Search results for "Peroxisomes"

showing 10 items of 27 documents

Changes of peroxisomal fatty acid metabolism during cold acclimatization in hibernating jerboa (Jaculus orientalis)

2003

Abstract Jerboa (Jaculus orientalis) is a deep hibernator originating from sub-desert highlands and represents an excellent model to help to understand the incidence of seasonal variations of food intake and of body as well as environmental temperatures on lipid metabolism. In jerboa, hibernation processes are characterized by changes in the size of mitochondria, the number of peroxisomes in liver and in the expression of enzymes linked to fatty acid metabolism. In liver and kidney, cold acclimatization shows an opposite effect on the activities of the mitochondrial acyl-CoA dehydrogenase (–50%) and the peroxisomal acyl-CoA oxidase (AOX) (+50%), while in brown and white adipose tissues, bot…

Malemedicine.medical_specialtyAcclimatizationAdipose tissueRodentiaWhite adipose tissueBiologyFatty acid degradationBiochemistryAcclimatizationchemistry.chemical_compoundHibernationInternal medicineBrown adipose tissuePeroxisomesmedicineAnimalsRNA MessengerFatty acid metabolismFatty AcidsLipid metabolismGeneral MedicinePeroxisomeMitochondriaCold TemperatureEnzyme ActivationEndocrinologymedicine.anatomical_structureLiverchemistryBiochemistryAcyl-CoA OxidaseBody Temperature RegulationBiochimie
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Molecular cloning, gene structure and expression profile of two mouse peroxisomal 3-ketoacyl-CoA thiolase genes

2004

Abstract Background In rats, two peroxisomal 3-ketoacyl-CoA thiolase genes (A and B) have been cloned, whereas only one thiolase gene is found in humans. The aim of this study was thus to clone the different mouse thiolase genes in order to study both their tissue expression and their associated enzymatic activity. Results In this study, we cloned and characterized two mouse peroxisomal 3-ketoacyl-CoA thiolase genes (termed thiolase A and B). Both thiolase A and B genes contain 12 exons and 11 introns. Using RNA extracted from mouse liver, we cloned the two corresponding cDNAs. Thiolase A and B cDNAs possess an open reading frame of 1272 nucleotides encoding a protein of 424 amino acids. In…

Molecular Sequence Datalcsh:Animal biochemistryGene Expressionexpérimentation animalesourislcsh:BiochemistryMiceFenofibratePeroxisomesAnimals[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyTissue Distributionlcsh:QD415-436Amino Acid SequenceRNA MessengerCloning Molecularlcsh:QP501-801adn complémentaireBase Sequencegèneactivité enzymatiquemammifèreBIOLOGIE MOLECULAIREAcetyl-CoA C-AcyltransferasefoieGene Componentsprotéinegénie génétiqueclonageResearch Articleexpression des gènesBMC Biochemistry
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Evolutionary aspects of peroxisomes as cell organelles, and of genes encoding peroxisomal proteins

2001

Peroxisomes are present in most eukaryotic cell types, and have different enzymatic content and metabolic functions throughout the life scale. The endosymbiotic origin of these DNA-devoid organelles is supported by evolutionary data concerning genes encoding not only most peroxisomal proteins, but also several transcriptional factors regulating their expression such as peroxisome proliferator-activated receptors.

OrganellesNuclear ProteinsReceptors Cytoplasmic and NuclearCell BiologyGeneral MedicinePlantsMitochondrionPeroxisomeBiologyMicrobodiesCell biologyEvolution MolecularGene Expression RegulationBiochemistryPhylogeneticsOrganellePeroxisomesAnimalsHumansMicrobodyReceptorTranscription factorGeneTranscription FactorsBiology of the Cell
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The human peroxisome in health and disease: The story of an oddity becoming a vital organelle

2013

Abstract Since the first report by Rhodin in 1954, our knowledge on mammalian microbodies/peroxisomes has known several periods. An initial two decades period (1954–1973) has contributed to the biochemical individualisation of peroxisomes as a new class of subcellular organelles (de Duve, 1965). The corresponding research period failed to define a clear role of mammalian peroxisomes in vital functions and intermediary metabolism, explaining why feeling that peroxisomes might be in the human cell oddities has prevailed during several decades. The period standing from 1973 to nowadays has progressively removed this cell oddity view of peroxisomes by highlighting vital function and metabolic r…

Peroxisome Proliferator-Activated ReceptorsDiseaseBiologyCell FractionationMicrobodiesBiochemistryPeroxisomal DisordersOrganellePeroxisomal disorderCentrifugation Density GradientPeroxisomesmedicineAnimalsHumansMicrobodyZellweger SyndromeOrganelle envelopeFatty AcidsGeneral MedicinePeroxisomeLipid Metabolismmedicine.diseaseCell biologyBiochemistryNuclear receptorMetabolic Networks and PathwaysFunction (biology)Biochimie
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Functional characterization of a peroxisome proliferator response-element located in the intron 3 of rat peroxisomal thiolase B gene.

2003

Expression of the rat peroxisomal 3-ketoacyl-CoA thiolase gene B is induced by peroxisome proliferators. Although a sequence element like a peroxisome proliferator-activated receptor (PPAR)-binding site is located in the promoter region of this gene, we previously found that this element is competent for the activation by hepatocyte nuclear factor-4, but not functional with PPARalpha. We describe here a new peroxisome proliferator-response element located in the intron 3 (+1422/+1434) that binds in vitro the PPARalpha/retinoid X receptor alpha heterodimer and confers the induction by PPARalpha in transfection assays. We propose a model of regulation of the rat thiolase B gene involving thos…

Peroxisome proliferator-activated receptor gammaResponse elementBiophysicsPeroxisome proliferator-activated receptorReceptors Cytoplasmic and NuclearRetinoid X receptorBiochemistryGene Expression Regulation EnzymologicStructure-Activity RelationshipPeroxisomesAnimalsAcetyl-CoA C-AcetyltransferaseMolecular BiologyCells Culturedchemistry.chemical_classificationThiolaseChemistryCell BiologyPhosphoproteinsMolecular biologyIntronsRatsDNA-Binding ProteinsBiochemistryHepatocyte Nuclear Factor 4LiverPeroxisome proliferator-activated receptor deltaPeroxisome ProliferatorsPeroxisome proliferator-activated receptor alphaPPARGC1BTranscription FactorsBiochemical and biophysical research communications
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Hepatic steatosis and peroxisomal fatty acid beta-oxidation.

2012

Three subhepatocellular compartments concur for fatty acids degradation including ω-oxidation in endoplasmic reticulum and β-oxidation in both mitochondria and peroxisomes. Deficits affecting the peroxisomal physiology may be associated with multiple metabolic disturbances. Nowadays, a growing body of evidence underlines the key role of peroxisomal β-oxidation in the sensing of lipid metabolism through the production/degradation of some essential metabolites. Lessons from several mice models strengthen the link between fatty acid β-oxidation in peroxisomes and the nuclear hormone receptor Peroxisome Proliferator-Activated Receptor (PPAR)-α with an additional level of coregualtor complexity,…

Pharmacologychemistry.chemical_classificationClinical BiochemistryFatty AcidsLiver NeoplasmsFatty acidPeroxisome proliferator-activated receptorLipid metabolismPeroxisomeBiologyFatty acid beta-oxidationmedicine.diseaseFatty LiverchemistryBiochemistrymedicinePeroxisomesAnimalsHumansPPAR alphaPeroxisome proliferator-activated receptor alphaSteatosisFlux (metabolism)Oxidation-ReductionCurrent drug metabolism
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PPARα/HNF4α Interplay on Diversified Responsive Elements. Relevance in the Regulation of Liver Peroxisomal Fatty Acid Catabolism

2012

In mammals, the liver is the major organ of fatty acid catabolism. This pathway is involved in both mitochondria and peroxisome. While mitochondria breaks down fatty acids with short, medium and long carbon chains, peroxisomes are involved in the catabolism of very long and branched chain fatty acids, which are degraded by three enzymes: acyl-CoA oxidase, multifunctional enzyme and thiolase enzyme. The active pathway results mainly from a tight transcriptional control of these gene-encoding enzymes. Two major nuclear receptors that are highly expressed in this organ are involved in this control, e.g. PPARα (peroxisome proliferator-activated receptor, α isoform) and HNF4α (hepatic nuclear fa…

Pharmacologychemistry.chemical_classificationFatty acid metabolismCatabolismThiolaseFatty AcidsClinical BiochemistryPeroxisome proliferator-activated receptorMetabolismPeroxisomeBiologyResponse Elementschemistry.chemical_compoundGene Expression RegulationHepatocyte Nuclear Factor 4LiverHepatocyte nuclear factor 4BiochemistrychemistryNuclear receptorPeroxisomesAnimalsHumansPPAR alphaCurrent Drug Metabolism
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Prevention by Dietary Polyphenols (Resveratrol, Quercetin, Apigenin) Against 7-Ketocholesterol-Induced Oxiapoptophagy in Neuronal N2a Cells: Potentia…

2020

The Mediterranean diet is associated with health benefits due to bioactive compounds such as polyphenols. The biological activities of three polyphenols (quercetin (QCT), resveratrol (RSV), apigenin (API)) were evaluated in mouse neuronal N2a cells in the presence of 7-ketocholesterol (7KC), a major cholesterol oxidation product increased in patients with age-related diseases, including neurodegenerative disorders. In N2a cells, 7KC (50 &micro

Programmed cell deathanimal diseasesSOD2N2a cellsApoptosisresveratrolmedicine.disease_causeoxiapoptophagyArticleCell LinequercetinMiceage-related diseasesmedicineAutophagyPeroxisomesAnimalsHumansApigeninlcsh:QH301-705.5Ketocholesterols7-ketocholesterolchemistry.chemical_classificationNeuronsReactive oxygen speciesDose-Response Relationship DrugChemistryfood and beveragesPolyphenolsNeurodegenerative DiseasesGeneral MedicinePeroxisomeMolecular biologyMitochondriaOxidative StresspolyphenolMitochondrial biogenesislcsh:Biology (General)ApoptosisACOX1Reactive Oxygen SpeciesoxysterolOxidative stressCells
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Peroxisomal and mitochondrial status of two murine oligodendrocytic cell lines (158N, 158JP): potential models for the study of peroxisomal disorders…

2009

International audience; In some neurodegenerative disorders (leukodystrophies) characterized by myelin alterations, the defect of peroxisomal functions on myelin-producing cells (oligodendrocytes) are poorly understood. The development of in vitro models is fundamental to understanding the physiopathogenesis of these diseases. We characterized two immortalized murine oligodendrocyte cell lines: a normal (158N) and a jimpy (158JP) cell line mutated for the proteolipid protein PLP/DM20. Fluorescence microscopy, flow cytometry, and western blotting analysis allow to identify major myelin proteins (PLP colocalizing with mitochondria; myelin basic protein), oligodendrocyte (CNPase and myelin oli…

Proteolipid protein 1BiochemistryMiceMyelinMESH : PhenylbutyratesperoxisomeIsomerasesMESH : Myelin Basic ProteinsEnoyl-CoA HydrataseCell Line TransformedUltrasonographybiologyMESH : Gene Expression RegulationMESH : Myelin Proteolipid Protein3-Hydroxyacyl CoA DehydrogenasesMESH : Myelin-Associated GlycoproteinMESH : Cell Line TransformedPeroxisomeMESH : Multienzyme ComplexesMESH : OligodendrogliaMESH : Enoyl-CoA HydrataseCatalaseFlow CytometryMESH : 3-Hydroxyacyl CoA DehydrogenasesPhenylbutyratesmitochondriaMyelin-Associated GlycoproteinOligodendrogliamyelinMESH : Antineoplastic Agentsmedicine.anatomical_structureMESH : Microscopy Electron TransmissionBiochemistryACOX1MESH : MitochondriaMESH : Acyl-CoA Oxidase2'3'-Cyclic-Nucleotide PhosphodiesterasesMESH : IsomerasesOxidation-ReductionMyelin ProteinsMESH : Flow CytometryAntineoplastic AgentsPeroxisomal Bifunctional EnzymeStatistics NonparametricMyelin oligodendrocyte glycoproteinCellular and Molecular NeuroscienceMicroscopy Electron TransmissionMultienzyme ComplexesMESH : CatalaseMESH : MicePeroxisomesmedicineAnimalsMESH : ATP-Binding Cassette TransportersMyelin Proteolipid ProteinMESH : Statistics Nonparametric[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH : Oxidation-ReductionMyelin Basic Proteinmurine oligodendrocytesMESH : 2'3'-Cyclic-Nucleotide PhosphodiesterasesPeroxisomal transportOligodendrocyteMyelin basic proteinGene Expression Regulationbiology.proteinATP-Binding Cassette TransportersMyelin-Oligodendrocyte GlycoproteinAcyl-CoA OxidaseMESH : AnimalsMESH : Peroxisomes
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The four murine peroxisomal ABC-transporter genes differ in constitutive, inducible and developmental expression.

1999

Four ATP-binding cassette (ABC) half-transporters have been identified in mammalian peroxisomes: adrenoleukodystrophy protein (ALDP), adrenoleukodystrophy-related protein (ALDRP), 70-kDa peroxisomal membrane protein (PMP70) and PMP70-related protein (P70R). Inherited defects in ALDP cause the neurodegenerative disorder X-linked adrenoleukodystrophy (X-ALD). By comparative Northern blot analyses we found each of the four murine peroxisomal ABC transporter mRNA species at maximum abundance only in a few tissues, which differed for each family member. The four genes were also regulated differentially during mouse brain development: ALDP mRNA was most abundant in embryonic brain and gradually d…

Response elementMolecular Sequence DataATP-binding cassette transporterMice Inbred StrainsBiologyATP Binding Cassette Transporter Subfamily DBiochemistryATP Binding Cassette Transporter Subfamily D Member 1MiceFenofibrateGene expressionmedicinePeroxisomesAnimalsNorthern blotATP Binding Cassette Transporter Subfamily B Member 1RNA MessengerPromoter Regions GeneticGeneHypolipidemic AgentsMice KnockoutMessenger RNABrainGene Expression Regulation DevelopmentalMembrane ProteinsProteinsBiological Transportmedicine.diseaseMolecular biologyNuclear receptorLiverAdrenoleukodystrophyATP-Binding Cassette TransportersEuropean journal of biochemistry
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