Search results for "XENOPUS LAEVIS"

showing 10 items of 43 documents

Light-Dependent Translocation of Arrestin in Rod Photoreceptors is Signaled through a Phospholipase C Cascade and Requires ATP

2009

Light adaptation of rod photoreceptors induces translocation of arrestin from inner segments (IS) to outer segments (OS). Our study suggests that components of the G-protein linked phosphoinositide pathway play a role in signaling the initiating events of arrestin translocation. We show that arrestin translocation can be stimulated by activators of phospholipase C (PLC) and protein kinase C (PKC) in the absence of light. Conversely, arrestin translocation to the OS is significantly slowed by inhibitors of PLC and PKC.In the second part of this study, we investigated the mechanism by which arrestin translocates in response to light. Other investigators have suggested that arrestin translocat…

Cholera ToxinLightgenetic structuresG proteinBiophysicsXenopusChromosomal translocationBiologyPhosphatidylinositolsArticleMiceXenopus laevisAdenosine TriphosphateRetinal Rod Photoreceptor CellsArrestinAnimalsEnzyme InhibitorsPotassium CyanideCells CulturedProtein Kinase CProtein kinase CArrestinPhosphoinositide PathwayPhospholipase CChemistryCell Biologybiology.organism_classificationeye diseasesCell biologyRhodopsinType C Phospholipasesbiology.proteinPhosphorylationArrestin beta 2Arrestin beta 1sense organsSignal transductionSignal TransductionBiophysical Journal
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Identification of Cysteine Residues in Human Cationic Amino Acid Transporter hCAT-2A That Are Targets for Inhibition by N-Ethylmaleimide

2013

In most cells, cationic amino acids such as l-arginine, l-lysine, and l-ornithine are transported by cationic (CAT) and y(+)L (y(+)LAT) amino acid transporters. In human erythrocytes, the cysteine-modifying agent N-ethylmaleimide (NEM) has been shown to inhibit system y(+) (most likely CAT-1), but not system y(+)L (Devés, R., Angelo, S., and Chávez, P. (1993) J. Physiol. 468, 753-766). We thus wondered if sensitivity to NEM distinguishes generally all CAT and y(+)LAT isoforms. Transport assays in Xenopus laevis oocytes established that indeed all human CATs (including the low affinity hCAT-2A), but neither y(+)LAT isoform, are inhibited by NEM. hCAT-2A inhibition was not due to reduced tran…

Gene isoformMutantMutation MissenseXenopusBiologyBiochemistryXenopus laevischemistry.chemical_compoundMembrane BiologyAnimalsHumansheterocyclic compoundsCysteineAmino acid transporterEnzyme InhibitorsMolecular Biologychemistry.chemical_classificationN-EthylmaleimideTransporterCell Biologybiology.organism_classificationMolecular biologyProtein Structure TertiaryAmino acidAmino Acid SubstitutionchemistryBiochemistryEthylmaleimideOocytesAmino Acid Transport Systems BasicCysteineJournal of Biological Chemistry
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The Xenopus Oocyte as an Ectopic Expression System for the Selection of Protein Isoform-Specific Antibodies

1993

A panel of Xenopus oocytes, each injected with cRNA coding for one specific isoform of the rat brain RCK family of voltage gated potassium channel proteins, was employed to screen for isoform-specific monoclonal antibodies. Several days after injection, cryosections of embedded oocytes were produced and were employed in immunohistochemical analysis of antibody binding. Of the advantageous properties of the assay, it employs the native antigen, it can be applied to homooligomeric and heterooligomeric proteins, and cryosections of the same batch can be stored frozen for later tests. The method may be advantageous also for the selection of isoform-specific antibodies of other protein families.

Gene isoformProtein isoformPotassium ChannelsProtein familymedicine.drug_classRecombinant Fusion ProteinsXenopusNerve Tissue ProteinsBiologyMonoclonal antibodyEpitopeMiceXenopus laevisAntigenAntibody SpecificitymedicineAnimalsPharmacologyMice Inbred BALB CHybridomasAntibodies Monoclonalbiology.organism_classificationMolecular biologyOocytesFemaleEctopic expressionJournal of Receptor Research
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Mutations in SLC20A2 link familial idiopathic basal ganglia calcification with phosphate homeostasis.

2012

Familial idiopathic basal ganglia calcification (IBGC) is a genetic condition with a wide spectrum of neuropsychiatric symptoms, including parkinsonism and dementia. Here, we identified mutations in SLC20A2, encoding the type III sodium-dependent phosphate transporter 2 (PiT2), in IBGC-affected families of varied ancestry, and we observed significantly impaired phosphate transport activity for all assayed PiT2 mutants in Xenopus laevis oocytes. Our results implicate altered phosphate homeostasis in the etiology of IBGC.

Genetic Markersmedicine.medical_specialtyGenetic LinkageMolecular Sequence DataMutation MissenseXenopusBasal ganglia calcification610 Medicine & healthPhosphates10052 Institute of PhysiologyXenopus laevis03 medical and health scienceschemistry.chemical_compound0302 clinical medicineAsian PeopleBasal Ganglia Diseases1311 GeneticsCalcinosisGenetic linkageInternal medicineGeneticsmedicineAnimalsHomeostasisHumansBasal ganglia disease030304 developmental biology0303 health sciencesBase SequencebiologySodium-Phosphate Cotransporter Proteins Type IIIParkinsonismCalcinosisSequence Analysis DNAmedicine.diseasePhosphatebiology.organism_classificationPedigreeEndocrinologychemistry10076 Center for Integrative Human PhysiologyOocytes570 Life sciences; biologyLod Score030217 neurology & neurosurgeryHomeostasisChromosomes Human Pair 8Nature genetics
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Galloway-Mowat syndrome: New insights from bioinformatics and expression during Xenopus embryogenesis.

2021

Abstract Galloway-Mowat syndrome (GAMOS) is a rare developmental disease. Patients suffer from congenital brain anomalies combined with renal abnormalities often resulting in an early-onset steroid-resistant nephrotic syndrome. The etiology of GAMOS has a heterogeneous genetic contribution. Mutations in more than 10 different genes have been reported in GAMOS patients. Among these are mutations in four genes encoding members of the human KEOPS ( k inase, e ndopeptidase and o ther p roteins of small s ize) complex, including OSGEP, TP53RK, TPRKB and LAGE3. Until now, these components have been functionally mainly investigated in bacteria, eukarya and archaea and in humans in the context of t…

GeneticsIn silicoEmbryogenesisXenopusComputational BiologyEmbryonic DevelopmentContext (language use)In situ hybridizationBiologyXenopus Proteinsmedicine.diseasebiology.organism_classificationGalloway Mowat syndromePronephrosXenopus laevisHernia HiatalGeneticsmedicineMicrocephalyAnimalsHumansNephrosisMolecular BiologyGeneDevelopmental BiologyGene expression patterns : GEP
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Excretion and metabolism of phenol, 4-nitrophenol and 2-methylphenol by the frogs Rana temporaria and Xenopus laevis.

1987

1. Rana and Xenopus excrete 90-95% dose, and metabolize 50-65% dose of phenol, 4-nitrophenol and 2-methylphenol within 24 h, to about the same extent. 2. Kinetic data for the excretion of phenols from both species fit a two-compartment model. The elimination constants of Rana and Xenopus are not significantly different. 3. Metabolism is mostly conjugation by glucuronidation and sulphation of the original phenols. Additionally, oxidations leading to dihydroxyphenols and benzoic acid from 2-methylphenol, and reduction of 4-nitrophenol occur, followed by conjugation. 4. There is an important difference between the metabolite patterns of Rana and Xenopus in that the latter is unable to glucuron…

Health Toxicology and MutagenesisMetaboliteRana temporariaXenopusGlucuronidationBiologyToxicologyBiochemistryRanaNitrophenolschemistry.chemical_compoundCresolsXenopus laevisSulfationPhenolsAnimalsPhenolsBiotransformationChromatography High Pressure LiquidBenzoic acidPharmacologyGeneral MedicineMetabolismbiology.organism_classificationBiochemistrychemistryXenobiotica; the fate of foreign compounds in biological systems
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A chimera carrying the functional domain of the orphan protein SLC7A14 in the backbone of SLC7A2 mediates trans-stimulated arginine transport.

2012

In human skin fibroblasts, a lysosomal transport system specific for cationic amino acids has been described and named system c. We asked if SLC7A14 (solute carrier family 7 member A14), an orphan protein assigned to the SLC7 subfamily of cationic amino acid transporters (CATs) due to sequence homology, may represent system c. Fusion proteins between SLC7A14 and enhanced GFP localized to intracellular vesicles, co-staining with the lysosomal marker LysoTracker(®). To perform transport studies, we first tried to redirect SLC7A14 to the plasma membrane (by mutating putative lysosomal targeting motifs) but without success. We then created a chimera carrying the backbone of human (h) CAT-2 and …

Lysosomal transportArginineRecombinant Fusion ProteinsProtein domainBiological Transport ActiveBiologyArginineBiochemistryCell LineXenopus laevisMembrane BiologyAnimalsHumansMolecular BiologySkinchemistry.chemical_classificationArginine transportCell BiologyMembrane transportFibroblastsHydrogen-Ion ConcentrationFusion proteinSolute carrier familyAmino acidProtein Structure TertiaryBiochemistrychemistryAmino Acid Transport Systems BasicLysosomesThe Journal of biological chemistry
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Specific expression of olfactory binding protein in the aerial olfactory cavity of adult and developing Xenopus

2005

International audience

METAMORPHOSISXENOPUS TROPICALISXENOPUS LAEVISOLFACTION[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC][SDV.NEU] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]ComputingMilieux_MISCELLANEOUSODORANT-BINDING PROTEINOLFACTORY BINDING PROTEIN
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Cellular composition and organization of the spinal cord central canal during metamorphosis of the frogXenopus laevis

2017

Studying the cellular composition and morphological changes of cells lining the central canal during Xenopus laevis metamorphosis could contribute to understand postnatal development and spinal cord regeneration. Here we report the analysis of central canal cells at different stages during metamorphosis using immunofluorescence for protein markers expression, transmission and scanning electron microscopy and cell proliferation assays. The central canal was regionalized according to expression of glial markers, ultrastructure, and proliferation in dorsal, lateral, and ventral domains with differences between larvae and froglets. In regenerative larvae, all cell types were uniciliated, have a…

Male0301 basic medicineCell typeEpendymal Cellmedia_common.quotation_subjectXenopusCell CountBiologyXenopus laevis03 medical and health sciencesNeural Stem CellsmedicineAnimalsCiliaMetamorphosisSpinal Cord RegenerationCell Proliferationmedia_commonGeneral NeuroscienceMetamorphosis BiologicalSpinal cordbiology.organism_classificationDeoxyuridineNerve RegenerationCell biologyChromatin030104 developmental biologymedicine.anatomical_structureSpinal CordLarvaUltrastructureFemalesense organsNeurogliaJournal of Comparative Neurology
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Deficient membrane integration of the novel p.N14D-GJB2mutant associated with non-syndromic hearing impairment

2006

Mutations in GJB2, the gene encoding for the Gap Junction protein Connexin 26 (Cx26), have been established as the major cause of hereditary, non-syndromic hearing impairment (HI). We report here the identification of a novel point mutation in GJB2, c.40A>G [p.N14D], detected in compound heterozygosity with the c.35delG mutation in two brothers with moderate non-syndromic sensorineural HI. The mother who carried one wildtype and a p.N14D allele displayed normal hearing. The mutation leads to substitution of the neutral amino acid asparagine (N) by the negatively charged aspartic acid (D) at amino acid number 14, a position that is conserved among Cx26 of different organisms and among many o…

MaleDNA Mutational AnalysisMutantGene ExpressionConnexinIn Vitro TechniquesBiologymedicine.disease_causeCompound heterozygosityConnexinsXenopus laevisAspartic acidotorhinolaryngologic diseasesGeneticsmedicineAnimalsHumansCloning MolecularChildHearing LossGenetics (clinical)chemistry.chemical_classificationMutationPoint mutationCell MembraneWild typeGap JunctionsMolecular biologyPedigreeAmino acidConnexin 26Protein TransportchemistryChild PreschoolAntigens SurfaceMutationOocytesHuman Mutation
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