Search results for "amino acid transport"

showing 10 items of 80 documents

Polyamines Impair Immunity to Helicobacter pylori by Inhibiting L-Arginine Uptake Required for Nitric Oxide Production

2010

International audience; BACKGROUND & AIMS: Helicobacter pylori-induced immune responses fail to eradicate the bacterium. Nitric oxide (NO) can kill H pylori. However, translation of inducible NO synthase (iNOS) and NO generation by H pylori-stimulated macrophages is inhibited by the polyamine spermine derived from ornithine decarboxylase (ODC), and is dependent on availability of the iNOS substrate L-arginine (L-Arg). We determined if spermine inhibits iNOS-mediated immunity by reducing L-Arg uptake into macrophages. METHODS: Levels of the inducible cationic amino acid transporter (CAT) 2, ODC, and iNOS were measured in macrophages and H pylori gastritis tissues. L-Arg uptake, iNOS expressi…

ArginineSpermineNitric Oxide Synthase Type IIArginineNitric OxideOrnithine DecarboxylaseArticleOrnithine decarboxylaseNitric oxideHelicobacter Infections03 medical and health scienceschemistry.chemical_compoundMice0302 clinical medicineImmune systemGastric mucosamedicinePolyaminesAnimalsHumansCationic Amino Acid Transporter 2Cells Cultured030304 developmental biology0303 health sciencesImmunity CellularHepatologybiologyHelicobacter pyloriReverse Transcriptase Polymerase Chain ReactionMacrophagesGastroenterology[SDV.MHEP.HEG]Life Sciences [q-bio]/Human health and pathology/Hépatology and GastroenterologyHelicobacter pyloribiology.organism_classificationMolecular biologyMice Inbred C57BLDisease Models Animalmedicine.anatomical_structurechemistryGene Expression RegulationGastric Mucosa030220 oncology & carcinogenesisGastritisRNASperminePolyamine
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Rapamycin stimulates arginine influx through CAT2 transporters in human endothelial cells

2007

In endothelial cells Tumor Necrosis Factor-alpha (TNFalpha) stimulates arginine transport through the increased expression of SLC7A2/CAT2 transcripts. Here we show that also rapamycin, an inhibitor of mTOR kinase, stimulates system y(+)-mediated arginine uptake in human endothelial cells derived from either saphenous (HSVECs) or umbilical veins (HUVECs). When used together with TNFalpha, rapamycin produces an additive stimulation of arginine transport in both cell models. These effects are observed also upon incubation with AICAR, a stimulator of Adenosine-Monophosphate-dependent-Protein Kinase (AMPK) that produces a rapamycin-independent inhibition of the mTOR pathway. Rapamycin increases …

CAT transporterArginineBlotting WesternBiophysicsBiologyArginineNitric OxideBiochemistryWestern blotSLC7A genemedicineHumansAmino AcidsPI3K/AKT/mTOR pathwayDNA PrimersSirolimusArginine transportmedicine.diagnostic_testKinaseReverse Transcriptase Polymerase Chain ReactionTumor Necrosis Factor-alphaAMPKEndothelial CellsBiological TransportCell BiologySystem y+Molecular biologyImmunohistochemistryGene Expression RegulationmTORAmino Acid Transport Systems BasicTumor necrosis factor alphaIntracellularBiochimica et Biophysica Acta (BBA) - Biomembranes
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T-cell receptor transfer into human T cells with ecotropic retroviral vectors

2014

Adoptive T-cell transfer for cancer immunotherapy requires genetic modification of T cells with recombinant T-cell receptors (TCRs). Amphotropic retroviral vectors (RVs) used for TCR transduction for this purpose are considered safe in principle. Despite this, TCR-coding and packaging vectors could theoretically recombine to produce replication competent vectors (RCVs), and transduced T-cell preparations must be proven free of RCV. To eliminate the need for RCV testing, we transduced human T cells with ecotropic RVs so potential RCV would be non-infectious for human cells. We show that transfection of synthetic messenger RNA encoding murine cationic amino-acid transporter 1 (mCAT-1), the re…

CD4-Positive T-LymphocytesAdoptive cell transfermedicine.medical_treatmentGenetic enhancementGenetic VectorsReceptors Antigen T-CellCD8-Positive T-LymphocytesBiologyImmunotherapy AdoptiveJurkat cellsVesicular stomatitis Indiana virusCell LineJurkat CellsMiceTransduction (genetics)Viral Envelope ProteinsCancer immunotherapyTransduction GeneticGeneticsmedicineAnimalsHumansRNA MessengerMolecular BiologyCationic Amino Acid Transporter 1Membrane GlycoproteinsHEK 293 cellsT-cell receptorTransfectionAdoptive TransferVirologyElectroporationHEK293 CellsRetroviridaeLeukemia Virus Gibbon ApeMolecular MedicinePlasmidsGene Therapy
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CATs and HATs: the SLC7 family of amino acid transporters

2004

The SLC7 family is divided into two subgroups, the cationic amino acid transporters (the CAT family, SLC7A1-4) and the glycoprotein-associated amino acid transporters (the gpaAT family, SLC7A5-11), also called light chains or catalytic chains of the hetero(di)meric amino acid transporters (HAT). The associated glycoproteins (heavy chains) 4F2hc (CD98) or rBAT (D2, NBAT) form the SLC3 family. Members of the CAT family transport essentially cationic amino acids by facilitated diffusion with differential trans-stimulation by intracellular substrates. In some cells, they may regulate the rate of NO synthesis by controlling the uptake of l-arginine as the substrate for nitric oxide synthase (NOS…

CD98Amino Acid Transport System y+PhysiologyStereochemistryClinical Biochemistry610 Medicine & healthLarge Neutral Amino Acid-Transporter 11308 Clinical BiochemistryImmunoglobulin light chain142-005 142-0052737 Physiology (medical)CationsPhysiology (medical)medicineAnimalsHumansAmino Acidschemistry.chemical_classificationbiologySystem LBiological TransportTransporter1314 Physiologymedicine.diseaseLysinuric protein intoleranceAmino acidchemistryBiochemistryMultigene Familybiology.protein570 Life sciences; biologyCotransporterPfl�gers Archiv European Journal of Physiology
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Interference of L-arginine analogues with L-arginine transport mediated by the y+ carrier hCAT-2B.

1997

The inducible human cationic amino acid transporter hCAT-2B was expressed in Xenopus laevis oocytes, and this system was used to test the effect of several NO synthase (NOS) inhibitors and/or L-arginine analogues on L-arginine transport by this y+ carrier. L-NG-Methyl-L-arginine (L-NMA), asymmetrical L-NG, NG-dimethyl-L-arginine (L-ADMA), L-N5-(1-iminoethyl)-ornithine (L-NIO), L-NG-nitro-L-arginine (L-NNA), and L-NG-nitro-L-arginine methyl ester (L-NAME) all inhibited the inducible NOS II extracted from RAW 264.7 macrophages induced with bacterial lipopolysaccharide. L-NMA, L-ADMA, and L-NIO also competed with L-arginine for transport by hCAT-2B, whereas L-NNA and L-NAME did not. The two L-…

Cancer ResearchArginineLipopolysaccharideMonosaccharide Transport ProteinsPhysiologyStereochemistryClinical BiochemistryNitric Oxide Synthase Type IIArginineBiochemistryCell Linechemistry.chemical_compoundMiceXenopus laevisAnimalsHumansAmino acid transporterEnzyme Inhibitorschemistry.chemical_classificationGlucose Transporter Type 1Arginine transportChemistryLysineCationic polymerizationSubstrate (chemistry)Membrane ProteinsTransporterBiological TransportRatsEnzymeGlucoseBiochemistryOocytesAmino Acid Transport Systems BasicNitric Oxide SynthaseCarrier ProteinsNitric oxide : biology and chemistry
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Caveolin and GLT-1 gene expression is reciprocally regulated in primary astrocytes: Association of GLT-1 with non-caveolar lipid rafts

2004

Caveolae represent membrane microdomains acting as integrators of cellular signaling and functional processes. Caveolins are involved in the biogenesis of caveolae and regulate the activity of caveolae-associated proteins. Although caveolin proteins are found in the CNS, the regulation of caveolins in neural cells is poorly described. In the present study, we investigated different modes and mechanisms of caveolin gene regulation in primary rat astrocytes. We demonstrated that activation of cAMP-dependent signaling pathways led to a marked reduction in protein levels of caveolin-1/-2 in cortical astrocytes. Application of transforming growth factor-alpha (TGF-alpha) also resulted in a decre…

Central Nervous SystemCaveolin 2Caveolin 1Down-RegulationGlutamic AcidBiologyCaveolinsHistone DeacetylasesChromatin remodelingRats Sprague-DawleyPhosphatidylinositol 3-KinasesCellular and Molecular NeuroscienceAstrocyte differentiationMembrane MicrodomainsCaveolaeCaveolinCyclic AMPAnimalsRNA MessengerLipid raftCerebral CortexRegulation of gene expressionTransforming Growth Factor alphaRatsCell biologyCaveolin 2Animals NewbornExcitatory Amino Acid Transporter 2Gene Expression RegulationNeurologyAstrocytesCaveolin 1Signal TransductionGlia
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A glial amino-acid transporter controls synapse strength and courtship in Drosophila

2008

1097-6256 (Print) Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't; Mate choice is an evolutionarily critical decision that requires the detection of multiple sex-specific signals followed by central integration of these signals to direct appropriate behavior. The mechanisms controlling mate choice remain poorly understood. Here, we show that the glial amino-acid transporter genderblind controls whether Drosophila melanogaster males will attempt to mate with other males. Genderblind (gb) mutant males showed no alteration in heterosexual courtship or copulation, but were attracted to normally unappealing male species-specific chemosensory cues. As a resul…

Central Nervous SystemMaleNervous systemAmino Acid Transport System y+media_common.quotation_subjectNeuroscience(all)Glutamic AcidArticleAnimals Genetically ModifiedCourtshipSynapseGlutamatergicmedicineAnimalsDrosophila ProteinsRNA Small Interferingmedia_commonBehavior AnimalbiologyGeneral NeuroscienceCourtshipHomosexualitybiology.organism_classificationmedicine.anatomical_structureMate choiceMutationSynapsesGenderblindDrosophilaFemaleGlutamatergic synapseDrosophila melanogaster/dk/atira/pure/subjectarea/asjc/2800NeurogliaNeuroscience
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Differential Promotion of Glutamate Transporter Expression and Function by Glucocorticoids in Astrocytes from Various Brain Regions

2005

Steroids that activate glucocorticoid receptors (GRs) and mineralocorticoid receptors have important regulatory effects on neural development, plasticity, and the body's stress response. Here, we investigated the role of corticosteroids in regulating the expression of the glial glutamate transporters glial glutamate transporter-1 (GLT-1) and glutamate-aspartate transporter (GLAST) in rat primary astrocytes. The synthetic glucocorticoid dexamethasone provoked a marked increase of GLT-1 transcription and protein levels in cortical astrocytes, whereas GLAST expression remained unaffected. Up-regulation of GLT-1 expression was accompanied by an enhanced glutamate uptake, which could be blocked …

Central Nervous SystemTime FactorsAmino Acid Transport System X-AGLigandsBiochemistryDexamethasoneRats Sprague-Dawleychemistry.chemical_compoundGlucocorticoid receptorMineralocorticoid receptorAdrenal Cortex HormonesCorticosteroneCerebellumGene expressionLuciferasesReceptorDNA Modification MethylasesKainic AcidReverse Transcriptase Polymerase Chain ReactionGlutamate receptorBrainImmunohistochemistryUp-RegulationMifepristoneAzacitidineNeurogliaGlucocorticoidmedicine.drugmedicine.medical_specialtymedicine.drug_classBlotting WesternDetergentsBiologyDecitabineTransfectionMembrane MicrodomainsInternal medicinemedicineAnimalsGlucocorticoidsMolecular BiologyDNA PrimersFluorescent DyesDose-Response Relationship DrugCell BiologyDNA MethylationRatsReceptors MineralocorticoidEndocrinologychemistryMineralocorticoidAstrocytesCorticosteroneJournal of Biological Chemistry
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Transporter-mediated replacement of extracellular glutamate for GABA in the developing murine neocortex

2013

During early development, cortical neurons migrate from their places of origin to their final destinations where they differentiate and establish synaptic connections. During corticogenesis, radially migrating cells move from deeper zone to the marginal zone, but they do not invade the latter. This "stop" function of the marginal zone is mediated by a number of factors, including glutamate and γ-aminobutyric acid (GABA), two main neurotransmitters in the central nervous system. In the marginal zone, GABA has been shown to be released via GABA transporters (GAT)-2/3, whereas glutamate transporters (EAATs) operate in the uptake mode. In this study, GABAergic postsynaptic currents (GPSCs) were…

GABA Plasma Membrane Transport ProteinsAmino Acid Transport System X-AGGlutamic AcidNeocortexBiologyGABAB receptorMicemedicineAnimalsGABA transporterGABAergic Neuronsgamma-Aminobutyric AcidNeocortexGeneral NeuroscienceSodiumGlutamate receptorDepolarizationSynaptic PotentialsMarginal zoneCell biologyMice Inbred C57BLmedicine.anatomical_structurebiology.proteinGABAergicGABA Uptake InhibitorsNeuroscienceIntracellularEuropean Journal of Neuroscience
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Identification of Cysteine Residues in Human Cationic Amino Acid Transporter hCAT-2A That Are Targets for Inhibition by N-Ethylmaleimide

2013

In most cells, cationic amino acids such as l-arginine, l-lysine, and l-ornithine are transported by cationic (CAT) and y(+)L (y(+)LAT) amino acid transporters. In human erythrocytes, the cysteine-modifying agent N-ethylmaleimide (NEM) has been shown to inhibit system y(+) (most likely CAT-1), but not system y(+)L (Devés, R., Angelo, S., and Chávez, P. (1993) J. Physiol. 468, 753-766). We thus wondered if sensitivity to NEM distinguishes generally all CAT and y(+)LAT isoforms. Transport assays in Xenopus laevis oocytes established that indeed all human CATs (including the low affinity hCAT-2A), but neither y(+)LAT isoform, are inhibited by NEM. hCAT-2A inhibition was not due to reduced tran…

Gene isoformMutantMutation MissenseXenopusBiologyBiochemistryXenopus laevischemistry.chemical_compoundMembrane BiologyAnimalsHumansheterocyclic compoundsCysteineAmino acid transporterEnzyme InhibitorsMolecular Biologychemistry.chemical_classificationN-EthylmaleimideTransporterCell Biologybiology.organism_classificationMolecular biologyProtein Structure TertiaryAmino acidAmino Acid SubstitutionchemistryBiochemistryEthylmaleimideOocytesAmino Acid Transport Systems BasicCysteineJournal of Biological Chemistry
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