Search results for "Membrane transport"

showing 10 items of 215 documents

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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Characterisation of serotonin transport mechanisms in rainbow trout peripheral blood lymphocytes: role in PHA-induced lymphoproliferation

1999

Abstract AbstractIn this study we investigated the serotonin transport mechanisms in rainbow trout (Oncorhynchus mykiss) peripheral blood lymphocytes We have observed that the transport of serotonin is a membrane transport process that have the properties of a secondary active transport system The binding isotherm of [3H]-paroxetine a serotonin transport blocker demonstrated a high-affinity binding site with a positive type of cooperativity Hill coefficient being higher than unity Known specific inhibitors of the mammalian serotonin transporter significantly inhibited the uptake process in fish lymphocytes In order to demonstrate the physiological relevance of the serotonin transporter in T…

AgonistSerotoninmedicine.medical_specialtySerotonin uptakemedicine.drug_classImmunologySerotonin transportNerve Tissue ProteinsLymphocyte ActivationInternal medicineCyclic AMPmedicineAnimalsLymphocytesPhytohemagglutininsSerotonin Uptake InhibitorsSerotonin transporterSerotonin Plasma Membrane Transport ProteinsMembrane GlycoproteinsbiologyMembrane Transport ProteinsBiological TransportMembrane transportEndocrinologyOncorhynchus mykissActive transportbiology.proteinSerotoninCarrier ProteinsSelective Serotonin Reuptake InhibitorsDevelopmental BiologyDevelopmental & Comparative Immunology
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Computer simulations for bioequivalence trials: Selection of analyte in BCS class II and IV drugs with first-pass metabolism, two metabolic pathways …

2018

A semi-physiological two compartment pharmacokinetic model with two active metabolites (primary (PM) and secondary metabolites (SM)) with saturable and non-saturable pre-systemic efflux transporter, intestinal and hepatic metabolism has been developed. The aim of this work is to explore in several scenarios which analyte (parent drug or any of the metabolites) is the most sensitive to changes in drug product performance (i.e. differences in in vivo dissolution) and to make recommendations based on the simulations outcome. A total of 128 scenarios (2 Biopharmaceutics Classification System (BCS) drug types, 2 levels of KM Pgp, in 4 metabolic scenarios at 2 dose levels in 4 quality levels of t…

AnalyteCmaxPharmaceutical ScienceAdministration Oral02 engineering and technologyEquivalence Trials as TopicPharmacologyBioequivalence030226 pharmacology & pharmacyModels Biological03 medical and health sciencesFirst pass effect0302 clinical medicinePharmacokineticsHumansComputer SimulationPharmacokineticsIntestinal MucosaBiotransformationChemistryMembrane Transport Proteins021001 nanoscience & nanotechnologyBiopharmaceutics Classification SystemNONMEMNonlinear DynamicsPharmaceutical PreparationsSolubilityTherapeutic EquivalencyResearch DesignArea Under CurveLinear Models0210 nano-technologyMonte Carlo MethodDrug metabolismEuropean journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences
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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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Facilitated Anion Transport Induces Hyperpolarization of the Cell Membrane That Triggers Differentiation and Cell Death in Cancer Stem Cells

2015

Facilitated anion transport potentially represents a powerful tool to modulate various cellular functions. However, research into the biological effects of small molecule anionophores is still at an early stage. Here we have used two potent anionophore molecules inspired in the structure of marine metabolites tambjamines to gain insight into the effect induced by these compounds at the cellular level. We show how active anionophores, capable of facilitating the transmembrane transport of chloride and bicarbonate in model phospholipid liposomes, induce acidification of the cytosol and hyperpolarization of plasma cell membranes. We demonstrate how this combined effect can be used against canc…

AnionsPHPhysiologyCellular differentiationTRANSMEMBRANE TRANSPORTChemistry OrganicFisiologiaPROGRESSIONApoptosisNanotechnologyStem cellsBiochemistryCatalysisCell LineMembrane PotentialsCell membraneColloid and Surface ChemistryCancer stem cellBINDINGPathologymedicineHumansSYNTHETIC ION CHANNELSMembrane potentialIon TransportANALOGSChemistryCHLORIDE TRANSPORTCell MembraneApoptosiQuímica orgánicaCell DifferentiationMICROBIOLOGIAGeneral ChemistryHyperpolarization (biology)Membrane transportCARRIERSPatologiaAPOPTOSISCell biologyCytosolmedicine.anatomical_structureLiposomesCancer cellNeoplastic Stem CellsCèl·lules mareJournal of the American Chemical Society
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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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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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The Low-Affinity ATP Binding Site of the Escherichia coli SecA Dimer Is Localized at the Subunit Interface

1997

The homodimeric SecA protein is the ATP-dependent force generator in the Escherichia coli precursor protein translocation cascade. SecA contains two essential nucleotide binding sites (NBSs), i.e., NBS1 and NBS2 that hind ATP with high and low affinity, respectively. The photoactivatable bifunctional cross-linking agent 3'-arylazido-8-azidoadenosine 5'-triphosphate (diN(3)ATP) was used to investigate the spatial arrangement of the nucleotide binding sites of SecA, DiN(3)ATP is an authentic ATP analogue as it supports SecA-dependent precursor protein translocation and translocation ATPase, UV-induced photo-cross-linking of the diN(3)ATP-bound SecA results in the formation of stable dimeric s…

AzidesUltraviolet RaysProtein subunitATPaseDimerMutantPhotoaffinity LabelsBiologymedicine.disease_causeESSENTIAL COMPONENTenvironment and public healthBiochemistryBACILLUS-SUBTILISchemistry.chemical_compoundAdenosine TriphosphateBacterial ProteinsPROTON MOTIVE FORCEEscherichia colimedicinePRECURSOR PROTEIN TRANSLOCATIONNucleotideBinding siteEscherichia coliAdenosine Triphosphataseschemistry.chemical_classificationBinding SitesSecA ProteinsNucleotidesChemiosmosisEscherichia coli ProteinsMembrane Transport ProteinsPHOTOAFFINITY CROSS-LINKINGCross-Linking ReagentschemistryBiochemistryMEMBRANE-VESICLES REQUIRESPLASMA-MEMBRANE3'-ARYLAZIDO-BETA-ALANYL-8-AZIDO ATPCYTOPLASMIC MEMBRANEbiology.proteinPREPROTEIN TRANSLOCASEbacteriaDimerizationSEC Translocation ChannelsBiochemistry
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Functional characterization of ORCTL2--an organic cation transporter expressed in the renal proximal tubules.

1998

AbstractChromosome 11p15.5 harbors a gene or genes involved in Beckwith-Wiedemann syndrome that confer(s) susceptibility to Wilms' tumor, rhabdomyosarcoma, and hepatoblastoma. We have previously identified a transcript at 11p15.5 which encodes a putative membrane transport protein, designated organic cation transporter-like 2 (ORCTL2), that shares homology with tetracycline resistance proteins and bacterial multidrug resistance proteins. In this report, we have investigated the transport properties of ORCTL2 and show that this protein can confer resistance to chloroquine and quinidine when overexpressed in bacteria. Immunohistochemistry analyses performed with anti-ORCTL2 polyc.onal antibod…

Beckwith-Wiedemann SyndromeOrganic Cation Transport ProteinsTranscription GeneticMolecular Sequence DataBiophysicsTransfectionBiochemistryHomology (biology)11p15.5Kidney Tubules ProximalStructural BiologyGeneticsmedicineAnimalsHumansMolecular BiologyGeneTetracycline/H+ antiporterKidneyOrganic cation transport proteinsbiologyBacteriaBase SequenceMembrane transport proteinOrganic cation transporterMultidrug resistance-associated protein 2Chromosomes Human Pair 11Tetracycline ResistanceOrganic cation transporter like-2Chromosome MappingMembrane ProteinsBiological TransportChloroquineCell BiologyApical membraneTetracyclineMolecular biologyQuinidineDrug Resistance MultipleRecombinant ProteinsKineticsmedicine.anatomical_structureBiochemistryOligodeoxyribonucleotidesCOS Cellsbiology.proteinImmunohistochemistryCarrier ProteinsFEBS letters
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Involvement of the Pseudomonas aeruginosa MexAB–OprM efflux pump in the secretion of the metallophore pseudopaline

2020

ABSTRACTThe ability for all organisms to acquire metals from their environment is essential for life. To overcome the metal restriction imposed by the host’s nutritional immunity, bacterial pathogens exploits the use of small high metal affinity molecules called metallophores. Metallophores are first synthetized in the cytoplasm, then secreted into the medium where they sequester the metal. The metal-metallophore complex is then imported into the bacterium following binding to dedicated cell surface receptors. Recently, a new family of metallophores has been discovered in pathogenic bacteria called staphylopine in Staphylococcus aureus and pseudopaline in Pseudomonas aeruginosa. Here, we ar…

Bodily Secretions[SDV]Life Sciences [q-bio]Microbial Sensitivity TestsBiologymedicine.disease_causeMicrobiology03 medical and health sciencesBacterial ProteinsIn vivoDrug Resistance Multiple BacterialpseudopalinemedicineInner membraneSecretionMolecular Biology030304 developmental biology0303 health sciencesMexAB–OprMBacteriametallophoreChemistry030306 microbiologyPseudomonas aeruginosaMembrane Transport Proteinsbiology.organism_classificationIn vitroCell biology[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyCytoplasmPseudomonas aeruginosaefflux pumpEffluxCell envelopeBacterial outer membraneOligopeptidesBacteriaBacterial Outer Membrane Proteins
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