Search results for "Acetyl-CoA C-Acyltransferase"

showing 7 items of 7 documents

Targeted disruption of the peroxisomal thiolase B gene in mouse: a new model to study disorders related to peroxisomal lipid metabolism

2004

The peroxisomal beta-oxidation system consists of four steps catalysed by three enzymes: acyl-CoA oxidase, 3-hydroxyacyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase (multifunctional enzyme) and thiolase. In humans, thiolase activity is encoded by one gene, whereas in rodents, three enzymes encoded by three distinct genes (i.e. thiolase A, thiolase B and SCP2/thiolase) catalyse the thiolase activity. So far, acyl-CoA oxidase- and multifunctional enzyme-deficient patients have been identified and knock-out mice for these genes have been produced. Conversely, no isolated thiolase-deficient patient has been found, and no thiolase (A or B)-deficient mice have been generated. Hence, to better u…

DehydrogenaseBiologymedicine.disease_causeBiochemistryGene Expression Regulation EnzymologicPeroxisomal DisordersMiceStructure-Activity RelationshipPeroxisomesmedicineAnimalsHumansRNA MessengerGeneHydro-LyasesSCP2chemistry.chemical_classificationMutationOxidase testThiolaseStem Cells3-Hydroxyacyl CoA DehydrogenasesGeneral MedicinePeroxisomeAcetyl-CoA C-AcyltransferaseEmbryo MammalianLipid MetabolismMolecular biologyMice Mutant StrainsMice Inbred C57BLDisease Models AnimalPhenotypeEnzymechemistryBiochemistryAcyl-CoA OxidaseBiochimie
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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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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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The peroxisome proliferator response element (PPRE) present at positions -681/-669 in the rat liver 3-ketoacyl-CoA thiolase B gene functionally inter…

2000

Although previous data showed that the putative thiolase B PPRE located at -681/-669 bind the PPARalpha-RXRalpha heterodimer in vitro (Kliewer et al. (1992) Nature 358, 771-774), there is no evidence about the functional role of this element. By gel mobility-shift assay, we found an interaction of this PPRE with not only PPARalpha but also with HNF-4. By transfection of cells with the putative PPRE-driven luciferase reporter vector and PPARalpha, we found no significant activation of the luciferase gene expression, in contrast to the case with reporter expression driven by the PPRE of the peroxisomal bifunctional enzyme. On the other hand, HNF-4 activated the luciferase gene expression driv…

Response elementBiophysicsReceptors Cytoplasmic and NuclearBiologyTransfectionBiochemistryDNA-binding proteinPeroxisomal Bifunctional EnzymeGenes ReporterGene expressionAnimalsMolecular BiologyGeneDNA PrimersBase SequenceThiolaseCell BiologyTransfectionDNAAcetyl-CoA C-AcyltransferasePhosphoproteinsMolecular biologyRatsDNA-Binding ProteinsHepatocyte nuclear factor 4Hepatocyte Nuclear Factor 4LiverCOS CellsPeroxisome ProliferatorsTranscription FactorsBiochemical and biophysical research communications
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A new glucose-repressible gene identified from the analysis of chromatin structure in deletion mutants of yeast SUC2 locus.

1991

We have previously shown that some changes occur in the chromatin structure of the 3' flank of the yeast SUC2 gene in going from a repressed to an active state. In an attempt to find out the causes of these changes, we have carried out experiments in which mutant copies of SUC2 locus lacking either 5' or 3' flanks have been analysed for their transcriptional activity and chromatin structure. These experiments allowed us to discard any relationship between SUC2 transcription and chromatin changes within its 3'flank. Sequencing of this flank and mRNA analysis, however, resulted in the location of a putative peroxisomal 3-oxoacyl-CoA thiolase gene (POT1), which is repressible by glucose. The d…

Transcription GeneticSaccharomyces cerevisiaeMutantGenes FungalMolecular Sequence DataBioengineeringLocus (genetics)Saccharomyces cerevisiaeApplied Microbiology and BiotechnologyBiochemistryOpen Reading FramesGene Expression Regulation FungalGeneticsAmino Acid SequenceDNA FungalGeneChIA-PETRegulation of gene expressionGeneticsbiologyBase SequenceNucleic acid sequencebiology.organism_classificationAcetyl-CoA C-AcyltransferaseBlotting NorthernChromatinChromatinGlucoseMutagenesisBiotechnologyPlasmidsYeast (Chichester, England)
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Disturbances in cholesterol, bile acid and glucose metabolism in peroxisomal 3-ketoacylCoA thiolase B deficient mice fed diets containing high or low…

2014

SPE IPM UB; International audience; : The peroxisomal 3-ketoacyl-CoA thiolase B (ThB) catalyzes the thiolytic cleavage of straight chain 3-ketoacyl-CoAs. Up to now, the ability of ThB to interfere with lipid metabolism was studied in mice fed a routinely laboratory chow enriched or not with the synthetic agonist Wy14,643, a pharmacological activator of the nuclear hormone receptor PPARα. The aim of the present study was therefore to determine whether ThB could play a role in obesity and lipid metabolism when mice are chronically fed a synthetic High Fat Diet (HFD) or a Low Fat Diet (LFD) as a control diet. To investigate this possibility, wild-type (WT) mice and mice deficient for Thb (Thb(…

lathosterol.medicine.medical_specialtymedicine.drug_classLathosterolCarbohydrate metabolismBiologyCholesterol 7 alpha-hydroxylaseDiet High-FatBiochemistrylathosterolBile Acids and Saltschemistry.chemical_compoundMiceInternal medicineIntestine Smallmedicine[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyAnimals[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyInsulin-Like Growth Factor I[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular Biology2. Zero hunger[SDV.MHEP.EM] Life Sciences [q-bio]/Human health and pathology/Endocrinology and metabolismbile acidsBile acidFatty acid metabolismCholesterolCholesterol HDLfood and beveragesLipid metabolismGeneral Medicine[SDV.MHEP.EM]Life Sciences [q-bio]/Human health and pathology/Endocrinology and metabolism[ SDV.MHEP.EM ] Life Sciences [q-bio]/Human health and pathology/Endocrinology and metabolismAcetyl-CoA C-AcyltransferaseDietary FatsLiver GlycogenEndocrinologyCholesterolGlucosehypoglycemiade novo biosynthesis of cholesterolchemistryGrowth HormoneACOX1lipids (amino acids peptides and proteins)peroxisomal 3-ketoacyl-CoA thiolase B
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Age-related changes in cholesterol metabolism in macrosomic offspring of rats with streptozotocin-induced diabetes.

2001

The aim of this study was to determine the impact of diabetic macrosomia on cholesterol and lipoprotein metabolism. Age-related changes in the activities of serum LCAT, hepatic HMG-CoA reductase, cholesterol 7α-hydroxylase, and ACAT, the major enzymes involved in cholesterol metabolism, were determined in macrosomic offspring of streptozotocin-induced diabetic rats. Hepatic, serum, and lipoprotein cholesterol contents were also examined. Mild hyperglycemia in pregnant rats was induced by intraperitoneal injection of streptozotocin (40 mg/kg body weight) on day 5 of gestation. Control pregnant rats were injected with citrate buffer. At birth, macrosomic pups had higher serum, LDL-HDL1, and H…

medicine.medical_specialtyOffspringmedicine.medical_treatmentLipoproteinsLCATIntraperitoneal injectionQD415-436GrowthReductaseBiologyBiochemistryStreptozocinDiabetes Mellitus ExperimentalFetal MacrosomiaPhosphatidylcholine-Sterol O-Acyltransferasechemistry.chemical_compoundEndocrinologyHMG-CoA reductasePregnancyInternal medicineDiabetes mellitusmedicineAnimalsmacrosomiaRats Wistarmaternal diabetesCholesterol 7-alpha-Hydroxylasecholesterol 7α-hydroxylaseCholesterolCell Biologymedicine.diseaseStreptozotocinAcetyl-CoA C-AcyltransferaseHydroxymethylglutaryl-CoA reductaseACATRatsEndocrinologyCholesterolchemistryLiverHydroxymethylglutaryl-CoA-Reductases NADP-dependentHyperglycemiaPrenatal Exposure Delayed EffectsGestationPregnancy Animallipids (amino acids peptides and proteins)FemaleHydroxymethylglutaryl CoA Reductasesmedicine.drugJournal of lipid research
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