Search results for "ATP citrate lyase"

showing 9 items of 9 documents

Caloric Restriction Mimetics Enhance Anticancer Immunosurveillance

2016

International audience; Caloric restriction mimetics (CRMs) mimic the biochemical effects of nutrient deprivation by reducing lysine acetylation of cellular proteins, thus triggering autophagy. Treatment with the CRM hydroxycitrate, an inhibitor of ATP citrate lyase, induced the depletion of regulatory T cells (which dampen anticancer immunity) from autophagy-competent, but not autophagy-deficient, mutant KRAS-induced lung cancers in mice, thereby improving anticancer immunosurveillance and reducing tumor mass. Short-term fasting or treatment with several chemically unrelated autophagy-inducing CRMs, including hydroxycitrate and spermidine, improved the inhibition of tumor growth by chemoth…

0301 basic medicineCancer ResearchATP citrate lyaseSpermidineBariatric SurgeryimmunosurveillanceT-Lymphocytes RegulatoryAutophagy-Related Protein 5[ SDV.CAN ] Life Sciences [q-bio]/Cancerchemistry.chemical_compoundMiceregulatory T cellCitrates3. Good healthImmunogenic Cell-DeathImmunosurveillancemedicine.anatomical_structureOncologyBiochemistryDifferentiationembryonic structuresImmunogenic cell deathIn-VivoHumanRegulatory T cell[SDV.CAN]Life Sciences [q-bio]/Cancer[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyDietary RestrictionNOProto-Oncogene Proteins p21(ras)03 medical and health sciencesMonitoring ImmunologicIn vivoCell Line TumormedicineAutophagyAnimalsHumanscancerChemotherapyBreast-CancerCaloric Restrictioncancer; chemotherapy immunosurveillance regulatory T cellAnimal[ SDV.BC ] Life Sciences [q-bio]/Cellular Biologyregulatory T&nbspAutophagyfungiNeoplasms ExperimentalcellSpermidineMethotrexate030104 developmental biologychemistryAcetylationMutationCancer researchCitrateNeoplasm Transplantation
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Partial substitution of fish meal with vegetable protein sources in a diet for sea bass: effects on lipogenesis

2005

Three isoproteic (49.4%) and isolipidic (17.0%) diets were prepared: A control diet FM, in which protein was derived from fish meal and two experimental diets in which 70% of the fish meal protein was substituted with wheat gluten meal (WGM) or wheat gluten meal plus soybean meal (WGMsb), respectively. The essential limiting amino acids were added to satisfy the requirements of the species (Tibaldi et al., 1996). Three hundred and fifteen sea bass (initial weight = 23.9±0. 1g )were randomly divided into nine homogenous groups. The animals were reared in a closed recirculation system at 23.9 ◦ C and were fed ad libitum twice a day for 96 days. The fish were weighed at the beginning and the e…

ATP citrate lyaseDicentrarchus labrax; Dietary Proteins; body lipid composition; adipositySoybean mealfish meal lipid composition lipid deposition sea bass vegetable proteinsBiologyGlucosephosphate DehydrogenasePlant Proteins DietaryFish mealMalate DehydrogenaseSettore BIO/10 - BiochimicaFish ProductsAnimalsSettore AGR/18 - Nutrizione E Alimentazione AnimaleDicentrarchus labraxFood scienceSea basschemistry.chemical_classificationMealadiposityGeneral VeterinaryBody WeightFatty acidGeneral MedicineLipid MetabolismAnimal Feedbody lipid compositionchemistryLiverLipogenesisATP Citrate (pro-S)-LyaseBody CompositionComposition (visual arts)BassDietary Proteins
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Clinical evaluation of bempedoic acid for the treatment of hyperlipidaemia.

2021

Bempedoic acid (BA) is a novel first-in-class oral lipid-lowering therapy. BA has been approved by the European Medicinal Agency and Food and Drug Administration and has been commercialised throughout Europe since the end of 2020 as an add-on therapy in patients at high/very-high cardiovascular risk that are not at LDL-C goals with current lipid-lowering treatments. Recently, Italian lipid management experts gathered to discuss several open questions on BA characteristics and BArelated practical clinical issues. The panel permitted collection of its opinions in a ten Q&A format. Aim: The aim of this viewpoint is to discuss and answer several open questions on BA characteristics and BA-r…

ATP citrate lyaseEndocrinology Diabetes and MetabolismMedicine (miscellaneous)HyperlipidemiasPharmacologyLipid-lowering therapyLipid-lowering treatmentMedicineLDL-cholesterolHumansDicarboxylic AcidsHypolipidemic AgentsLdl cholesterolNutrition and DieteticsLipid managementbusiness.industryNovel LDL-C treatment.Fatty AcidsCholesterol LDLBempedoic acidNovel LDL-C treatmentATP citrate lyaseATP citrate lyase; bempedoic acid; LDL-cholesterol; lipid-lowering treatment; novel LDL-C treatmentLipid loweringCardiology and Cardiovascular MedicinebusinessClinical evaluationBempedoic acidNutrition, metabolism, and cardiovascular diseases : NMCD
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CitA/CitB Two-Component System Regulating Citrate Fermentation in Escherichia coli and Its Relation to the DcuS/DcuR System In Vivo

2011

ABSTRACT Citrate fermentation by Escherichia coli requires the function of the citrate/succinate antiporter CitT ( citT gene) and of citrate lyase ( citCDEFXG genes). Earlier experiments suggested that the two-component system CitA/CitB, consisting of the membrane-bound sensor kinase CitA and the response regulator CitB, stimulates the expression of the genes in the presence of citrate, similarly to CitA/CitB of Klebsiella pneumoniae . In this study, the expression of a chromosomal citC-lacZ gene fusion was shown to depend on CitA/CitB and citrate. CitA/CitB is related to the DcuS/DcuR two-component system which induces the expression of genes for fumarate respiration in response to C 4 -di…

ATP citrate lyaseOperonBiologymedicine.disease_causeMicrobiologyCitric AcidFusion geneGene clusterEscherichia colimedicinePromoter Regions GeneticMolecular BiologyEscherichia coliEscherichia coli ProteinsPromoterGene Expression Regulation BacterialArticlesMolecular biologyTwo-component regulatory systemDNA-Binding ProteinsResponse regulatorBiochemistryFermentationProtein KinasesProtein BindingTranscription FactorsJournal of Bacteriology
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Genetic organization of the citCDEF locus and identification of mae and clyR genes from Leuconostoc mesenteroides.

1999

ABSTRACT In this paper, we describe two open reading frames coding for a NAD-dependent malic enzyme ( mae ) and a putative regulatory protein ( clyR ) found in the upstream region of citCDEFG of Leuconostoc mesenteroides subsp. cremoris 195. The transcriptional analysis of the citrate lyase locus revealed one polycistronic mRNA covering the mae and citCDEF genes. This transcript was detected only on RNA prepared from cells grown in the presence of citrate. Primer extension experiments suggest that clyR and the citrate lyase operon are expressed from a bidirectional A-T-rich promoter region located between mae and clyR.

ATP citrate lyaseTranscription GeneticOperonMolecular Sequence DataMalatesLocus (genetics)Genetics and Molecular BiologyBiologyMicrobiologyPrimer extensionCitric AcidOpen Reading FramesBacterial ProteinsMalate DehydrogenaseMultienzyme ComplexesLeuconostocAmino Acid SequenceMolecular BiologyGeneGeneticsBase SequenceOxo-Acid-LyasesPromoterGene Expression Regulation BacterialSequence Analysis DNAbiology.organism_classificationMolecular biologyLeuconostoc mesenteroidesGenes BacterialSequence AlignmentLeuconostocJournal of bacteriology
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Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster

1998

ABSTRACT A citrate lyase (EC 4.1.3.6 ) was purified 25-fold from Leuconostoc mesenteroides and was shown to contain three subunits. The first 42 amino acids of the β subunit were identified, as well as an internal peptide sequence spanning some 20 amino acids into the α subunit. Using degenerated primers from these sequences, we amplified a 1.2-kb DNA fragment by PCR from Leuconostoc mesenteroides subsp. cremoris . This fragment was used as a probe for screening a Leuconostoc genomic bank to identify the structural genes. The 2.7-kb gene cluster encoding citrate lyase of L. mesenteroides is organized in three open reading frames, citD , citE , and citF , encoding, respectively, the three ci…

DNA BacterialATP citrate lyaseMolecular Sequence DataGene ExpressionBiologymedicine.disease_causeMicrobiologyBacterial ProteinsCarbon-Sulfur LigasesMultienzyme ComplexesGene clusterAcyl Carrier ProteinEscherichia colimedicineLeuconostocAmino Acid SequenceCloning MolecularMolecular BiologyEscherichia coliBase SequenceSequence Homology Amino AcidStructural geneOxo-Acid-LyasesSequence Analysis DNALyasebiology.organism_classificationEnzymes and ProteinsMolecular biologyOxaloacetate decarboxylaseBiochemistryGenes BacterialLeuconostoc mesenteroidesMultigene FamilyCoenzyme A-TransferasesLeuconostoc
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Mutation of the oxaloacetate decarboxylase gene of Lactococcus lactis subsp. lactis impairs the growth during citrate metabolism

2007

 ; Aims: Citrate metabolism generates metabolic energy through the generation of a membrane potential and a pH gradient. The purpose of this work was to study the influence of oxaloacetate decarboxylase in citrate metabolism and intracellular pH maintenance in relation to acidic conditions. Methods and Results: A Lactococcus lactis oxaloacetate decarboxylase mutant [ILCitM (pFL3)] was constructed by double homologous recombination. During culture with citrate, and whatever the initial pH, the growth rate of the mutant was lower. In addition, the production of diacetyl and acetoin was altered in the mutant strain. However, our results indicated no relationship with a change in the maintenanc…

Oxaloacetic AcidATP citrate lyaseCarboxy-LyasesCITRATE METABOLISMIntracellular pHMolecular Sequence DataDiacetylACIDE LACTIQUEApplied Microbiology and BiotechnologyCitric Acidchemistry.chemical_compoundLACTIC ACID BACTERIAOxaloacetic acidCitrate synthaseBacteriological TechniquesBase SequencebiologyOXALOACETATE DECARBOXYLASEAcetoinLactococcus lactisGeneral MedicineHydrogen-Ion Concentrationbiology.organism_classificationLactococcus lactis[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyOxaloacetate decarboxylaseBiochemistrychemistryGenes BacterialFermentationMutationINTRACELLULAR PHFood Microbiologybiology.proteinGenetic EngineeringCitric acidPhosphoenolpyruvate carboxykinaseBiotechnologyJournal of Applied Microbiology
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Citrate permease gene expression inLactococcus lactissubsp.lactisstrains IL1403 and MG1363

1996

Citrate permease gene expression in the plasmid-free Lactococcus lactis strains IL1403 and MG1363 was studied. The ability to transport citrate results in diacetyl and acetoin production in IL1403 but not in MG1363. Citrate lyase, α-acetolactate decarboxylase, diacetyl and acetoin reductase were detected in IL1403. These data show that L. lactis ssp. lactis strain IL1403 is a citrate permease mutant of the biovar. diacetylactis. Immunological analysis revealed the α-and β-subunits of citrate lyase not only in IL1403 but also in MG1363 where no citrate lyase activity was found.

biologyATP citrate lyasePermeaseAcetoinBiovarLactococcus lactisMutantfood and beveragesbiology.organism_classificationLyaseMicrobiologyDiacetylMicrobiologychemistry.chemical_compoundchemistryBiochemistryGeneticsMolecular BiologyFEMS Microbiology Letters
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Citrate lyases of lactic acid bacteria

1998

Citrate Iyase is a key enzyme of the citrate metabolism which is involved in flavor and texture of many fermented milk products. Citrate Iyase which catalyses the cleavage of citrate into oxaloacetate and acetate is a multienzyme complex composed of three proteins: an acyl carrier protein (ACP); a citrate, acetate-ACP transferase; and a citryl-S-ACP Iyase. The citrate Iyase is active only when the thioester residue of the prosthetic group bound to ACP is acetylated. In the presence of citrate, the transferase mediates the formation of citryl-S-acyl carrier protein by acyl exchange and liberation of acetate. Then the Iyase subunit cleaves the citryl-S-ACP with libe- ration of oxaloacetate an…

biologyATP citrate lyasefood and beverages[SDV.IDA] Life Sciences [q-bio]/Food engineeringbiology.organism_classificationCofactorLactic acidchemistry.chemical_compoundAcyl carrier protein[SDV.AEN] Life Sciences [q-bio]/Food and NutritionBiochemistrychemistryLeuconostoc mesenteroidesbiology.proteinTransferaseLeuconostocCitrate synthaselipids (amino acids peptides and proteins)ComputingMilieux_MISCELLANEOUSFood Science
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