Search results for "Transport system"

showing 10 items of 77 documents

CyaC, a redox-regulated adenylate cyclase of Sinorhizobium meliloti with a quinone responsive diheme-B membrane anchor domain.

2019

The nucleotide cyclase CyaC of Sinorhizobium meliloti is a member of class III adenylate cyclases (AC), a diverse group present in all forms of life. CyaC is membrane-integral by a hexahelical membrane domain (6TM) with the basic topology of mammalian ACs. The 6TM domain of CyaC contains a tetra-histidine signature that is universally present in the membrane anchors of bacterial diheme-B succinate-quinone oxidoreductases. Heterologous expression of cyaC imparted activity for cAMP formation from ATP to Escherichia coli, whereas guanylate cyclase activity was not detectable. Detergent solubilized and purified CyaC was a diheme-B protein and carried a binuclear iron-sulfur cluster. Single poin…

Amino Acid Transport SystemsAdenylate kinasemedicine.disease_causeMicrobiologyCyclase03 medical and health sciencesmedicineBenzoquinonesNucleotideHistidineAmino Acid SequenceMolecular BiologyEscherichia coliHistidine030304 developmental biologychemistry.chemical_classification0303 health sciencesSinorhizobium melilotibiology030306 microbiologyEscherichia coli ProteinsGuanylate cyclase activityQuinonesMembrane Proteinsbiology.organism_classificationchemistryBiochemistryGenes BacterialHeterologous expressionOxidation-ReductionAdenylyl CyclasesSinorhizobium melilotiMolecular microbiology
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Voltage dependence of L-arginine transport by hCAT-2A and hCAT-2B expressed in oocytes from Xenopus laevis.

2000

Membrane potential and currents were investigated with the two-electrode voltage-clamp technique in Xenopus laevisoocytes expressing hCAT-2A or hCAT-2B, the splice variants of the human cationic amino acid transporter hCAT-2. Both hCAT-2A- and hCAT-2B-expressing oocytes exhibited a negative extracellularl-arginine concentration ([l-Arg]o)-sensitive membrane potential, additive to the K+diffusion potential, when cells were incubated in Leibovitz medium (containing 1.45 mM l-Arg and 0.25 mM l-lysine). The two carrier proteins produced inward and outward currents, which were dependent on the l-Arg gradient and membrane potential. Ion substitution experiments showed that the hCAT-induced curren…

ArgininePhysiologyXenopusBiologyArginineL-arginine transportXenopus laevisElectrochemistryAnimalsHumansProtein IsoformsspliceAmino acid transporterMembrane potentialMembrane ProteinsBiological TransportCell BiologyMembrane transportbiology.organism_classificationIn vitroCell biologyElectrophysiologyKineticsBiochemistryOocytesAmino Acid Transport Systems BasicFemaleCarrier ProteinsAmerican journal of physiology. Cell physiology
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INFγ stimulates arginine transport through system y+L in human monocytes

2004

Freshly isolated human monocytes transport L-arginine mostly through a sodium independent, NEM insensitive pathway inhibited by L-leucine in the presence, but not in the absence of sodium. Interferon-gamma (IFNgamma) stimulates this pathway, identifiable with system y+L, and markedly enhances the expression of SLC7A7, the gene that encodes for system y+L subunit y+LAT1, but not of SLC7A6, that codes for the alternative subunit y+LAT2. System y+ plays a minor role in arginine uptake by monocytes and the expression of system y+-related genes, SLC7A1 and SLC7A2, is not changed by IFNgamma. These results demonstrate that system y+L is sensitive to IFNgamma.

ArginineSodiumProtein subunitBiophysicschemistry.chemical_elementBiologyLPI - Lysinuric protein intoleranceArginineMonocyteBiochemistryMonocytesInterferon-gammaInterferon γLeucineStructural BiologyArginine transportSystem y+L.GeneticsmedicineHumansMolecular BiologyGeneLysinuric protein intoleranceCells CulturedArginine transportReverse Transcriptase Polymerase Chain ReactionFusion Regulatory Protein 1 Light ChainsMonocyteSodiumAmino Acid Transport System y+LBiological TransportCell BiologyMolecular biologyRecombinant ProteinsKineticsmedicine.anatomical_structurechemistryEthylmaleimideAmino Acid Transport Systems BasicInterferon-γFEBS Letters
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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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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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Car sharing demand estimation and urban transport demand modelling using stated preference techniques

2008

The research deals with the use of the stated preference technique (SP) and transport demand modelling to analyse travel mode choice behaviour for commuting urban trips in Palermo, Italy. The principal aim of the study was the calibration of a demand model to forecast the modal split of the urban transport demand, allowing for the possibility of using innovative transport systems like car sharing and car pooling. In order to estimate the demand model parameters, a specific survey was carried out inside the urban area of Palermo. The survey focused on the morning rush hour and involved mainly employees, self-employed workers and students (about 500 respondents) whose final destination was lo…

Car sharingSettore ICAR/05 - Trasporticar sharing demand modelling stated preferencesCar poolingStated PreferenceSustainable transport systemsRandom Utility ModelsCar sharing Car pooling Stated Preference Random Utility Models Sustainable transport systems
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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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Ein schnelles on-line trennsystem unter anwendung von helium-jet- und zentrifugentechnik

1975

Abstract A centrifuge for continuous liquid-liquid phase separation is described. It is designed for rapid solvent extraction of short-lived radioactive isotopes (half-lives in the order of seconds). The centrifuge is characterized by simple construction and operation principle, easy handling, low cost, and a minimum hold-up time of less than five seconds (phase purity 99.0–99.9%). The on-line connection to a helium-jet transport system is described. Problems concerning the transfer of activities into a liquid phase from the helium-jet at atmospheric pressure are discussed.

CentrifugeMaterials scienceAtmospheric pressureAnalytical chemistryLiquid phaseGeneral MedicineSolvent extractionPhase purityTransport systemNuclear Instruments and Methods
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