Search results for "Coenzyme A"

showing 10 items of 30 documents

Mitochondrial respiration on rumenic and linoleic acids

2001

Rumenic acid ( cis -9, trans -11-C 18:2 ) represents approx. 80% of conjugated linoleic acid (CLA) in dairy products. CLA has been shown to exert beneficial effects on health, but little work has been devoted to the ability to oxidize CLA isomers and the role of these isomers in the modulation of β-oxidation flux. In the present study, respiration on rumenic acid was compared with that on linoleic acid ( cis -9, cis -12-C 18:2 ) with the use of rat liver mitochondria. In state-3, respiration was decreased by half with rumenic acid in comparison with linoleic acid. In the uncoupled state, respiration on CLA remained 30% lower. The lower ability to oxidize CLA was investigated through charact…

Linoleic acidConjugated linoleic acidCell RespirationMitochondria LiverMitochondrionBiochemistryFatty Acids MonounsaturatedLinoleic Acidchemistry.chemical_compoundOxygen ConsumptionCoenzyme A LigasesRespirationmedicineAnimalsPalmitoleic acidCarnitineATP synthasebiologyRumenic acidfood and beveragesStereoisomerismRatsCarnitine AcyltransferasesLiverchemistryBiochemistrybiology.proteinCattleDairy ProductsCaprylatesStearic Acidsmedicine.drugBiochemical Society Transactions
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Extracellular oxidoreduction potential modifies carbon and electron flow in Escherichia coli.

2000

ABSTRACT Wild-type Escherichia coli K-12 ferments glucose to a mixture of ethanol and acetic, lactic, formic, and succinic acids. In anoxic chemostat culture at four dilution rates and two different oxidoreduction potentials (ORP), this strain generated a spectrum of products which depended on ORP. Whatever the dilution rate tested, in low reducing conditions (−100 mV), the production of formate, acetate, ethanol, and lactate was in molar proportions of approximately 2.5:1:1:0.3, and in high reducing conditions (−320 mV), the production was in molar proportions of 2:0.6:1:2. The modification of metabolic fluxes was due to an ORP effect on the synthesis or stability of some fermentation enzy…

MESH : Models Chemical0106 biological sciencesMESH: Oxidation-ReductionMESH : Acetic AcidMESH : Escherichia coliMESH : NADFormatesOxaloacetatesMESH: Phosphoenolpyruvate CarboxylaseSuccinic AcidMESH: Alcohol DehydrogenaseMESH : CarbonMESH : EthanolMESH: Carbon Dioxide01 natural sciencesPhosphoenolpyruvatechemistry.chemical_compoundModels[INFO.INFO-BT]Computer Science [cs]/BiotechnologyAcetic Acid0303 health sciencesbiologyMESH: Escherichia coliMESH: Models ChemicalMESH : Acetyl Coenzyme AMESH: NADLactic acidMESH : Carbon DioxideBiochemistryFormic AcidsMESH: PhosphoenolpyruvateMESH: Acetic AcidMESH: Pyruvate KinaseMESH : Phosphoenolpyruvate CarboxylaseMESH: Oxaloacetic AcidsOxidation-Reduction[ INFO.INFO-BT ] Computer Science [cs]/BiotechnologyMESH: EthanolPhysiology and MetabolismPyruvate KinaseElectronsChemicalMESH: CarbonMESH : Formic AcidsChemostatMicrobiologyMESH: Fermentation03 medical and health sciencesAcetic acidMESH : Alcohol DehydrogenaseAcetyl Coenzyme AMESH : Fermentation010608 biotechnology[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyEscherichia coliFormate[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyLactic Acid[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMolecular Biology030304 developmental biologyAlcohol dehydrogenaseMESH : Oxidation-ReductionMESH: ElectronsEthanolEthanolMESH : Succinic AcidAlcohol DehydrogenaseCarbon DioxideNADMESH: Formic AcidsMESH : Pyruvate KinaseCarbonOxaloacetic AcidsPhosphoenolpyruvate CarboxylaseMESH: Succinic Acid[INFO.INFO-BT] Computer Science [cs]/BiotechnologychemistryModels ChemicalSuccinic acidMESH : Lactic AcidMESH : Oxaloacetic AcidsFermentationbiology.proteinFermentationMESH: Lactic AcidMESH : ElectronsMESH : PhosphoenolpyruvateMESH: Acetyl Coenzyme A
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Pathway of alpha-linolenic acid through the mitochondrial outer membrane in the rat liver and influence on the rate of oxidation. Comparison with lin…

1989

The movement of alpha-linolenic acid (C18:3, n-3) through the mitochondrial outer membrane to oxidation sites was studied in rat liver and compared with the movement of linoleic acid (C18:2, n-6) and oleic acid (C18:1, n-9). All differ in the degree of unsaturation, but have the same chain length and the same position of the first double bond when counted from the carboxyl end. The following results were obtained. (1) The overall beta-oxidation in total mitochondria was in the order C18:3, n-3 greater than C18:2, n-6 greater than C18:1, n-9, independent of the amount of albumin in the medium. (2) The rate of formation of acylcarnitine from acyl-CoA was higher with oleoyl-CoA than with linol…

MaleLinolenic AcidsLinoleic acidPotassiumchemistry.chemical_elementMitochondria LiverOleic AcidsMitochondrionIn Vitro TechniquesBiochemistryLinoleic Acidchemistry.chemical_compoundCarnitinemedicineAnimalsCarnitineMolecular BiologyDegree of unsaturationCarnitine O-PalmitoyltransferaseChemistryalpha-Linolenic acidBiological TransportRats Inbred StrainsCell BiologyIntracellular MembranesPeroxisomeRatsOleic acidBiochemistryLinoleic Acidslipids (amino acids peptides and proteins)Acyl Coenzyme AOxidation-Reductionmedicine.drugOleic AcidResearch ArticleThe Biochemical journal
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Induction of the fatty acid transport protein 1 and acyl-CoA synthase genes by dimer-selective rexinoids suggests that the peroxisome proliferator-ac…

2000

The intracellular fatty acid content of insulin-sensitive target tissues determines in part their insulin sensitivity. Uptake of fatty acids into cells is a controlled process determined in part by a regulated import/export system that is controlled at least by two key groups of proteins, i.e. the fatty acid transport protein (FATP) and acyl-CoA synthetase (ACS), which facilitate, respectively, the transport of fatty acids across the cell membrane and catalyze their esterification to prevent their efflux. Previously it was shown that the expression of the FATP-1 and ACS genes was controlled by insulin and by peroxisome proliferator-activated receptor (PPAR) agonists in liver or in adipose t…

MalePeroxisome proliferator-activated receptor gammaTime FactorsReceptors Retinoic AcidRetinoic acidReceptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorTretinoinRetinoid X receptorBiologyFatty Acid-Binding ProteinsBiochemistryMicechemistry.chemical_compoundCoenzyme A LigasesTumor Cells CulturedAnimalsHumansTissue DistributionMolecular BiologyNucleic Acid Synthesis InhibitorsCell Nucleuschemistry.chemical_classificationDose-Response Relationship DrugFatty AcidsMembrane ProteinsFatty acidMembrane Transport ProteinsSerum Albumin Bovine3T3 CellsCell BiologyFatty Acid Transport ProteinsRatsRats ZuckerRetinoic acid receptorRetinoid X ReceptorschemistryBiochemistryDactinomycinFree fatty acid receptorRNAPeroxisome proliferator-activated receptor alphaCaco-2 CellsCarrier ProteinsTranscription Factors
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Involvement of microsomal vesicles in part of the sensitivity of carnitine palmitoyltransferase I to malonyl-CoA inhibition in mitochondrial fraction…

1994

Liver mitochondrial fractions as normally isolated contain only 10-20% of total mitochondria and may not be representative of the whole mitochondrial population. This study was designed to evaluate the dependence of the sensitivity of carnitine palmitoyl-transferase I (CPT I) to malonyl-CoA inhibition in mitochondrial fractions that are not normally studied. Four fractions prepared from rat liver were found to be contaminated to different extents by microsome vesicles, on the basis of marker-enzyme activities and micrographic data. Purification of mitochondrial fractions on a Percoll gradient decreased to some extent the microsomal contamination, which was due in part to the existence of cl…

MalePopulationMitochondria LiverMitochondrionBiologyCell FractionationBiochemistrychemistry.chemical_compoundAdenosine TriphosphatemedicineCentrifugation Density GradientAnimalsCarnitineRats WistareducationMolecular Biologyeducation.field_of_studyCarnitine O-PalmitoyltransferaseEndoplasmic reticulumCell BiologyRatsMalonyl Coenzyme AMalonyl-CoABiochemistrychemistryMicrosomeMicrosomes LiverCarnitine palmitoyltransferase IPercollmedicine.drugResearch Article
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Effect of dietary n−3 and n−6 polyunsaturated fatty acids on lipid-metabolizing enzymes in obese rat liver

1994

This study was designed to examine whether n-3 and n-6 polyunsaturated fatty acids at a very low dietary level (about 0.2%) would alter liver activities in respect to fatty acid oxidation. Obese Zucker rats were used because of their low level of fatty acid oxidation, which would make increases easier to detect. Zucker rats were fed diets containing different oil mixtures (5%, w/w) with the same ratio of n-6/n-3 fatty acids supplied either as fish oil or arachidonic acid concentrate. Decreased hepatic triacylglycerol levels were observed only with the diet containing fish oil. In mitochondrial outer membranes, which support carnitine palmitoyltransferase I activity, cholesterol content was …

MaleUrate OxidaseMitochondria LiverBiochemistryMicechemistry.chemical_compoundDietary Fats UnsaturatedFatty Acids Omega-6Fatty Acids Omega-3AnimalsObesityFood scienceMonoamine OxidaseBeta oxidationchemistry.chemical_classificationCarnitine O-PalmitoyltransferasePalmitoyl Coenzyme ACholesterolOrganic ChemistryFatty acidCell BiologyPeroxisomeLipid MetabolismFish oilRatsRats ZuckerMalonyl Coenzyme AchemistryBiochemistryFatty Acids UnsaturatedMicrosomes LiverArachidonic acidCarnitine palmitoyltransferase ICarboxylic Ester HydrolasesSubcellular FractionsPolyunsaturated fatty acidLipids
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Mildronate, the inhibitor of l-carnitine transport, induces brain mitochondrial uncoupling and protects against anoxia-reoxygenation

2013

Abstract The preservation of mitochondrial function is essential for normal brain function after ischaemia-reperfusion injury. l -carnitine is a cofactor involved in the regulation of cellular energy metabolism. Recently, it has been shown that mildronate, an inhibitor of l -carnitine transport, improves neurological outcome after ischaemic damage of brain tissues. The aim of the present study was to elucidate the mitochondria targeted neuroprotective action of mildronate in the model of anoxia-reoxygenation-induced injury. Wistar rats were treated daily with mildronate ( per os ; 100 mg/kg) for 14 days. The acyl-carnitine profile was determined in the brain tissues. Mitochondrial respirati…

Malemedicine.medical_specialtyBioenergeticsCell RespirationMitochondrionBiologyNeuroprotectionCarnitine transportAdenosine TriphosphateCarnitineInternal medicineRespirationmedicineAnimalsCarnitineRats WistarHypoxiaPharmacologyBrainMetabolismMitochondriaRatsOxygenCitric acid cycleNeuroprotective AgentsEndocrinologyCarnitine AcyltransferasesAcyl Coenzyme AMethylhydrazinesmedicine.drugEuropean Journal of Pharmacology
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Hepatic steatosis is not due to impaired fatty acid oxidation capacities in C57BL/6J mice fed the conjugated trans-10,cis-12-isomer of linoleic acid.

2004

Decreased body fat mass and liver steatosis have been reported in mice fed diets containing the conjugated linoleic acid trans-10,cis-12-C18:2 (CLA2), but not in those fed diets containing cis-9,trans-11-C18:2 (CLA1). Because the decrease in fatty acid (FA) oxidation may cause fat accumulation, we questioned whether the effects of both CLAs on enzyme activities and mRNA expression were related to liver FA oxidation. To address this question, 7-wk-old male C57BL/6J mice were fed for 4 wk a diet supplemented with 1% CLA1, CLA2, or cis-9-C18:1 (control) esterified as triacylglycerols. In CLA2-fed mice, the proportions of CLA2 in the total FA of liver lipids were substantially lower than those …

Malemedicine.medical_specialtyLinoleic acidConjugated linoleic acidMedicine (miscellaneous)Mitochondria LiverBiologychemistry.chemical_compoundMiceDietary Fats UnsaturatedInternal medicinemedicineAnimalsLinoleic Acids ConjugatedCarnitineRNA MessengerEnzyme InhibitorsUnsaturated fatty acidTriglycerideschemistry.chemical_classificationNutrition and DieteticsCarnitine O-PalmitoyltransferaseEsterificationReverse Transcriptase Polymerase Chain ReactionFatty liverFatty AcidsFatty acidmedicine.diseaseFatty LiverMalonyl Coenzyme AMice Inbred C57BLEndocrinologychemistryBiochemistryLiverCarnitine palmitoyltransferase IOxidation-ReductionPolyunsaturated fatty acidmedicine.drug
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PLTP activity is a risk factor for subsequent cardiovascular events in CAD patients under statin therapy: the AtheroGene study.

2009

Phospholipid transferprotein (PLTP) mediates both net transfer and exchange of phospholipids between different lipoproteins. Although many studies have investigated the role of PLTP in atherogenesis, the role of PLTP in atherosclerotic diseases is unclear. We investigated the association of serum PLTP activity with the incidence of a combined endpoint (myocardial infarction and cardiovascular death) and its relation to other markers of atherosclerosis in 1,085 patients with angiographically documented coronary artery disease (CAD). In the median follow-up of 5.1 years, 156 patients had suffered from the combined endpoint of myocardial infarction or cardiovascular death including 47 of 395 p…

Malemedicine.medical_specialtyMyocardial InfarctionQD415-436Coronary Artery DiseaseKaplan-Meier Estimatelipid transfer proteinsBiochemistryCoronary artery diseasechemistry.chemical_compoundEndocrinologyRisk FactorsInternal medicinePhospholipid transfer proteinmedicineHumansMyocardial infarctionRisk factorPhospholipid Transfer Proteins3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitorsAgedCholesterolbusiness.industryProportional hazards modelConfoundingCase-control studyCell BiologyMiddle Agedmedicine.diseaseAtherosclerosisPrognosisEndocrinologychemistryCase-Control StudiesCardiologyFemaleHydroxymethylglutaryl-CoA Reductase InhibitorsbusinessPatient-Oriented and Epidemiological ResearchFollow-Up StudiesJournal of lipid research
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Structures of yeast peroxisomal Δ(3),Δ(2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks f…

2015

Δ3,Δ2-Enoyl-CoA isomerases (ECIs) catalyze the shift of a double bond from 3Z- or 3E-enoyl-CoA to 2E-enoyl-CoA. ECIs are members of the crotonase superfamily. The crotonase framework is used by many enzymes to catalyze a wide range of reactions on acyl-CoA thioesters. The thioester O atom is bound in a conserved oxyanion hole. Here, the mode of binding of acyl-CoA substrate analogues to peroxisomalSaccharomyces cerevisiaeECI (ScECI2) is described. The best defined part of the bound acyl-CoA molecules is the 3′,5′-diphosphate-adenosine moiety, which interacts with residues of loop 1 and loop 2, whereas the pantetheine part is the least well defined. The catalytic base, Glu158, is hydrogen-bo…

Models MolecularSaccharomyces cerevisiae ProteinsDouble bondStereochemistryProtein ConformationIsomeraseSaccharomyces cerevisiaeEnoyl CoA isomeraseThioesterPhotochemistryDodecenoyl-CoA Isomerasebeta-oxidationSubstrate SpecificityStructural Biologyddc:570Catalytic DomainEnzyme StabilitySide chainMoietyta116chemistry.chemical_classificationHydrogen bondenoyl-CoA isomeraseta1182Hydrogen BondingGeneral Medicinehydrogen-bond networkcrotonaseoxyanion holechemistryAcyl Coenzyme AOxyanion holeOxidation-ReductionProtein BindingActa crystallographica. Section D, Biological crystallography
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