Search results for "XENOPUS LAEVIS"

showing 10 items of 43 documents

Human cationic amino acid transporter hCAT-3 is preferentially expressed in peripheral tissues.

2001

At least five distinct carrier proteins form the family of mammalian cationic amino acid transporters (CATs). We have cloned a cDNA containing the complete coding region of human CAT-3. hCAT-3 is glycosylated and localized to the plasma membrane. Transport studies in Xenopus laevis oocytes revealed that hCAT-3 is selective for cationic L-amino acids and exhibits a maximal transport activity similar to other CAT proteins. The apparent substrate affinity and sensitivity to trans-stimulation of hCAT-3 resembles most closely hCAT-2B. This is in contrast to rat and murine CAT-3 proteins that have been reported to display a very low activity and to be inhibited by neutral and anionic L-amino acid…

MaleDNA ComplementaryGene ExpressionThymus GlandIn Vitro TechniquesBiochemistryCell LineMiceXenopus laevisComplementary DNACoding regionAnimalsHumansTissue DistributionAmino acid transporterAmino Acid SequenceCationic Amino Acid Transporterschemistry.chemical_classificationCATSBase SequenceChemistryCationic polymerizationBrainMembrane ProteinsAmino acidRatsBiochemistryCarrier proteinOocytesAmino Acid Transport Systems BasicFemaleCarrier ProteinsBiochemistry
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Applying Support Vector Machines for Gene Ontology based gene function prediction.

2004

Abstract Background The current progress in sequencing projects calls for rapid, reliable and accurate function assignments of gene products. A variety of methods has been designed to annotate sequences on a large scale. However, these methods can either only be applied for specific subsets, or their results are not formalised, or they do not provide precise confidence estimates for their predictions. Results We have developed a large-scale annotation system that tackles all of these shortcomings. In our approach, annotation was provided through Gene Ontology terms by applying multiple Support Vector Machines (SVM) for the classification of correct and false predictions. The general perform…

Methodology ArticleGenes FungalGenes ProtozoanComputational BiologyGenes Insectlcsh:Computer applications to medicine. Medical informaticsGenes PlantRatsMiceXenopus laevislcsh:Biology (General)GenesArtificial IntelligenceGenes BacterialPredictive Value of TestsDatabases Geneticlcsh:R858-859.7AnimalsNeural Networks Computerlcsh:QH301-705.5Genes HelminthBMC bioinformatics
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Synthesis of GABAA receptor agonists and evaluation of their alpha-subunit selectivity and orientation in the GABA binding site.

2008

Drugs used to treat various disorders target GABA A receptors. To develop alpha subunit selective compounds, we synthesized 5-(4-piperidyl)-3-isoxazolol (4-PIOL) derivatives. The 3-isoxazolol moiety was substituted by 1,3,5-oxadiazol-2-one, 1,3,5-oxadiazol-2-thione, and substituted 1,2,4-triazol-3-ol heterocycles with modifications to the basic piperidine substituent as well as substituents without basic nitrogen. Compounds were screened by [(3)H]muscimol binding and in patch-clamp experiments with heterologously expressed GABA A alpha ibeta 3gamma 2 receptors (i = 1-6). The effects of 5-aminomethyl-3 H-[1,3,4]oxadiazol-2-one 5d were comparable to GABA for all alpha subunit isoforms. 5-pipe…

Models MolecularPatch-Clamp TechniquesStereochemistryAlpha (ethology)gamma-Aminobutyric acidArticleGABAA-rho receptorCell Linechemistry.chemical_compoundStructure-Activity RelationshipXenopus laevisPiperidinesDrug DiscoverymedicineAnimalsHumansGABA-A Receptor AgonistsBinding siteReceptorgamma-Aminobutyric AcidG alpha subunitBinding SitesMolecular StructureChemistryGABAA receptorMuscimolBrainIsoxazolesReceptors GABA-ARatsElectrophysiologyProtein SubunitsBiochemistryMuscimolMutationOocytesMolecular MedicineFemalemedicine.drugJournal of medicinal chemistry
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Sizzled Is Unique among Secreted Frizzled-related Proteins for Its Ability to Specifically Inhibit Bone Morphogenetic Protein-1 (BMP-1)/Tolloid-like …

2012

BMP-1/tolloid-like proteinases (BTPs) are major enzymes involved in extracellular matrix assembly and activation of bioactive molecules, both growth factors and anti-angiogenic molecules. Although the control of BTP activity by several enhancing molecules is well established, the possibility that regulation also occurs through endogenous inhibitors is still debated. Secreted frizzled-related proteins (sFRPs) have been studied as possible candidates, with highly contradictory results, after the demonstration that sizzled, a sFRP found in Xenopus and zebrafish, was a potent inhibitor of Xenopus and zebrafish tolloid-like proteases. In this study, we demonstrate that mammalian sFRP-1, -2, and …

Models MolecularProteasesFrizzledanimal structuresMolecular Sequence DataXenopusXenopus ProteinsBiochemistryBone morphogenetic protein 1Bone Morphogenetic Protein 1MiceXenopus laevismedicineAnimalsHumansProtease InhibitorsAmino Acid SequenceMolecular BiologyZebrafishGlycoproteinsSequence Homology Amino AcidbiologyExtracellular matrix assemblyfungiIntracellular Signaling Peptides and ProteinsTissue Inhibitor of MetalloproteinasesCell BiologySurface Plasmon Resonancebiology.organism_classificationMatrix MetalloproteinasesRecombinant ProteinsExtracellular MatrixWnt ProteinsBiochemistryMechanism of actionembryonic structuresEnzymologySignal transductionmedicine.symptomPeptide HydrolasesSignal TransductionJournal of Biological Chemistry
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Structural and Functional Similarity of Amphibian Constitutive Androstane Receptor with Mammalian Pregnane X Receptor

2016

The nuclear receptors and xenosensors constitutive androstane receptor (CAR, NR1I3) and pregnane X receptor (PXR, NR1I2) induce the expression of xenobiotic metabolizing enzymes and transporters, which also affects various endobiotics. While human and mouse CAR feature a high basal activity and low induction upon ligand exposure, we recently identified two constitutive androstane receptors in Xenopus laevis (xlCARá and â) that possess PXR-like characteristics such as low basal activity and activation in response to structurally diverse compounds. Using a set of complementary computational and biochemical approaches we provide evidence for xlCARá being the structural and functional counterpa…

Models MolecularReceptors SteroidReceptors Cytoplasmic and Nuclearlcsh:MedicineMolecular Dynamics SimulationPharmacologyBiologyCrystallography X-Raydigestive systemAmphibian ProteinsCell LineXenopus laevischemistry.chemical_compoundChlorocebus aethiopsConstitutive androstane receptorCoactivatorAnimalsHumansBinding sitelcsh:ScienceReceptorConstitutive Androstane ReceptorPregnane X receptorBinding SitesMultidisciplinarylcsh:RPregnane X ReceptorCorrectionLigand (biochemistry)digestive system diseasesCell biologychemistryNuclear receptorCOS Cellslcsh:QAndrostanePLOS ONE
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Xenopus Laevis and Xenopus Tropicalis have different number of OBP genes : Xlaeobp and Xtroobp

2008

International audience

OBPOBP GENEXENOPUS TROPICALISXENOPUS LAEVIS[CHIM.OTHE] Chemical Sciences/OtherXLAEOBPODORANT BINDING PROTEIN[CHIM.OTHE]Chemical Sciences/OtherXTROOBPComputingMilieux_MISCELLANEOUS
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3D atlas describing the ontogenic evolution of the primary olfactory projections in the olfactory bulb of Xenopus laevis.

2005

The adult Xenopus presents the unique capability to smell odors both in water and air thanks to two different olfactory pathways. Nevertheless, the tadpole can initially perceive only water-borne odorants, as the olfactory receptor neurons (ORN) that will detect air-borne odorants develop later. Such a phenomenon requires major reorganization processes. Here we focused on the precise description of the neuroanatomical modifications occurring in the olfactory bulb (OB) of the tadpole throughout metamorphosis. Using both carbocyanine dyes and lectin staining, we investigated the evolution of ORN projection patterns into the OB from Stages 47 to 66, thus covering the period of time when all th…

Olfactory systemMaleOlfactory Nervemedia_common.quotation_subjectGrowth ConesXenopusOlfactionOlfactory Receptor NeuronsXenopus laevisLectinsmedicineAnimalsMetamorphosismedia_commonFluorescent DyesBrain MappingOlfactory receptorMicroscopy ConfocalbiologyGeneral NeuroscienceMetamorphosis BiologicalOlfactory PathwaysCarbocyaninesbiology.organism_classificationOlfactory BulbOlfactory bulbmedicine.anatomical_structureLarvaFemaleNeuroscienceDevelopmental biologyNeuroanatomyThe Journal of comparative neurology
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Identification and functional expression of HCx31.9, a novel gap junction gene

2002

By combining in silico and bench molecular biology methods we have identified a novel human gap junction gene that encodes a protein designated HCx31.9. We have determined its human chromosomal location and gene structure, and we have identified a putative mouse ortholog, mCx30.2. We have observed the presence of HCx31.9 in human cerebral cortex, liver, heart, spleen, lung, and kidney and the presence of mCx30.2 in mouse cerebral cortex, liver and lung. Moreover, preliminary data on the electrophysiological properties of HCx31.9 have been obtained by functional expression in paired Xenopus oocytes and in transfected N2A cells.

Patch-Clamp TechniquesIn silicoMolecular Sequence DataClinical BiochemistryXenopuscloningGene ExpressionConnexinConnexinsCell Linegap junctionMiceXenopus laevisGene expressionmedicineAnimalsHumansTissue DistributionAmino Acid SequenceCloning MolecularGenePhylogenybiologycloning; CNS; gap junctionGap junctionGap JunctionsCell BiologyGeneral MedicineTransfectionbiology.organism_classificationMolecular biologymedicine.anatomical_structureCerebral cortexOocytesCNSSequence Alignment
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Activation by Acidic pH of CLC-7 Expressed in Oocytes from Xenopus laevis

2002

ClC chloride channels are important in diverse physiological functions such as transepithelial transport, cell volume regulation, excitability, and acidification of intracellular organelles. We have investigated the expression of CLC-7 in oocytes from Xenopus laevis with the two electrode voltage clamp technique and Western blot analysis. Using a specific antibody against CLC-7, we found an approximately 80 kDa protein in oocytes, previously injected with CLC-7-cRNA. In voltage clamp experiments on ClC-7-cRNA-injected oocytes, no current changes were detected at normal pH (7.4). However, acidification of the Ringer solution to pH values between 6 and 4 revealed strong currents which reverse…

Patch-Clamp TechniquesVoltage clampBlotting WesternBiophysicsXenopusBiologyBiochemistryChlorideXenopus laevisWestern blotChloride ChannelsmedicineAnimalsPatch clampMolecular Biologymedicine.diagnostic_testurogenital systemElectric ConductivityCell BiologyHydrogen-Ion Concentrationbiology.organism_classificationMolecular biologyResting potentialRatsBlotOocytesChloride channelBiophysicsmedicine.drugBiochemical and Biophysical Research Communications
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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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