Search results for "transporters"

showing 10 items of 203 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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Anxiolytic-like effects of acute and chronic GABA transporter inhibition in rats.

2002

Acute GABA transporter inhibition can induce anxiolytic-like behaviors. The present analysis addressed whether chronic treatment (23 days via drinking water) with a GABA transporter inhibitor affects rat behavior similar to acute treatment and interferes with additional benzodiazepine-receptor agonistic treatment. Seventy-one rats divided into seven groups were acutely treated with either vehicle, diazepam (2 mg/kg), zolpidem (0.05 mg/kg), tiagabine (19 mg/kg) or chronically with tiagabine with or without acute diazepam or zolpidem. Animals were behaviorally characterized in an elevated plus-maze. None of the treatments induced changes in the activity of the animals. Acute and chronic treat…

AgonistMalemedicine.medical_specialtyElevated plus mazeZolpidemGABA Plasma Membrane Transport ProteinsTime FactorsTiagabinemedicine.drug_classPyridinesNipecotic AcidsOrganic Anion TransportersPharmacologyAnxiolyticDrug Administration Schedulechemistry.chemical_compoundInternal medicinemedicineGABA transporterAnimalsNeurotransmitterMaze LearningTiagabineBiological PsychiatryDiazepambiologyBehavior Animalbusiness.industryMembrane ProteinsMembrane Transport ProteinsDrug SynergismRats Inbred StrainsRatsZolpidemPsychiatry and Mental healthEndocrinologyNeurologychemistryAnti-Anxiety Agentsbiology.proteinNeurology (clinical)businessCarrier ProteinsDiazepammedicine.drugJournal of neural transmission (Vienna, Austria : 1996)
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LXR antagonists induce ABCD2 expression

2014

X-linked adrenoleukodystrophy (X-ALD) is a rare neurodegenerative disorder characterized by the accumulation of very-long-chain fatty acids resulting from a beta-oxidation defect. Oxidative stress and inflammation are also key components of the pathogenesis. X-ALD is caused by mutations in the ABCDI gene, which encodes for a peroxisomal half ABC transporter predicted to participate in the entry of VLCFA-CoA into the peroxisome, the unique site of their beta-oxidation. Two homologous peroxisomal ABC transporters, ABCD2 and ABCD3 have been proven to compensate for ABCD1 deficiency when overexpressed. Pharmacological induction of these target genes could therefore represent an alternative ther…

Agonistx-ald;very-long-chain fatty acid;lxr;hydroxycholesterol;abcd2medicine.medical_specialtymedicine.drug_classx-aldEndogenyContext (language use)ATP-binding cassette transporterBiologyATP Binding Cassette Transporter Subfamily DInternal medicinemedicineHumanslxr[ SDV.BDD ] Life Sciences [q-bio]/Development BiologyhydroxycholesterolLiver X receptorAdrenoleukodystrophyMolecular Biology[SDV.BDD]Life Sciences [q-bio]/Development BiologyLiver X ReceptorsFatty AcidsBiologie du développementNeurosciencesCell BiologyHep G2 CellsPeroxisomemedicine.diseaseOrphan Nuclear ReceptorsDevelopment BiologyHydroxycholesterolsvery-long-chain fatty acidOxidative StressEndocrinologyGene Expression RegulationCell cultureabcd2Neurons and Cognition[ SDV.NEU ] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]Cancer researchlipids (amino acids peptides and proteins)AdrenoleukodystrophyATP-Binding Cassette Transporters[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]
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Activation of classical protein kinase C decreases transport via systems y+and y+L

2007

Activation of protein kinase C (PKC) downregulates the human cationic amino acid transporters hCAT-1 (SLC7A1) and hCAT-3 (SLC7A3) (Rotmann A, Strand D, Martiné U, Closs EI. J Biol Chem 279: 54185–54192, 2004; Rotmann A, Vekony N, Gassner D, Niegisch G, Strand D, Martine U, Closs EI. Biochem J 395: 117–123, 2006). However, others found that PKC increased arginine transport in various mammalian cell types, suggesting that the expression of different arginine transporters might be responsible for the opposite PKC effects. We thus investigated the consequence of PKC activation by phorbol-12-myristate-13-acetate (PMA) in various human cell lines expressing leucine-insensitive system y+[hCAT-1, h…

Amino Acid Transport System y+ArgininePhysiologyBiological Transport ActiveBiologyArginineEnzyme activatorLeucineCell Line TumorHumansRNA MessengerCationic Amino Acid TransportersProtein Kinase CProtein kinase CRegulation of gene expressionchemistry.chemical_classificationBase SequenceAmino Acid Transport System y+LCell BiologyMolecular biologyEnzyme ActivationEnzymeGene Expression RegulationchemistryTetradecanoylphorbol AcetateTetradecanoylphorbol AcetateLeucineAmerican Journal of Physiology-Cell Physiology
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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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Sterically geared tris-thioureas; transmembrane chloride transporters with unusual activity and accessibility

2015

Tris-N-arylthioureas derived in one step from 1,3,5-tris(aminomethyl)-2,4,6-triethylbenzene are remarkably effective anion carriers. With optimised aryl substituents their activities come close to the best currently known, suggesting that they might find use as readily available standards in anion transport research.

AnionsModels MolecularTrisSteric effectsCrystallography X-RayChlorideCatalysisPhysico-chimie généralechemistry.chemical_compoundChloridesMaterials ChemistrymedicineChimieMoleculeOrganic chemistryta116Ion transporterIon TransportMolecular StructureChemistryArylThioureatransmembrane anion carriersMetals and Alloystransmembrane transportersGeneral ChemistryCombinatorial chemistryTransmembrane proteinSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsChimie organiqueThioureaCeramics and Compositesmedicine.drugChemical Communications
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TAP off - tumors on

1997

Abstract The molecular characterization of T-cell-defined tumor-associated antigens has provided targets for cell-mediated immunotherapy for malignant diseases. The success of this strategy is negatively influenced by structural and functional abnormalities of major histocompatibility complex (MHC) class I molecules, which provide tumor cells with resistance to T-cell-mediated immune recognition. This article reviews the physiology of the MHC class I processing machinery and describes the deficiencies of this pathway in malignant cells.

Antigen processingImmunologyAntigen presentationCD1Human leukocyte antigenBiologyMHC restrictionMajor histocompatibility complexMajor Histocompatibility ComplexAntigenATP Binding Cassette Transporter Subfamily B Member 3NeoplasmsMHC class IImmunologyTumor Cells Culturedbiology.proteinHumansATP-Binding Cassette TransportersATP Binding Cassette Transporter Subfamily B Member 2Immunology Today
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DctA- and Dcu-independent transport of succinate in Escherichia coli : contribution of diffusion and of alternative carriers

2001

Quintuple mutants of Escherichia coli deficient in the C4-dicarboxylate carriers of aerobic and anaerobic metabolism (DctA, DcuA, DcuB, DcuC, and the DcuC homolog DcuD, or the citrate/succinate antiporter CitT) showed only poor growth on succinate (or other C4-dicarboxylates) under oxic conditions. At acidic pH (pH 6) the mutants regained aerobic growth on succinate, but not on fumarate. Succinate uptake by the mutants could not be saturated at physiological succinate concentrations (≤5 mM), in contrast to the wild-type, which had a K m for succinate of 50 µM and a V max of 35 U/g dry weight at pH 6. At high substrate concentrations, the mutants showed transport activities (32 U/g dry weigh…

AntiporterMutantSuccinic AcidBiologymedicine.disease_causeBiochemistryMicrobiologyBacterial ProteinsFumaratesNitrilesEscherichia coliGeneticsmedicineMolecular BiologyEscherichia coliDicarboxylic Acid TransportersUncoupling AgentsEscherichia coli ProteinsBiological TransportGeneral MedicineMetabolismHydrogen-Ion ConcentrationFumarate reductasebiology.organism_classificationEnterobacteriaceaeBiochemistryMutationFermentationEffluxCarrier ProteinsArchives of Microbiology
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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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The selection of aptamers specific for membrane molecular targets

2010

AbstractA growing number of RNA aptamers have been selected experimentally using the SELEX combinatorial approach, and these aptamers have several advantages over monoclonal protein antibodies or peptides with respect to their applications in medicine and nanobiotechnology. Relatively few successful selections have been reported for membrane molecular targets, in contrast to the situation with non-membrane molecular targets. This review compares the procedures and techniques used in selections against membrane proteins and membrane lipids. In the case of membrane proteins, the selections were performed against soluble protein fragments, detergent-membrane protein mixed micelles, whole cells…

AptamerMembrane lipidsReviewBiologyAptamersBiochemistryCell membraneMembrane LipidsRaftsMembrane transportersmedicineMolecular BiologyMembranesSELEXVesicleCell MembraneSELEX Aptamer TechniqueMembrane ProteinsCell BiologyAptamers NucleotideLipidsmedicine.anatomical_structureMembraneMembrane proteinBiochemistryLiposomesVirusesSELEX Aptamer TechniqueRNASystematic evolution of ligands by exponential enrichmentCellular and Molecular Biology Letters
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