Search results for "Peroxisome Proliferation"

showing 10 items of 26 documents

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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Acute hepatotoxicity of the polycyclic musk 7-acetyl-1,1,3,4,4,6-hexamethyl-1,2,3,4-tetrahydronaphtaline (AHTN).

2000

Synthetic musks are present in fine fragrances, cosmetics, soaps and laundry detergents. One of the most important synthetic musks is 7-acetyl-1,1,3,4,4,6-hexamethyl-1,2,3,4-tetrahydro-naphthaline+ ++ (AHTN; annual production: about 1500 metric tons). An increasing number of studies show that AHTN accumulates in surface water and fish and can be detected in human adipose tissue, as well in human milk. In the present report it is shown that a single high dose of AHTN leads to acute hepatic damage in rats, characterized by single cell necrosis, inflammation, swelling of liver parenchymal cells, and the presence of cytoplasmic condensations in the hepatocytes, while at the ultrastructural leve…

MalebiologyDose-Response Relationship DrugEndoplasmic reticulumAdipose tissuePeroxisome ProliferationGeneral MedicineMitochondrionNaphthalenesToxicologyPerfumeRatsFatty Acids MonounsaturatedRats Sprague-DawleyCytolysisBiochemistryLiverToxicitybiology.proteinAnimalsEnzyme inducerCarcinogenToxicology letters
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Evaluation of the therapeutic potential of PPARalpha agonists for X-linked adrenoleukodystrophy.

2003

Adrenoleukodystrophy protein (ABCD1), a peroxisomal membrane protein, is mutated in patients affected by X-linked adrenoleukodystrophy (X-ALD). Adrenoleukodystrophy-related protein (ABCD2) is the closest relative of ABCD1. Pharmacological induction of ABCD2 gene expression has been proposed as a novel therapy strategy for X-ALD. Fibrates induce peroxisome proliferation and Abcd2 expression in rodent liver. Here we evaluate the possibility of using peroxisome proliferator-activated receptor alpha (PPARalpha) agonists for pharmacological induction of ABCD2 expression. In the liver of PPARalpha-deficient mice, both the constitutive and the fenofibrate-inducible Abcd2 gene expression was found …

Malemedicine.medical_specialtyEndocrinology Diabetes and MetabolismMolecular Sequence DataDrug Evaluation PreclinicalPeroxisome ProliferationReceptors Cytoplasmic and NuclearBiologySulfidesATP Binding Cassette Transporter Subfamily DResponse ElementsBiochemistrychemistry.chemical_compoundMiceEndocrinologyInternal medicineGene expressionGeneticsmedicineAnimalsAdrenoleukodystrophyMolecular BiologyGenePhenylurea CompoundsTetradecylthioacetic acidBrainmedicine.diseaseMolecular biologyIntronsMice Mutant StrainsSterol regulatory element-binding proteinDNA-Binding ProteinsMice Inbred C57BLButyratesSterolsEndocrinologychemistryGene Expression RegulationLiverCCAAT-Enhancer-Binding ProteinsSterol Regulatory Element Binding Protein 1AdrenoleukodystrophyATP-Binding Cassette TransportersSterol regulatory element-binding protein 2Sterol Regulatory Element Binding Protein 1Sterol Regulatory Element Binding Protein 2Transcription FactorsMolecular genetics and metabolism
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Difference between Guinea Pig and Rat in the Liver Peroxisomal Response to Equivalent Plasmatic Level of Ciprofibrate

1996

Abstract Guinea pig was previously classified as a species nonresponsive to peroxisome proliferators. However, none of the previous reports was based on pharmacokinetic data. Here, after a comparative pharmacokinetic study between guinea pig and rat, we evaluate the guinea pig liver peroxisomal response to ciprofibrate, a hypolipemic agent and a potent peroxisome proliferator in rat. (1) Pharmacokinetic results show that plasmatic concentrations of ciprofibrate are equivalent in guinea pig and rat when guinea pigs are treated with ciprofibrate at 30 mg/kg twice a day and rats are treated at 3 mg/kg once a day. (2) The treatment of guinea pigs at 30 mg/kg twice a day for 2 weeks leads to a s…

Malemedicine.medical_specialtyGuinea PigsBiophysicsGene ExpressionPeroxisome ProliferationBiologyCell FractionationMicrobodiesBiochemistryMixed Function OxygenasesGuinea pigClofibric AcidCytochrome P-450 Enzyme SystemSpecies SpecificityPharmacokineticsInternal medicinemedicineAnimalsRNA MessengerMolecular BiologyHypolipidemic AgentsMessenger RNAOxidase testFibric AcidsPeroxisomeBlotting NorthernRatsEndocrinologyLiverMicrosomeAcyl-CoA OxidaseCiprofibrateCytochrome P-450 CYP4ADNA ProbesOxidoreductasesmedicine.drugArchives of Biochemistry and Biophysics
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Response of genetically obese Zucker rats to ciprofibrate, a hypolipidemic agent, with peroxisome proliferation activity as compared to Zucker lean a…

1993

Genetically obese Zucker (fa/fa) rats were used as an experimental model to study the effects of hypolipidemic agents on peroxisome proliferation; comparison was made with Zucker lean phenotype (Fa/-) and Sprague-Dawley strain/phenotype. The pharmacokinetics of a single administration of ciprofibrate (1 or 3 mg/kg), appeared to be similar in all strains/phenotypes. After a 2-week oral administration at the same dosages, there were dosage-related increases in hepatocellular peroxisomal yield and in the hepatic enzymes' cyanide-insensitive acyl-CoA oxidase and catalase. The peroxisomal yield was less increased in Zucker than in Sprague-Dawley rats, while the enzyme activities were similarly i…

Malemedicine.medical_specialtyPeroxisome ProliferationBiologyMicrobodiesRats Sprague-Dawleychemistry.chemical_compoundClofibric AcidCytochrome P-450 Enzyme SystemSpecies SpecificityOral administrationReference ValuesInternal medicinemedicineAnimalsObesityEnzyme inducerTriglyceridesHypolipidemic AgentsTriglycerideCholesterolFibric AcidsCell BiologyGeneral MedicinePeroxisomeRatsRats ZuckerIsoenzymesEndocrinologyCholesterolchemistryLiverEnzyme InductionHypolipidemic Agentsbiology.proteinCiprofibratemedicine.drugBiology of the cell
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Role of thyroid state on induction by ciprofibrate of laurate hydroxylase and peroxisomal enzymes in rat liver microsomes.

1993

The effects of hypothyroidism and hyperthyroidism upon liver microsomal omega-laurate hydroxylase activity (cytochrome P450 IV A1-dependent), peroxisome proliferation marker enzyme activities and acyl CoA oxidase (AOX) expression induced by ciprofibrate (2 mg/kg/day during 8 days) were studied in the male Wistar rat so as to clarify firstly the possible involvement of thyroid hormones in the modification of peroxisomal ciprofibrate-induced enzyme activities in relation to hepatic microsomal cytochrome P450 IV A1 induction, and secondly the possible direct effect of thyroid hormones on the gene expression of specific peroxisomal enzymes. No significant change was found in the ciprofibrate-in…

Malemedicine.medical_specialtyThyroid HormonesPeroxisome ProliferationGlucuronatesGlycerolphosphate DehydrogenaseBiochemistryMicrobodiesMixed Function OxygenasesClofibric AcidCytochrome P-450 Enzyme SystemInternal medicinemedicineAnimalsEnzyme inducerRats WistarPharmacologyTriiodothyroninebiologyBody WeightFibric AcidsCytochrome P450Organ SizePeroxisomeEnoyl-CoA hydrataseRatsEndocrinologyGene Expression RegulationEnzyme InductionProtein Biosynthesisbiology.proteinMicrosomes LiverCiprofibrateCytochrome P-450 CYP4Amedicine.drugHormoneBiochemical pharmacology
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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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Influence of peroxisome proliferators on phosphoprotein levels in human and rat hepatic-derived cell lines.

1995

To elucidate the effect of peroxisome proliferators on the signal-transduction pathway, we have compared the effect of ciprofibrate, an hypolipaemic agent, on the overall phosphoprotein level between rat and human well differentiated hepatic derived cell lines. The phosphorylation status of several phosphoproteins in the rat Fao cell line was increased by the drug while no changes were observed in the human HepG2 cell line. In rat Fao cells, this increase, which is concentration and time dependent, can be as much as eightfold for 20-kDa and 22-kDa proteins. Wy-14,643, a non-fibrate molecule and a more potent peroxisome proliferator than ciprofibrate, increased the phosphorylation status of …

PhosphatasePeroxisome ProliferationBiologyBiochemistryMicrobodiesCell LineClofibric AcidmedicineAnimalsHumansPhosphorylationHypolipidemic AgentsKinaseFibric AcidsPhosphoproteinsRatsPyrimidinesBiochemistryLiverCell culturePhosphoproteinPhosphorylationPeroxisome proliferator-activated receptor alphaCiprofibrateOxidoreductasesmedicine.drugEuropean journal of biochemistry
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Gene Regulation of Peroxisomal Enzymes by Nutrients, Hormones and Nuclear Signalling Factors in Animal and Human Species

2003

Many peroxisomal enzymes are controlled at the transcriptional level. This gene regulation is well documented in liver from rodent species and is more important upon peroxisome proliferation, although both phenomena are not always associated. Understanding of this regulation comes largely from studies on PPARs (Peroxisome Proliferator-Activated Receptors). Other transcription factors including thyroid hormone receptors, glucocorticoid receptors, LXR, also influence peroxisomal gene expression often in combination with tissue specific cofactors (co-activators or co-repressors). In human tissues and cells, inducibility of peroxisomal enzymes often has not been investigated. De Craemer (1995) …

Regulation of gene expressionPristanic acidchemistry.chemical_compoundchemistryBiochemistryPeroxisome ProliferationPeroxisomeBiologyReceptorLiver X receptorTranscription factorPPAR agonist
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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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