Search results for "Xenopus"

showing 10 items of 87 documents

Can the introduction of Xenopus laevis affect native amphibian populations? Reduction of reproductive occurrence in presence of the invasive species

2010

Biological invasions are regarded as a form of global change and potential cause of biodiversity loss. Xenopus laevis is an anuran amphibian native to sub-Saharan Africa with strong invasive capacity, especially in geographic regions with a Mediterranean climate. In spite of the worldwide diffusion of X. laevis, the effective impact on local ecosystems and native amphibian populations is poorly quantified. A large population of X. laevis occurs in Sicily and our main aim of this work was to assess the consequences of introduction of this alien species on local amphibian populations. In this study we compare the occurrence of reproduction of native amphibians in ponds with and without X. lae…

Amphibianeducation.field_of_studyEcologybiologyEcologyHyla intermediaPelophylaxPopulationXenopus laeviBiodiversityIntroduced speciesbiology.organism_classificationImpactbiology.animalBiological dispersaleducationBufoSicilyEcology Evolution Behavior and SystematicsBiological Invasions
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Xenopus Oocyte’s Conductance for Bioactive Compounds Screening and Characterization

2019

Background: Astaxanthin (ATX) is a lipophilic compound found in many marine organisms. Studies have shown that ATX has many strong biological properties, including antioxidant, antiviral, anticancer, cardiovascular, anti-inflammatory, neuro-protective and anti-diabetic activities. However, no research has elucidated the effect of ATX on ionic channels. ATX can be extracted from shrimp by-products. Our work aims to characterize ATX cell targets to lend value to marine by-products. Methods: We used the Xenopus oocytes cell model to characterize the pharmacological target of ATX among endogenous Xenopus oocytes&rsquo

AntioxidantSodiummedicine.medical_treatmentXenopuschemistry.chemical_elementEndogeny+Sodium ChannelsCatalysisArticleAmilorideInorganic Chemistrylcsh:ChemistryXenopus laevischemistry.chemical_compoundXenopus oocyte INaAstaxanthinDrug DiscoverymedicineAnimalsPhysical and Theoretical ChemistryMolecular BiologyIC50lcsh:QH301-705.5SpectroscopyXenopus oocyte INa+Biological Productsbioactive compoundsbiologySodium channelOrganic Chemistry<i>Xenopus</i> oocyte INa<sup>+</sup>marine natural productsGeneral Medicinebiology.organism_classificationElectrophysiological PhenomenaComputer Science ApplicationsShrimpastaxanthinchemistryBiochemistrylcsh:Biology (General)lcsh:QD1-999OocytesInternational Journal of Molecular Sciences
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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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Arginine-rich peptides are blockers of VR-1 channels with analgesic activity

2000

Vanilloid receptors (VRs) play a fundamental role in the transduction of peripheral tissue injury and/or inflammation responses. Molecules that antagonize VR channel activity may act as selective and potent analgesics. We report that synthetic arginine-rich hexapeptides block heterologously expressed VR-1 channels with submicromolar efficacy in a weak voltage-dependent manner, consistent with a binding site located near/at the entryway of the aqueous pore. Dynorphins, natural arginine-rich peptides, also blocked VR-1 activity with micromolar affinity. Notably, synthetic and natural arginine-rich peptides attenuated the ocular irritation produced by topical capsaicin application onto the eye…

ArginineReceptors DrugBiophysicsTRPV Cation ChannelsPainDynorphinPharmacologyArginineEyeDynorphinsBiochemistryInhibitory Concentration 50MiceXenopus laevisDynorphinchemistry.chemical_compoundStructural BiologyNon-competitive antagonistGeneticsAnimalsChannel blockerAmino Acid SequenceBinding siteReceptorMolecular BiologyNon-competitive antagonistAnalgesicsChemistryElectric ConductivityNociceptorCell BiologyCapsaicinIonic poreOocytesNociceptorCapsaicinPeptidesFEBS Letters
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A Wnt-specific astacin proteinase controls head formation inHydra

2020

AbstractTheHydrahead organizer acts as a signaling center that initiates and maintains the primary body axis in steady state polyps and during budding or regeneration. Wnt/beta-Catenin signaling functions as a primary cue controlling this process, but how Wnt ligand activity is locally restricted at the protein level is poorly understood.Here we report the identification of an astacin family proteinase as a Wnt processing factor.Hydraastacin-7 (HAS-7) is expressed from gland cells as an apical-distal gradient in the body column, peaking close beneath the tentacle zone.HAS-7siRNA knockdown abrogates HyWnt3 proteolysis in the head tissue and induces a robust double axis phenotype, which is re…

BuddingGene knockdownbiologyChemistryRegeneration (biology)XenopusWnt signaling pathwayLernaean HydraAstacinbiology.organism_classificationActinCell biology
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Interference of L-arginine analogues with L-arginine transport mediated by the y+ carrier hCAT-2B.

1997

The inducible human cationic amino acid transporter hCAT-2B was expressed in Xenopus laevis oocytes, and this system was used to test the effect of several NO synthase (NOS) inhibitors and/or L-arginine analogues on L-arginine transport by this y+ carrier. L-NG-Methyl-L-arginine (L-NMA), asymmetrical L-NG, NG-dimethyl-L-arginine (L-ADMA), L-N5-(1-iminoethyl)-ornithine (L-NIO), L-NG-nitro-L-arginine (L-NNA), and L-NG-nitro-L-arginine methyl ester (L-NAME) all inhibited the inducible NOS II extracted from RAW 264.7 macrophages induced with bacterial lipopolysaccharide. L-NMA, L-ADMA, and L-NIO also competed with L-arginine for transport by hCAT-2B, whereas L-NNA and L-NAME did not. The two L-…

Cancer ResearchArginineLipopolysaccharideMonosaccharide Transport ProteinsPhysiologyStereochemistryClinical BiochemistryNitric Oxide Synthase Type IIArginineBiochemistryCell Linechemistry.chemical_compoundMiceXenopus laevisAnimalsHumansAmino acid transporterEnzyme Inhibitorschemistry.chemical_classificationGlucose Transporter Type 1Arginine transportChemistryLysineCationic polymerizationSubstrate (chemistry)Membrane ProteinsTransporterBiological TransportRatsEnzymeGlucoseBiochemistryOocytesAmino Acid Transport Systems BasicNitric Oxide SynthaseCarrier ProteinsNitric oxide : biology and chemistry
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Identification and characterisation of the dopamine receptor II from the cat flea Ctenocephalides felis (CfDopRII)

2006

International audience; G protein-coupled receptors (GPCRs) represent a protein family with a wide range of functions. Approximately 30% of human drug targets are GPCRs, illustrating their pharmaceutical relevance. In contrast, the knowledge about invertebrate GPCRs is limited and is mainly restricted to model organisms like Drosophila melanogaster and Caenorhabditis elegans. Especially in ectoparasites like ticks and fleas, only few GPCRs are characterised. From the cat flea Ctenocephalides felis, a relevant parasite of cats and dogs, no GPCRs are known so far. Thus, we performed a bioinformatic analysis of available insect GPCR sequences from the honeybee Apis mellifera, the mosquito Anop…

Cat fleaAnopheles gambiaeMolecular Sequence Dataved/biology.organism_classification_rank.speciesBiochemistryCell LineReceptors DopamineAnimals Genetically ModifiedXenopus laevisAnimalsHumansAmino Acid SequenceCloning MolecularModel organismMolecular BiologyPhylogenyCaenorhabditis elegansCtenocephalides[INFO.INFO-BI] Computer Science [cs]/Bioinformatics [q-bio.QM]G protein-coupled receptorGeneticsbiologyved/biologyEcologyFelisComputational Biologybiology.organism_classificationDrosophila melanogasterMultigene FamilyInsect ScienceOocytesInsect ProteinsSiphonapteraFemaleRNA Interference[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]Drosophila melanogasterSequence Alignment[CHIM.CHEM]Chemical Sciences/Cheminformaticshormones hormone substitutes and hormone antagonistsInsect Biochemistry and Molecular Biology
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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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Cellular and Molecular Mechanism of Spinal Cord Regeneration in the Frog Xenopus laevis

2017

EmbryologyMolecular mechanismXenopusBiologybiology.organism_classificationSpinal Cord RegenerationDevelopmental BiologyCell biologyMechanisms of Development
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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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