Search results for "ion transport"

showing 10 items of 162 documents

A conserved role for the mitochondrial citrate transporter Sea/SLC25A1 in the maintenance of chromosome integrity.

2009

Histone acetylation plays essential roles in cell cycle progression, DNA repair, gene expression and silencing. Although the knowledge regarding the roles of acetylation of histone lysine residues is rapidly growing, very little is known about the biochemical pathways providing the nucleus with metabolites necessary for physiological chromatin acetylation. Here, we show that mutations in the scheggia (sea)-encoded Sea protein, the Drosophila ortholog of the human mitochondrial citrate carrier Solute carrier 25 A1 (SLC25A1), impair citrate transport from mitochondria to the cytosol. Interestingly, inhibition of sea expression results in extensive chromosome breakage in mitotic cells and indu…

MaleAnion Transport ProteinsBlotting WesternMolecular Sequence DataOrganic Anion Transporterscitrate transporterSAP30BiologyModels BiologicalHistonesMitochondrial ProteinsHistone H2AGeneticsHistone codeAnimalsDrosophila ProteinsHumansAmino Acid SequenceCitratesSLC25A1Molecular BiologyGenetics (clinical)Cells CulturedConserved SequenceChromosome Aberrationsmetabolism epigenetics histone acetylation AcCoA Citrate carrierSequence Homology Amino AcidChromosome integrityhistone acetylationHDAC8AcetylationChromosome BreakageGeneral MedicineCitrate transportFibroblastsHDAC4mitochondriaHistoneBiochemistryAcetylationMutationcitrate transporter histone acetylationbiology.proteinFemaleRNA InterferenceCarrier ProteinsHuman molecular genetics
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KLHL3 mutations cause familial hyperkalemic hypertension by impairing ion transport in the distal nephron

2012

Familial hyperkalemic hypertension (FHHt) is a Mendelian form of arterial hypertension that is partially explained by mutations in WNK1 and WNK4 that lead to increased activity of the Na(+)-Cl(-) cotransporter (NCC) in the distal nephron. Using combined linkage analysis and whole-exome sequencing in two families, we identified KLHL3 as a third gene responsible for FHHt. Direct sequencing of 43 other affected individuals revealed 11 additional missense mutations that were associated with heterogeneous phenotypes and diverse modes of inheritance. Polymorphisms at KLHL3 were not associated with blood pressure. The KLHL3 protein belongs to the BTB-BACK-kelch family of actin-binding proteins tha…

MaleCarrier Proteins/geneticsPseudohypoaldosteronism/genetics/metabolism/physiopathologyPseudohypoaldosteronism[SDV]Life Sciences [q-bio]Blood Pressure030204 cardiovascular system & hematologyNephrons/metabolismKidney0302 clinical medicineMissense mutationChildComputingMilieux_MISCELLANEOUSGeneticsddc:616Aged 80 and over0303 health sciencesbiologyMicrofilament ProteinsMiddle AgedWNK1PhenotypeSodium Chloride SymportersWNK4Ubiquitin ligaseFemaleSignal TransductionAdultmedicine.medical_specialtyAdolescentBlood Pressure/geneticsIon Transport/geneticsMolecular Sequence DataPolymorphism Single Nucleotide03 medical and health sciencesYoung AdultInternal medicineGeneticsmedicineHumansAmino Acid SequenceSodium Chloride Symporters/genetics/metabolism030304 developmental biologyAdaptor Proteins Signal TransducingAgedIon TransportBase Sequenceurogenital systemPseudohypoaldosteronismKidney metabolismNephronsSequence Analysis DNAmedicine.diseaseKidney/metabolismEndocrinologyIon homeostasisbiology.proteinCarrier Proteins
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Kinetics of zinc transport in vitro in rat small intestine and colon: interaction with copper.

2002

The present study was planned to investigate the kinetic transport of zinc, in the intact intestine of the rat, in order to establish if more than one transporter is involved as well as the existence of a preferent sector in the cation uptake. Using an in vitro technique, the influx of zinc across the brush border membrane in three sectors of the small intestine (proximal, mid and distal) and in the colon of the rat was measured at six different concentrations (from 0.0007 to 11 mM). The kinetic study showed that intestinal transport of zinc occurs by a saturable process in the small intestine. The K(m) value obtained in the proximal segment (10.78+/-4.40 mM) is clearly higher than those ob…

MaleCell Membrane PermeabilityBrush borderColonKineticsPharmaceutical Sciencechemistry.chemical_elementZincIn Vitro TechniquesModels BiologicalIntestine SmallmedicineAnimalsDrug InteractionsTissue DistributionRats WistarIon TransportDose-Response Relationship DrugTransporterCopperIn vitroSmall intestineRatsDose–response relationshipZincmedicine.anatomical_structurechemistryBiochemistryIntestinal AbsorptionBiophysicsCopperEuropean journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences
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Tiagabine, a gamma-amino-butyric acid transporter inhibitor impairs spatial learning of rats in the Morris water-maze.

2002

Abstract γ-Amino-butyric acid (GABA) is cleaved from the synaptic cleft by uptake via specific transporters. Inhibition of such transporters increases the effectiveness of physiologically released GABA. Increased GABAergic neurotransmission has an impact on learning and memory. Therefore, effects of tiagabine, a GABA-transporter inhibitor, were investigated on spatial orientation in the Morris water-maze. Rats were given four training trials per day for 4 days and a probe trial without platform on the 5th day. Compared to saline treated rats, rats treated daily with 20 mg/kg tiagabine showed impaired learning during the acquisition trials. Retrieval was impaired in rats treated only at the …

MaleGABA Plasma Membrane Transport ProteinsSynaptic cleftTiagabinemedicine.medical_treatmentNipecotic AcidsMorris water navigation taskOrganic Anion TransportersPharmacologyBehavioral Neurosciencechemistry.chemical_compoundMemorymedicineGABA transporterAnimalsNeurotransmitterMaze LearningTiagabineSalineGABA AgonistsSwimmingbiologyMembrane ProteinsMembrane Transport ProteinsTransporterRats Inbred StrainsReceptors GABA-ARatschemistrybiology.proteinReuptake inhibitorCarrier ProteinsNeurosciencemedicine.drugBehavioural brain research
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Gitelman-Like Syndrome Caused by Pathogenic Variants in mtDNA

2022

Contains fulltext : 248375.pdf (Publisher’s version ) (Closed access) BACKGROUND: Gitelman syndrome is the most frequent hereditary salt-losing tubulopathy characterized by hypokalemic alkalosis and hypomagnesemia. Gitelman syndrome is caused by biallelic pathogenic variants in SLC12A3, encoding the Na(+)-Cl(-) cotransporter (NCC) expressed in the distal convoluted tubule. Pathogenic variants of CLCNKB, HNF1B, FXYD2, or KCNJ10 may result in the same renal phenotype of Gitelman syndrome, as they can lead to reduced NCC activity. For approximately 10 percent of patients with a Gitelman syndrome phenotype, the genotype is unknown. METHODS: We identified mitochondrial DNA (mtDNA) variants in th…

MaleKidneyDISEASEion transportGenotypeSolute Carrier Family 12 Member 3Gitelman-s syndromeCHANNEL GENEChildRNA Transfer IlePHOSPHORYLATIONNCCbiologygenetic renal diseaseblood pressureMetabolic Disorders Radboud Institute for Molecular Life Sciences [Radboudumc 6]General MedicineMiddle Agedchronic kidney failureTUBULENa transportPedigreemitochondriaBARTTER-SYNDROMEPhenotypemedicine.anatomical_structureMitochondrial respiratory chainMAGNESIUMNephrologyChild Preschoolepithelial sodium transportFemaleGitelman SyndromeAdultMitochondrial DNAAdolescentGenotypehuman geneticsKCNJ10DNA MitochondrialModels BiologicalPolymorphism Single NucleotideRNA Transfer PheYoung AdultTubulopathymedicineHumansDistal convoluted tubuleHYPOMAGNESEMIAAgedCLCNKBNeurodevelopmental disorders Donders Center for Medical Neuroscience [Radboudumc 7]MITOCHONDRIAL-DNA MUTATIONBase SequenceInfantGitelman syndromemedicine.diseaseMolecular biologySODIUM-CHLORIDE COTRANSPORTERHEK293 CellsRenal disorders Radboud Institute for Molecular Life Sciences [Radboudumc 11]Basic ResearchMutationbiology.proteinNucleic Acid Conformationchronic kidney disease
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Effects of typical inducers on olfactory xenobiotic-metabolizing enzyme, transporter, and transcription factor expression in rats.

2010

International audience; Several xenobiotic-metabolizing enzymes (XMEs) have been identified in the olfactory mucosa (OM) of mammals. However, the molecular mechanisms underlying the regulation of these enzymes have been little explored. In particular, information on the expression of the transcriptional factors in this tissue is quite limited. The aim of the present study was to examine the impact of five typical inducers, Aroclor 1254, 3-methylcholanthrene, dexamethasone, phenobarbital, and ethoxyquin, on the activities and mRNA expression of several XMEs in the OM and in the liver of rats. We also evaluated the effects of these treatments on the mRNA expression of transcription factors an…

MaleLIVERMESH : Transcription FactorsMESH: Microsomes Liver[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionPharmaceutical ScienceMESH : CytochromesMESH: Down-RegulationMESH: Membrane Transport ProteinsMESH : Down-RegulationCytosol0302 clinical medicineGlucocorticoid receptorMESH : Membrane Transport ProteinsMESH: CytosolMESH: Reverse Transcriptase Polymerase Chain ReactionGene expressionConstitutive androstane receptorMESH: Up-RegulationMESH: AnimalsReceptorMESH : Up-RegulationMESH: Cytochromes0303 health sciencesPregnane X receptorMESH : Metabolic Detoxication Phase IbiologyReverse Transcriptase Polymerase Chain ReactionMESH : RatsMESH : CytosolINDUCTIONMESH : Reverse Transcriptase Polymerase Chain ReactionMESH: Transcription FactorsUp-Regulation3. Good healthMESH : Microsomes LiverHYDROCARBON HYDROXYLASE-ACTIVITYmedicine.anatomical_structurePHASE-IBiochemistryMESH: Metabolic Detoxication Phase IIEnzyme InductionMicrosomes LiverMESH: Metabolic Detoxication Phase IMESH: XenobioticsMESH: Enzyme InductionMESH: RatsMESH : MaleDown-RegulationMESH : XenobioticsPHENOL SULFOTRANSFERASEMESH : Rats WistarXenobiotics03 medical and health sciencesOlfactory mucosaOlfactory MucosamedicineAnimalsRats WistarMESH: Olfactory MucosaTranscription factor030304 developmental biologyPharmacologyMESH : Olfactory MucosaIDENTIFICATIONRECEPTORMESH : Enzyme InductionMembrane Transport ProteinsMESH : Metabolic Detoxication Phase IIUDP-GLUCURONOSYLTRANSFERASEMESH: Rats WistarAryl hydrocarbon receptorORGANIC ANION TRANSPORTERMolecular biologyMetabolic Detoxication Phase IIMESH: MaleRatsNASAL-MUCOSAbiology.proteinCytochromesMetabolic Detoxication Phase IMESH : Animals[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition030217 neurology & neurosurgeryTranscription Factors
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Regulation of organic anion transporters in a new rat model of acute and chronic cholangitis resembling human primary sclerosing cholangitis

2002

Primary sclerosing cholangitis (PSC) is a cholestatic liver disease of unknown etiology. Although the primary defect affects cholangiocytes, cholestatic injury of hepatocytes may promote further liver damage. Since down-regulation of hepatocellular organic anion transporters is implicated in the molecular pathogenesis of cholestasis, expression of these transporters was determined in a novel rat model, which closely resembles human PSC.Hepatic protein and mRNA expression of basolateral (Ntcp, Oatp1, 2 and 4) and canalicular (Mrp2, Bsep) organic anion transporters were analyzed 1, 4 and 12 weeks after induction of experimental PSC by 2,4,6-trinitrobenzenesulfonic acid (TNBS).Specific down-re…

MalePathologymedicine.medical_specialtyOrganic Cation Transport ProteinsOrganic anion transporter 1Cholangitis SclerosingGene ExpressionOrganic Anion Transporters Sodium-DependentInflammationOrganic Anion Transporters Sodium-Independentdigestive systemPrimary sclerosing cholangitisSolute Carrier Organic Anion Transporter Family Member 1B3CholestasismedicineAnimalsRNA MessengerChronic CholangitisLiver injurySymportersHepatologybiologybusiness.industryMultidrug resistance-associated protein 2Membrane Transport ProteinsTransportermedicine.diseasedigestive system diseasesRatsDisease Models AnimalRats Inbred LewAcute DiseaseChronic Diseasebiology.proteinATP-Binding Cassette TransportersFemalemedicine.symptomCarrier ProteinsbusinessJournal of Hepatology
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Plasma membrane Ca2+ ATPase 4 is required for sperm motility and male fertility.

2004

Calcium and Ca(2+)-dependent signals play a crucial role in sperm motility and mammalian fertilization, but the molecules and mechanisms underlying these Ca(2+)-dependent pathways are incompletely understood. Here we show that homozygous male mice with a targeted gene deletion of isoform 4 of the plasma membrane calcium/calmodulin-dependent calcium ATPase (PMCA), which is highly enriched in the sperm tail, are infertile due to severely impaired sperm motility. Furthermore, the PMCA inhibitor 5-(and-6)-carboxyeosin diacetate succinimidyl ester reduced sperm motility in wild-type animals, thus mimicking the effects of PMCA4 deficiency on sperm motility and supporting the hypothesis of a pivot…

MaleTime FactorsBiochemistryMiceTestisProtein IsoformsCloning MolecularCation Transport Proteinsreproductive and urinary physiologySperm motilityMice KnockoutRecombination GeneticReverse Transcriptase Polymerase Chain ReactionPlasma Membrane Calcium-Transporting ATPasesFluoresceinsTransport proteinCell biologyBlotting SouthernBiochemistrySperm Motilityendocrine systemDNA ComplementaryGenotypeBlotting WesternMolecular Sequence Datachemistry.chemical_elementSuccinimidesCalcium-Transporting ATPasesFertilization in VitroCalciumBiologyPlasma Membrane Calcium-Transporting ATPasesAnimalsHumansMolecular BiologyFluorescent DyesCalcium metabolismModels Geneticurogenital systemCell BiologyBlotting NorthernSpermProtein Structure TertiaryRatsCalcium ATPaseAlternative SplicingFertilitychemistryMicroscopy FluorescencePlasma membrane Ca2+ ATPaseCalciumThe Journal of biological chemistry
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Common Genetic Variation in Relation to Brachial Vascular Dimensions and Flow-Mediated Vasodilation

2019

Common Genetic Variation in Relation to Brachial Vascular Dimensions and Flow-Mediated Vasodilation

Malemedicine.medical_specialtyBrachial ArteryVasodilationGenome-wide association studyPolymorphism Single NucleotideArticleInternal medicinemedicine.arteryGenetic variationmedicineHumanscardiovascular diseasesBrachial arteryCation Transport ProteinsUltrasonographybusiness.industryGenetic VariationGeneral MedicineMethyltransferasesta3121Middle Agedbody regionsVasodilationInsulin-Like Growth Factor Binding Protein 3PhenotypeCardiovascular DiseasesGenetic Locicardiovascular systemCardiologyMedical geneticsDilation (morphology)Femalebusinesscirculatory and respiratory physiologyFlow-Mediated Vasodilation
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Thimerosal induces calcium mobilization, fructose 2,6-bisphosphate synthesis and cytoplasmic alkalinization in rat thymus lymphocytes

1991

The effect of thimerosal on intracellular calcium ([Ca2+]i), pH (pHi) and fructose 2,6-bisphosphate (Fru 2,6-P2) in thymus lymphocytes was investigated. The effect of thimerosal on cell growth was also examined. Thimerosal produced a dose-dependent increase in [Ca2+]i, pHi and in the level of fructose 2,6-bisphosphate. Thimerosal was, however, unable to produce cell proliferation and inhibited [3H]thymidine incorporation when cells were challenged with PHA and costimulator. In the absence of external calcium, thimerosal produced only a slight increase in [Ca2+]i. In Na(+)-containing buffer, thimerosal induced an initial acidification (0.05 +/- 0.01 pH units), followed by an alkalinization o…

Malemedicine.medical_specialtyCytoplasmT-LymphocytesFluorescence spectrometrychemistry.chemical_elementBiologyCalciumLymphocyte ActivationTritiumCalcium in biologychemistry.chemical_compoundInternal medicinemedicineFructosediphosphatesAnimalsLactic AcidMolecular BiologyIon transporterProtein kinase CThimerosalSodiumThimerosalFructoseRats Inbred StrainsCell BiologyHydrogen-Ion ConcentrationRatsEndocrinologyFructose 26-bisphosphatechemistryLactatesCalciumGlycolysisHydrogenThymidine
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