Search results for "Cationic Amino Acid Transporter 2"

showing 5 items of 5 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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Intracellular accumulation of l-Arg, kinetics of transport, and potassium leak conductance in oocytes from Xenopus laevis expressing hCAT-1, hCAT-2A,…

2004

AbstractCationic amino acid transporters play an important role in the intracellular supply of l-Arg and the generation of nitric oxide. Since the transport of l-Arg is voltage-dependent, we aimed at determining the intracellular l-Arg concentration and describing the transport of l-Arg in terms of Michaelis–Menten kinetics, taking into account membrane voltage. The human isoforms of the cationic amino acid transporters, hCAT-1, hCAT-2A, and hCAT-2B, were expressed in oocytes from Xenopus laevis and studied with the voltage clamp technique and in tracer experiments. We found that l-Arg was concentrated intracellularly by all hCAT isoforms and that influx and efflux, in the steady state of e…

Patch-Clamp TechniquesVoltage clampXenopusBiophysicsArginineBiochemistryMembrane PotentialsXenopus laevisVoltage dependencehCATAnimalsPatch clampCationic Amino Acid Transporter 2y+Cationic Amino Acid Transporter 1Membrane potentialbiologyChemistryBiological TransportTransporterCell Biologybiology.organism_classificationVmaxKMKineticsBiochemistryConductanceOocytesPotassiumBiophysicsAmino Acid Transport Systems BasicEffluxSteady state (chemistry)IntracellularBiochimica et Biophysica Acta (BBA) - Biomembranes
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Two amino acid residues determine the low substrate affinity of human cationic amino acid transporter-2A.

2003

Mammalian cationic amino acid transporters (CAT) differ in their substrate affinity and sensitivity to trans-stimulation. The apparent Km values for cationic amino acids and the sensitivity to trans-stimulation of CAT-1, -2B, and -3 are characteristic of system y+. In contrast, CAT-2A exhibits a 10-fold lower substrate affinity and is largely independent of substrate at the trans-side of the membrane. CAT-2A and -2B demonstrate such divergent transport properties, even though their amino acid sequences differ only in a stretch of 42 amino acids. Here, we identify two amino acid residues within this 42-amino acid domain of the human CAT-2A protein that are responsible for the apparent low af…

Protein ConformationRecombinant Fusion ProteinsBlotting WesternGreen Fluorescent ProteinsMolecular Sequence DataGene ExpressionArginineTransfectionBiochemistryStructure-Activity RelationshipXenopus laevisExtracellularAnimalsHumansBiotinylationAmino acid transporterAmino Acid SequenceAmino AcidsCationic Amino Acid Transporter 2Molecular BiologyGlutathione Transferasechemistry.chemical_classificationBinding SitesSubstrate (chemistry)Biological TransportCell BiologyPhoto-reactive amino acid analogAmino acidTransmembrane domainLuminescent ProteinsS-tagchemistryBiochemistryMutagenesis Site-DirectedOocytesElectrophoresis Polyacrylamide GelFemaleIntracellularThe Journal of biological chemistry
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Paradoxical effect of l-arginine: Acceleration of endothelial cell senescence

2009

We have recently shown that inhibition of nitric oxide (NO) synthesis by asymmetrical dimethylarginine (ADMA) accelerated endothelial cell (EC) senescence which was prevented by coincubation with L-arginine; however the effect of long-term treatment of l-arginine alone on senescence of ECs have not been investigated. Human ECs were cultured in medium containing different concentrations of L-arginine until senescence. L-Arginine paradoxically accelerated senescence indicated by inhibiting telomerase activity. Moreover, L-arginine decreased NO metabolites, increased peroxynitrite, and 8-iso-prostaglandin F(2alpha) formation. In old cells, the mRNA expression of human amino acid transporter (h…

SenescenceArginineEndotheliumBiophysicsBiologyArginineNitric OxideBiochemistryNitric oxidechemistry.chemical_compoundmedicineHumansCationic Amino Acid Transporter 2Molecular BiologyCells CulturedCellular SenescenceCationic Amino Acid Transporter 1ArginaseEndothelial CellsCell BiologyTransfectionMolecular biologyArginaseEndothelial stem cellOxidative Stressmedicine.anatomical_structurechemistryEndothelium VascularPeroxynitriteBiochemical and Biophysical Research Communications
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The stimulation of arginine transport by TNFα in human endothelial cells depends on NF-κB activation

2004

In human saphenous vein endothelial cells (HSVECs), tumor necrosis factor-alpha (TNFalpha) and bacterial lipopolysaccharide (LPS), but neither interferon gamma (IFNgamma) nor interleukin 1beta (IL-1beta), stimulate arginine transport. The effects of TNFalpha and LPS are due solely to the enhancement of system y+ activity, whereas system y+L is substantially unaffected. TNFalpha causes an increased expression of SLC7A2/CAT-2B gene while SLC7A1/CAT-1 expression is not altered by the cytokine. The suppression of PKC-dependent transduction pathways, obtained with the inhibitor chelerytrhine, the inhibitor peptide of PKCzeta isoform, or chronic exposure to phorbol esters, does not prevent TNFalp…

MAPK/ERK pathwayLipopolysaccharidesmedicine.medical_specialtyUmbilical VeinsTime FactorsCAT transporterArginineTranscription Geneticp38 mitogen-activated protein kinasesmedicine.medical_treatmentBiophysicsPharmacologyBiologyArgininePolymerase Chain Reactionp38 Mitogen-Activated Protein KinasesBiochemistryInterferon-gammaInternal medicineCationsmedicineTNFαHumansInterferon gammaRNA MessengerCationic Amino Acid Transporter 2Cells CulturedProtein Kinase CArginine transportReverse Transcriptase Polymerase Chain ReactionTumor Necrosis Factor-alphaNF-kappa BBiological TransportCell BiologyCytokineEndocrinologySLC7 geneAmino Acid Transport Systems BasicCytokinesTumor necrosis factor alphaEndothelium VascularSignal transductionMitogen-Activated Protein KinasesPeptidesmedicine.drugInterleukin-1Signal TransductionNFκBBiochimica et Biophysica Acta (BBA) - Biomembranes
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