Search results for "succinate"

showing 10 items of 105 documents

C4-dicarboxylate carriers and sensors in bacteria

2002

AbstractBacteria contain secondary carriers for the uptake, exchange or efflux of C4-dicarboxylates. In aerobic bacteria, dicarboxylate transport (Dct)A carriers catalyze uptake of C4-dicarboxylates in a H+- or Na+-C4-dicarboxylate symport. Carriers of the dicarboxylate uptake (Dcu)AB family are used for electroneutral fumarate:succinate antiport which is required in anaerobic fumarate respiration. The DcuC carriers apparently function in succinate efflux during fermentation. The tripartite ATP-independent periplasmic (TRAP) transporter carriers are secondary uptake carriers requiring a periplasmic solute binding protein. For heterologous exchange of C4-dicarboxylates with other carboxylic …

Aerobic bacteriaAntiporterSuccinic AcidBiophysicsOrganic Anion TransportersReceptors Cell Surfacemedicine.disease_causeBiochemistryFumarate (succinate) sensorTwo-component systemBacterial ProteinsFumaratesEscherichia colimedicineAmino Acid SequenceEscherichia coliDicarboxylate uptake SHistidine protein kinasePhylogenyHistidineDicarboxylic Acid TransportersDicarboxylate transport BbiologyEscherichia coli ProteinsBiological TransportPeriplasmic spaceCell Biologybiology.organism_classificationTwo-component regulatory systemBacteria AerobicModels ChemicalBiochemistryAntiportFumarate/succinate transportEffluxDicarboxylate uptake carrierProtein KinasesDicarboxylate transport A carrierBacteriaSignal TransductionBiochimica et Biophysica Acta (BBA) - Bioenergetics
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Transport of C(4)-dicarboxylates in Wolinella succinogenes.

2000

ABSTRACT C 4 -dicarboxylate transport is a prerequisite for anaerobic respiration with fumarate in Wolinella succinogenes , since the substrate site of fumarate reductase is oriented towards the cytoplasmic side of the membrane. W. succinogenes was found to transport C 4 -dicarboxylates (fumarate, succinate, malate, and aspartate) across the cytoplasmic membrane by antiport and uniport mechanisms. The electrogenic uniport resulted in dicarboxylate accumulation driven by anaerobic respiration. The molar ratio of internal to external dicarboxylate concentration was up to 10 3 . The dicarboxylate antiport was either electrogenic or electroneutral. The electroneutral antiport required the prese…

Anaerobic respirationAntiporterPhysiology and MetabolismMutantMalatesBiologymedicine.disease_causeMicrobiologyCell membraneElectron TransportOxygen ConsumptionBacterial ProteinsFumaratesRespirationmedicineDicarboxylic AcidsAnaerobiosisMolecular BiologyEscherichia coliDicarboxylic Acid TransportersAspartic AcidNitratesEscherichia coli ProteinsCell MembraneSodiumMembrane ProteinsBiological TransportSuccinatesFumarate reductaseElectron transport chainWolinellamedicine.anatomical_structureBiochemistryMutagenesisCarrier ProteinsGene DeletionJournal of bacteriology
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Folate-mediated targeting of polymeric conjugates of gemcitabine.

2005

The synthesis of two new macromolecular prodrugs for active tumor targeting was set up. Gemcitabine (2'-deoxy-2',2'-difluorocytidine) was conjugated to alpha,beta-poly(N-2-hydroxyethyl)-DL-aspartamide (PHEA) through succinyl or diglycolyl hydrolysable spacers. The targeting agent folic acid was attached to the macromolecular backbone through the aminocaproic spacer. The two conjugates [PHEA-(5'-succinylgemcitabine)-1'-carboxypentyl-folamide and PHEA-(5'-diglycolyl-gemcitabine)-1'-carboxypentyl-folamide], were purified and extensively characterised by spectroscopic (UV, IR and NMR) and chromatographic analyses to determine the correct chemical structure, the purity degree and the reaction yi…

Antimetabolites AntineoplasticTime FactorsStereochemistryCell SurvivalpolyaspartamideChemical structurePharmaceutical ScienceReceptors Cell SurfaceConjugated systemDeoxycytidineDrug Delivery SystemsFolic AcidCell Line Tumorfolate-mediated targetingExtracellularHumansProdrugsIncubationPolyhydroxyethyl MethacrylateDrug CarriersDose-Response Relationship DrugChemistrypolymeric conjugateFolate Receptors GPI-AnchoredSuccinatesHydrogen-Ion ConcentrationGemcitabineIn vitroBiochemistryCell cultureCarrier ProteinsMacromoleculeConjugateInternational journal of pharmaceutics
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The Fumarate/Succinate Antiporter DcuB of Escherichia coli Is a Bifunctional Protein with Sites for Regulation of DcuS-dependent Gene Expression

2008

DcuB of Escherichia coli catalyzes C4-dicarboxylate/succinate antiport during growth by fumarate respiration. The expression of genes of fumarate respiration, including the genes for DcuB (dcuB) and fumarate reductase (frdABCD) is transcriptionally activated by C4-dicarboxylates via the DcuS-DcuR two-component system, comprising the sensor kinase DcuS, which contains a periplasmic sensing domain for C4-dicarboxylates. Deletion or inactivation of dcuB caused constitutive expression of DcuS-regulated genes in the absence of C4-dicarboxylates. The effect was specific for DcuB and not observed after inactivation of the homologous DcuA or the more distantly related DcuC transporter. Random and s…

AntiporterMutantlac operonBiologymedicine.disease_causePeptide MappingBiochemistryAntiportersFumaratesEscherichia colimedicineMolecular BiologyEscherichia coliDerepressionDicarboxylic Acid TransportersIon TransportEscherichia coli ProteinsMutagenesisSuccinatesGene Expression Regulation BacterialCell BiologyPeriplasmic spaceFumarate reductaseDNA-Binding ProteinsSuccinate DehydrogenaseAmino Acid SubstitutionBiochemistryGene Knockdown TechniquesMutagenesis Site-DirectedProtein KinasesTranscription FactorsJournal of Biological Chemistry
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Causative role of oxidative stress in a Drosophila model of Friedreich ataxia

2006

Friedreich ataxia (FA), the most common form of hereditary ataxia, is caused by a deficit in the mitochondrial protein frataxin. While several hypotheses have been suggested, frataxin function is not well understood. Oxidative stress has been suggested to play a role in the pathophysiology of FA, but this view has been recently questioned, and its link to frataxin is unclear. Here, we report the use of RNA interference (RNAi) to suppress the Drosophila frataxin gene (fh) expression. This model system parallels the situation in FA patients, namely a moderate systemic reduction of frataxin levels compatible with normal embryonic development. Under these conditions, fh-RNAi flies showed a shor…

AtaxiaBlotting WesternLongevityGene ExpressionCHO Cellsmedicine.disease_causeBiochemistryAconitaseMitochondrial ProteinsCricetulusRNA interferenceCricetinaeIron-Binding ProteinsGeneticsmedicineAnimalsDrosophila ProteinsRNA MessengerMolecular BiologyGeneAconitate HydrataseHyperoxiaGeneticsElectron Transport Complex IbiologyReverse Transcriptase Polymerase Chain ReactionSuccinate dehydrogenasefungiImmunohistochemistryCell biologySuccinate DehydrogenaseOxidative StressDrosophila melanogasterFriedreich AtaxiaFrataxinbiology.proteinRNA Interferencemedicine.symptomOxidative stressBiotechnologyThe FASEB Journal
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Improved Bone Regeneration Using Biodegradable Polybutylene Succinate Artificial Scaffold in a Rabbit Model

2022

The treatment of extensive bone loss represents a great challenge for orthopaedic and reconstructive surgery. Most of the time, those treatments consist of multiple-stage surgeries over a prolonged period, pose significant infectious risks and carry the possibility of rejection. In this study, we investigated if the use of a polybutylene succinate (PBS) micro-fibrillar scaffold may improve bone regeneration in these procedures. In an in vivo rabbit model, the healing of two calvarial bone defects was studied. One defect was left to heal spontaneously while the other was treated with a PBS scaffold. Computed tomography (CT) scans, histological and immunohistochemical analyses were performed …

Biomaterialsbone defectbone regenerationpolybutylene succinatemicrofibrillar scaffoldBiomedical Engineeringrabbitbone reconstructionpolybutylene succinate; microfibrillar scaffold; rabbit; bone reconstruction; bone regeneration; bone defect
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Cannabinoid control of brain bioenergetics: Exploring the subcellular localization of the CB1 receptor

2014

Brain mitochondrial activity is centrally involved in the central control of energy balance. When studying mitochondrial functions in the brain, however, discrepant results might be obtained, depending on the experimental approaches. For instance, immunostaining experiments and biochemical isolation of organelles expose investigators to risks of false positive and/or false negative results. As an example, the functional presence of cannabinoid type 1 (CB1) receptors on brain mitochondrial membranes (mtCB1) was recently reported and rapidly challenged, claiming that the original observation was likely due to artifact results. Here, we addressed this issue by directly comparing the procedures…

CB1 receptorWIN WIN55212-2Cannabinoid receptorBrain bioenergeticsLactate dehydrogenase Amedicine.medical_treatmentSDHADMSO dimethyl sulfoxideMitochondrionBiologySlp2 stomatin-like protein 2SDHA succinate dehydrogenase aTechnical ReportmedicineantibodieseducationReceptorKO knock-outMolecular Biologyeducation.field_of_studyelectron microscopyLDHa lactate dehydrogenase aDAB–Ni Ni-intensified 33ʹ-diaminobenzidine–4HClCell BiologySubcellular localizationWT wild-typemitochondriaBiochemistryCB1 cannabinoid type 1 receptorBSA bovine serum albuminCannabinoidorganelle purificationNeuroscienceImmunostainingMolecular Metabolism
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Menaquinone-dependent succinate dehydrogenase of bacteria catalyzes reversed electron transport driven by the proton potential.

1998

Succinate dehydrogenases from bacteria and archaea using menaquinone (MK) as an electron acceptor (succinate/menaquinone oxidoreductases) contain, or are predicted to contain, two heme-B groups in the membrane-anchoring protein(s), located close to opposite sides of the membrane. All succinate/ubiquinone oxidoreductases, however, contain only one heme-B molecule. In Bacillus subtilis and other bacteria that use MK as the respiratory quinone, the succinate oxidase activity (succinate-->O2), and the succinate/menaquinone oxidoreductase activity were specifically inhibited by uncoupler (CCCP, carbonyl cyanide m-chlorophenylhydrazone) or by agents dissipating the membrane potential (valinomycin…

Carbonyl Cyanide m-Chlorophenyl HydrazoneVitamin KHemeBiochemistryCatalysisMembrane PotentialsElectron TransportValinomycinchemistry.chemical_compoundOxidoreductaseElectrochemistryEnzyme Inhibitorschemistry.chemical_classificationMembrane potentialBinding SitesbiologyBacteriaChemistryElectron Transport Complex IISuccinate dehydrogenaseElectron acceptorbiology.organism_classificationElectron transport chainSuccinate DehydrogenaseBiochemistrybiology.proteinProtonsBacteriaEuropean journal of biochemistry
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New artesunic acid homodimers: Potent reversal agents of multidrug resistance in leukemia cells

2012

Abstract To evade the problem of multidrug resistance, hybridization of natural products in dimers is considered as an effective method. After the successful synthesis of three artesunic acid homodimers connected by different types of chemical linkers, we analyzed their activity against human CCRF-CEM and multidrug-resistant p -glycoprotein-overexpressing CEM/ADR 5000 leukemia cells and observed, that multidrug resistant cells were not cross-resistant to the new compounds. Collateral sensitivity was observed for artesunic acid homodimer 2. The obtained results deliver valuable information about the linker’s structure which is required for homodimers to be highly cytotoxic.

Cell SurvivalClinical BiochemistryPharmaceutical ScienceAntineoplastic AgentsBiochemistryStructure-Activity RelationshipDrug DiscoveryTumor Cells CulturedmedicineHumansCytotoxic T cellMolecular BiologyArtesunic acidLeukemiaDose-Response Relationship DrugMolecular StructureChemistryOrganic ChemistrySuccinatesmedicine.diseaseArtemisininsDrug Resistance MultipleMultiple drug resistanceLeukemiaBiochemistryDrug Resistance NeoplasmApoptosisMolecular MedicineDrug Screening Assays AntitumorDimerizationLinkerBioorganic & Medicinal Chemistry
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Dimethylsulfoxide as carrier in enzyme cytochemistry.

1971

Addition of dimethylsulfoxide (DMSO) to the incubation medium of succinate dehydrogenase in a concentration of 10% enhances the staining reaction in the hyphae of the fungus Cercosporella herpotrichoides after an incubation period of 15 min. Controls without DMSO remain unstained. DMSO causes a rapid penetration of the components of the medium through the mucilage that covers the hyphae.

CercosporellaHistologyintegumentary systembiologyHyphaStaining and LabelingHistocytochemistryorganic chemicalsSuccinate dehydrogenasefungiCell BiologyStainingIncubation periodMedical Laboratory TechnologyBiochemistryMucilagebiology.proteinCytochemistryDimethyl SulfoxideMitosporic FungiMolecular BiologyIncubationHistochemie. Histochemistry. Histochimie
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