Search results for "Pyruvate Dehydrogenase Complex"

showing 10 items of 12 documents

2017

Previous studies reported that the use of Metschnikowia pulcherrima in sequential culture fermentation with Saccharomyces cerevisiae mainly induced a reduction of volatile acidity in wine. The impact of the presence of this yeast on the metabolic pathway involved in pyruvate dehydrogenase (PDH) bypass and glycerol production in S. cerevisiae has never been investigated. In this work, we compared acetic acid and glycerol production kinetics between pure S. cerevisiae culture and its sequential culture with M. pulcherrima during alcoholic fermentation. In parallel, the expression levels of the principal genes involved in PDH bypass and glyceropyruvic fermentation in S. cerevisiae were investi…

0301 basic medicineMicrobiology (medical)Fermentation in winemaking030106 microbiologyfood and beveragesBiologyEthanol fermentationbiology.organism_classificationPyruvate dehydrogenase complexMicrobiologyYeast03 medical and health sciencesBiochemistrybiology.proteinFermentationPyruvate decarboxylaseMetschnikowia pulcherrimaAlcohol dehydrogenaseFrontiers in Microbiology
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2019

Mitochondria have been increasingly recognized as a central regulatory nexus for multiple metabolic pathways, in addition to ATP production via oxidative phosphorylation (OXPHOS). Here we show that inducing mitochondrial DNA (mtDNA) stress in Drosophila using a mitochondrially-targeted Type I restriction endonuclease (mtEcoBI) results in unexpected metabolic reprogramming in adult flies, distinct from effects on OXPHOS. Carbohydrate utilization was repressed, with catabolism shifted towards lipid oxidation, accompanied by elevated serine synthesis. Cleavage and translocation, the two modes of mtEcoBI action, repressed carbohydrate rmetabolism via two different mechanisms. DNA cleavage activ…

0303 health sciencesCancer ResearchCatabolismMetabolismOxidative phosphorylationBiologyMitochondrionPyruvate dehydrogenase complexCell biology03 medical and health sciencesMetabolic pathway0302 clinical medicineLipid oxidationGeneticsSignal transductionMolecular Biology030217 neurology & neurosurgeryGenetics (clinical)Ecology Evolution Behavior and Systematics030304 developmental biologyPLOS Genetics
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Autoreactive liver-infiltrating T cells in primary biliary cirrhosis recognize inner mitochondrial epitopes and the pyruvate dehydrogenase complex.

1993

Primary biliary cirrhosis (PBC) is characterized by lymphoid infiltrates in the portal tracts of the liver and the occurrence of antimitochondrial autoantibodies in serum directed against components of the pyruvate dehydrogenase complex and the other alpha-keto acid dehydrogenase complexes. These enzymes are located on the inner mitochondrial membrane. The destruction of the biliary tract in PBC is thought to be mediated by autoreactive liver-infiltrating T cells exerting cytotoxic activity or releasing certain lymphokines. In this study the reactivity of liver infiltrating T cells was shown to a bovine pyruvate dehydrogenase complex (PDH), a purified E2 subunit (PDH-E2) and a crude prepara…

AdultMaleAdolescentBiliary cirrhosisT-LymphocytesEnzyme-Linked Immunosorbent AssayMitochondria LiverPyruvate Dehydrogenase ComplexAutoimmune hepatitisEpitopesPrimary biliary cirrhosisCell MovementmedicineCytotoxic T cellHumansCells CulturedAgedAutoantibodiesHepatologybiologyLiver Cirrhosis BiliaryAntibodies MonoclonalMiddle Agedmedicine.diseasePyruvate dehydrogenase complexPhenotypeLiverImmunologybiology.proteinFemaleAntibodyViral hepatitisCD8Journal of hepatology
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Immunoblotting as a confirmatory test for antimitochondrial antibodies in primary biliary cirrhosis.

1993

Primary biliary cirrhosis is characterised by the presence of antimitochondrial antibodies which are directed against components of mitochondrial dehydrogenase complexes. The specificity of antimitochondrial antibodies for primary biliary cirrhosis as detected by immunoblotting was investigated. Commercially available preparations of pyruvate and oxo-glutarate dehydrogenases and beef-heart mitochondria were used as source of antigens. Sera from 47 primary biliary cirrhosis patients (46 of whom were antimitochondrial antibody positive by immunofluorescence), 16 non-primary biliary cirrhosis patients (antimitochondrial antibody positive by immunofluorescence), 23 liver-kidney microsomal antib…

Adultmedicine.medical_specialtyPathologyBiliary cirrhosisImmunoblottingFluorescent Antibody TechniquePyruvate Dehydrogenase ComplexBiologyImmunofluorescenceGastroenterologyMitochondria HeartPrimary biliary cirrhosisAntigenAntibody SpecificityInternal medicinemedicineAnimalsHumansKetoglutarate Dehydrogenase ComplexAutoantibodiesHepatitismedicine.diagnostic_testLiver Cirrhosis BiliaryGastroenterologyAutoantibodyMiddle AgedPyruvate dehydrogenase complexmedicine.diseaseMitochondriabiology.proteinCattleFemaleAntibodyResearch ArticleGut
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Pyruvate dehydrogenase specific T cells in primary biliary cirrhosis show restricted antigen recognition sites

2002

:  Background/Aims: The aim was to characterise the antigen recognition sites of the variable T cell receptor α-chain (TCRAV) and β-chain (TCRBV) of T cells specific to the pyruvate dehydrogenase (PDC) in primary biliary cirrhosis. Methods: In 21 PDC-specific T cell clones isolated from five patients we analysed TCRAV and TCRBV usage by RT-PCR and sequenced the CDR3 regions. Results: Preferential expression of the TCR elements BV6 (6 clones), BV12 (4 clones) and BV1 (3 clones), and frequent usage of the joining elements JB2.3 and JB2.1 were seen. Analysis of the α chain revealed rearrangement of AV2 in 7 clones (35%) and AV7 in 3 clones, however, distribution of the joining elements was het…

HepatologyCell divisionT cellT-cell receptorhemic and immune systemsBiologymedicine.diseasePyruvate dehydrogenase complexMolecular biologyEpitopePrimary biliary cirrhosismedicine.anatomical_structureAntigenBiochemistrymedicineSequence motifLiver
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Kinetics of lactate fermentation and citrate bioconversion by LactococcusIactisssp.Iactisin batch culture

1993

The growth kinetics of Lactococcus lactis ssp. lactis were studied in batch culture in conditions of non-limiting lactose and the presence of citric acid. The control of pH modified growth and citrate metabolism but did not change the yield of acid formation. At controlled pH the growth rate was unaffected by citrate metabolism. Lactose was transformed to L-lactate and assay of the metabolic by-products showed some heterofermentation at the end of the growth of cultures with low growth rates. This heterofermentation was interpreted as a slowing down of glycolysis with activation of both the pyruvate formate lyase (PFL) and the pyruvate dehydrogenase complex (PDHC). Under these conditions th…

LactococcusLactococcus lactisBiologyPyruvate dehydrogenase complexbiology.organism_classificationApplied Microbiology and BiotechnologyMicrobiologyLactic acidchemistry.chemical_compoundchemistryBiochemistryGlycolysisFermentationCitric acidLactic acid fermentationJournal of Applied Bacteriology
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Leigh syndrome due to compound heterozygosity of dihydrolipoamide dehydrogenase gene mutations. Description of the first E3 splice site mutation.

2003

Item does not contain fulltext A boy with recurrent episodes of hypoglycaemia and ataxia, microcephaly, mental retardation, permanent lactic acidaemia, intermittent 2-oxoglutaric aciduria as well as elevation of serum branched chain amino acids was diagnosed with dihydrolipoamide dehydrogenase (E3) deficiency. Analysis of genomic DNA revealed compound heterozygosity for two novel mutations: I393T in exon 11, located at the interface domain of the protein and possibly interfering with its dimerisation, and IVS9+1G>A located at a consensus splice site. A heterozygous polymorphism was also detected. In the patient's cDNA the I393T mutation and the polymorphism appeared to be homozygous, indica…

MaleHeterozygoteMutation MissensePyruvate Dehydrogenase ComplexGene mutationBiologyCompound heterozygosityLoss of heterozygositymedicineHumansLeigh diseaseMuscle SkeletalDihydrolipoamide DehydrogenaseGeneticsSplice site mutationDihydrolipoamide dehydrogenasePyruvate Dehydrogenase (Lipoamide)Fibroblastsmedicine.diseasePyruvate dehydrogenase complexRenal disorders [UMCN 5.4]Genetic defects of metabolism [UMCN 5.1]Child PreschoolPediatrics Perinatology and Child HealthRNA Splice SitesLeigh DiseaseCellular energy metabolism [UMCN 5.3]
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Abnormalities of mitochondrial functioning can partly explain the metabolic disorders encountered in sarcopenic gastrocnemius.

2007

International audience; Aging triggers several abnormalities in muscle glycolytic fibers including increased proteolysis, reactive oxygen species (ROS) production and apoptosis. Since the mitochondria are the main site of substrate oxidation, ROS production and programmed cell death, we tried to know whether the cellular disorders encountered in sarcopenia are due to abnormal mitochondrial functioning. Gastrocnemius mitochondria were extracted from adult (6 months) and aged (21 months) male Wistar rats. Respiration parameters, opening of the permeability transition pore and ROS production, with either glutamate (amino acid metabolism) or pyruvate (glucose metabolism) as a respiration substr…

Malemuscle atrophyMESH : Cell Aging[SDV]Life Sciences [q-bio]MESH : Reactive Oxygen SpeciesMitochondrion0302 clinical medicineGlycolysisMESH: AnimalsMESH : Muscle SkeletalMESH : Fatty AcidsCellular SenescencePhospholipidsMESH: Superoxide Dismutasereactive oxygen speciesMESH : Free Radicals0303 health sciencesMESH: Muscle SkeletalMESH : RatsFatty Acidsfatty acid profile of mitochondrial lipidsMESH: Reactive Oxygen SpeciesPyruvate dehydrogenase complexMESH: Fatty Acidsmitochondria[SDV] Life Sciences [q-bio]BiochemistryMESH: Cell AgingMESH: CalciumMESH : MitochondriaCell agingPyruvate decarboxylationmedicine.medical_specialtyFree RadicalsMESH: RatsCellular respirationMESH: MitochondriaMESH : MaleCell Respirationchemistry.chemical_elementOxidative phosphorylationBiologyCalciumMESH : Rats WistarMESH : Phospholipids03 medical and health sciencesMESH: Free RadicalsInternal medicinemedicineAnimalsMESH : Superoxide DismutaseRats WistarMuscle SkeletalMESH : Calcium030304 developmental biologyMESH: Phospholipidscalciumpermeability transition poreSuperoxide Dismutaseagingaging;calcium;fatty acid profile of mitochondrial lipids;mitochondria;muscle atrophy;permeability transition pore;reactive oxygen species;Animals;Calcium;Cell Aging;Cell Respiration;Fatty Acids;Free Radicals;Male;Mitochondria;Muscle;Skeletal;Phospholipids;Rats;Wistar;Reactive Oxygen Species;Superoxide DismutaseCell BiologyMESH: Rats WistarMESH: MaleRatsEndocrinologychemistryMESH : Cell RespirationMESH : AnimalsMESH: Cell Respiration030217 neurology & neurosurgery
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Pyruvate kinase type M2: a crossroad in the tumor metabolome.

2002

Cell proliferation is a process that consumes large amounts of energy. A reduction in the nutrient supply can lead to cell death by ATP depletion, if cell proliferation is not limited. A key sensor for this regulation is the glycolytic enzyme pyruvate kinase, which determines whether glucose carbons are channelled to synthetic processes or used for glycolytic energy production. In unicellular organisms pyruvate kinase is regulated by ATP, ADP and AMP, by ribose 5-P, the precursor of the nucleic acid synthesis, and by the glycolytic intermediate fructose 1,6-P2 (FBP), thereby adapting cell proliferation to nutrient supply. The mammalian pyruvate kinase isoenzyme type M2 (M2-PK) displays the …

Pyruvate decarboxylationNutrition and DieteticsPyruvate dehydrogenase kinaseFatty AcidsPyruvate KinaseMedicine (miscellaneous)Glutamic AcidPyruvate dehydrogenase phosphataseBiologyPKM2Pyruvate dehydrogenase complexPyruvate carboxylaseNeoplasm ProteinsBiochemistryNeoplasmsAnimalsHumansGlycolysisPyruvate kinaseCell DivisionHydrogenThe British journal of nutrition
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Pyruvate fermentation by Oenococcus oeni and Leuconostoc mesenteroides and role of pyruvate dehydrogenase in anaerobic fermentation.

2005

ABSTRACT The heterofermentative lactic acid bacteria Oenococcus oeni and Leuconostoc mesenteroides are able to grow by fermentation of pyruvate as the carbon source (2 pyruvate → 1 lactate + 1 acetate + 1 CO 2 ). The growth yields amount to 4.0 and 5.3 g (dry weight)/mol of pyruvate, respectively, suggesting formation of 0.5 mol ATP/mol pyruvate. Pyruvate is oxidatively decarboxylated by pyruvate dehydrogenase to acetyl coenzyme A, which is then converted to acetate, yielding 1 mol of ATP. For NADH reoxidation, one further pyruvate molecule is reduced to lactate. The enzymes of the pathway were present after growth on pyruvate, and genome analysis showed the presence of the corresponding st…

Pyruvate decarboxylationPyruvate dehydrogenase kinaseEcologyPyruvate Dehydrogenase ComplexPyruvate dehydrogenase phosphataseBiologyPyruvate dehydrogenase complexPhysiology and BiotechnologyApplied Microbiology and BiotechnologyPyruvate carboxylaseCulture MediaGram-Positive CocciBiochemistryPyruvate oxidase activityFermentationPyruvic AcidFermentationAnaerobiosisDihydrolipoyl transacetylaseLeuconostocFood ScienceBiotechnologyApplied and environmental microbiology
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