Search results for "Biological Transport"

showing 10 items of 323 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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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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A plant genetically modified that accumulates Pb is especially promising for phytoremediation

2003

6 pages, 3 figures, 1 table.

AgrobacteriumBiophysicsPlant RootsBiochemistryHyperaccumulatorsBioremediationMetals HeavyTobaccoBotanyNicotiana glaucaHyperaccumulatorMolecular BiologyGlucuronidaseNicotianabiologyfungiWild typefood and beveragesBiological TransportCell BiologyPlants Genetically Modifiedbiology.organism_classificationRecombinant ProteinsGenetically modified organismPhytoremediationBiodegradation EnvironmentalLeadSeedlingPhytochelatin synthaseBioremediationCadmium
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Assessment of determinants affecting the dual topology of hepadnaviral large envelope proteins

2004

For functional diversity, the large (L) envelope protein of hepatitis B virus (HBV) acquires a dual transmembrane topology via co-translational membrane integration of the S region and partial post-translational translocation of the preS subdomain. Because each process requires the second transmembrane segment (TM2), we explored the action of this determinant by using protease protection analysis of mutant L proteins. We demonstrated that neither the disruption of a leucine zipper-like motif by multiple alanine substitutions nor the flanking charges of TM2 affected the topological reorientation of L. The dispensability of both putative subunit interaction modules argues against a link betwe…

AlanineHepatitis B virusHepatitis B virusVirus AssemblyAmino Acid MotifsMolecular Sequence DataProtein domainPhenotype mixingBiological TransportBiologyEndoplasmic Reticulummedicine.disease_causeVirologyTransmembrane domainDual topologyAmino Acid SubstitutionViral Envelope ProteinsVirologyMembrane topologymedicineHepadnavirusAmino Acid SequenceProtein Processing Post-TranslationalJournal of General Virology
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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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Cationic amino acid transport across the blood-brain barrier is mediated exclusively by system y+.

2006

Cationic amino acid (CAA) transport is brought about by two families of proteins that are found in various tissues: Cat (CAA transporter), referred to as system y+, and Bat [broad-scope amino acid (AA) transporter], which comprises systems b0,+, B0,+, and y+L. CAA traverse the blood-brain barrier (BBB), but experiments done in vivo have only been able to examine the BBB from the luminal (blood-facing) side. In the present study, plasma membranes isolated from bovine brain microvessels were used to identify and characterize the CAA transporter(s) on both sides of the BBB. From these studies, it was concluded that system y+was the only transporter present, with a prevalence of activity on the…

Amino Acid Transport System y+PhysiologyStereochemistryPolarity (physics)Endocrinology Diabetes and MetabolismBiological Transport ActiveBiologyBlood–brain barrierNitric OxidePhysiology (medical)CationsmedicineAnimalsAmino AcidsCells Culturedchemistry.chemical_classificationCationic polymerizationEndothelial CellsTransporterAmino acidmedicine.anatomical_structureBiochemistrychemistryBlood-Brain BarrierAmino Acid Transport Systems BasicCattleNitric Oxide SynthaseAmerican journal of physiology. Endocrinology and metabolism
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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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Lidocaine inhibits potassium efflux and hemolysis in erythrocytes during oxidative stress in vitro.

2000

Lidocaine is a widely used local anesthetic agent. The aim of this work was to study the action of lidocaine on human red blood cells exposed to an oxidative stress in vitro. Blood was obtained from healthy volunteers. After separation from plasma, the erythrocytes were suspended in phosphate buffer. Oxidative stress was induced by incubation with a free radical generator, the 2,2' azobis (2-amidinopropane) hydrochloride (AAPH). Erythrocytes were incubated with or without lidocaine at two concentrations (36.93 and 73.85 microM) and with or without AAPH (20 mM). Electron paramagnetic resonance (EPR) spectroscopy was performed to identify the free radical species generated by AAPH using the s…

AntioxidantErythrocytesOxygen radical absorbance capacityLidocaineRadicalPotassiummedicine.medical_treatmentAmidineschemistry.chemical_elementIn Vitro Techniquesmedicine.disease_causeHemolysisAntioxidantsmedicineHumansAnesthetics LocalPharmacologyChromatographyElectron Spin Resonance SpectroscopyLidocaineBiological Transportmedicine.diseaseOxidantsHemolysisRed blood cellOxidative Stressmedicine.anatomical_structureBiochemistrychemistryPotassiumOxidative stressmedicine.drugGeneral pharmacology
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In vitro bioaccessibility, transepithelial transport and antioxidant activity of Urtica dioica L. phenolic compounds in nettle based food products

2016

Nettle (Urtica dioica L.) is a well-known plant with a wide historical background use of stems, roots and leaves. Nettle leaves are an excellent source of phenolic compounds, principally 3-caffeoylquinic acid (3-CQA), caffeoylmalic acid (CMA) and rutin. The aim of this work was to evaluate the bioaccessibility (BAC), the bioavailability (BAV) and the antioxidant activity of nettle phenolic compounds present in foods and supplements. The BAC of nettle phenolics was evaluated with an in vitro dynamic digestion of real food matrices: the type of food matrix and chemical characteristic affected the kinetics of release and solubilization, with the highest BAC after duodenal digestion. A study of…

Antioxidantfood.ingredientFree Radicalsmedicine.medical_treatmentphenolicsBiological AvailabilityAntioxidantsNOchemistry.chemical_compoundRutinnettle phenolics HPLC-MS0404 agricultural biotechnologyfoodSuperoxidesmedicineHumansFood scienceUrtica dioicaUrticaUrtica dioicaBiological Transport04 agricultural and veterinary sciencesGeneral Medicinenettle040401 food scienceCaffeoylmalic acidBioavailabilityHPLC-MSBiochemistrychemistryFermentationCaco-2 CellsDigestionFood AnalysisFood Science
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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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