]MitochondrionMolecular BiologyCrosses Genetic030304 developmental biologyOrganellesLipid metabolismCell BiologyMice Inbred C57BLEndocrinologychemistrybiology.protein030217 neurology & neurosurgeryTranscription Factors
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l ‐carnitine: Structure and Function

2011

l-carnitine is found in nearly all living cells. l-carnitine present in human body can be either provided by a biosynthetic pathway or by food. Carnitine plays a major role in lipid and energy metabolism. In the human body, the primary role of l-carnitine is to shuttle long-chain fatty acids into the mitochondria where they are used to produce energy. l-carnitine is also involved in the peroxisomal oxidative metabolism and serves as a cofactor for various enzymatic reactions. Several reports suggest that l-carnitine may act as an anti-oxidant agent and limit the deleterious effects of free radicals. Many studies have estimated the role and the potential effectiveness of l-carnitine in vario…

biologySkeletal muscleLipid metabolismPhysical exerciseMitochondrionPeroxisomeCofactormedicine.anatomical_structureBiochemistrybiology.proteinmedicineCarnitineFunction (biology)medicine.drugeLS
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