Search results for "G-protein"

showing 10 items of 118 documents

Cloning of a novel putative G-protein-coupled receptor (NLR) which is expressed in neuronal and lymphatic tissue.

1993

AbstractA novel G-protein-coupled receptor was isolated from mouse and rat neuronal and lymphatic tissues. The amino acid sequence of the rat receptor (rNLR) shows an overall homology of 80% to a recently cloned receptor from Burkitt's lymphoma cells (BLR1) which is exclusively expressed in lymphatic tissues [(1992) Eur. J. Immunol. 22, 2795]. Much less homology between rNLR and BLR1 was observed at the N-terminus (about 40%), whereas rNLR and the mouse homologue mNLR show 92% amino acid identity. Northern blot analysis of NLR revealed a predominant 5.5 kb mRNA species in various brain regions and neuronal cell lines, whereas in the spleen a 3 kb transcript is predominant. This distribution…

Restriction MappingInterleukin 8BiochemistryReceptors G-Protein-CoupledMiceStructural BiologyTumor Cells CulturedLymphocytesCloning MolecularReceptorPeptide sequencechemistry.chemical_classificationNeuronsGenomic LibraryBurkitt's lymphomaBrainBurkitt LymphomaPolymerase chain reactionAmino acidOligodeoxyribonucleotidesOrgan SpecificityG-protein-coupled receptorBLR1Molecular Sequence DataBiophysicsReceptors Cell SurfaceBiologyNLRGTP-Binding ProteinsComplementary DNAGeneticsmedicineAnimalsHumansNorthern blotAmino Acid SequenceRNA MessengerMolecular BiologyG protein-coupled receptorMessenger RNABase SequenceSequence Homology Amino AcidCell Biologymedicine.diseaseMolecular biologyIntronsRatsNG108-15 cellchemistryBurkitt's lymphomaFEBS letters
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Scaffold protein harmonin (USH1C) provides molecular links between Usher syndrome type 1 and type 2.

2005

Contains fulltext : 48386.pdf (Publisher’s version ) (Closed access) Usher syndrome (USH) is the most frequent cause of combined deaf-blindness in man. USH is clinically and genetically heterogeneous with at least 11 chromosomal loci assigned to the three USH types (USH1A-G, USH2A-C, USH3A). Although the different USH types exhibit almost the same phenotype in human, the identified USH genes encode for proteins which belong to very different protein classes and families. We and others recently reported that the scaffold protein harmonin (USH1C-gene product) integrates all identified USH1 molecules in a USH1-protein network. Here, we investigated the relationship between the USH2 molecules a…

Scaffold proteinGenetics and epigenetic pathways of disease [NCMLS 6]Usher syndromeStereocilia (inner ear)Cell Cycle ProteinsBiologyInteractomeReceptors G-Protein-CoupledMiceotorhinolaryngologic diseasesGeneticsmedicineAnimalsNeurosensory disorders [UMCN 3.3]Photoreceptor CellsRats WistarMolecular BiologyGeneGenetics (clinical)Renal disorder [IGMD 9]GeneticsExtracellular Matrix ProteinsStereociliumBinding SitesHair Cells Auditory InnerSodium-Bicarbonate SymportersUsher Syndrome Type 1General Medicinemedicine.diseasePhenotypeRatsMice Inbred C57BLCytoskeletal ProteinsCarrier ProteinsUsher Syndromes
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A novel Usher protein network at the periciliary reloading point between molecular transport machineries in vertebrate photoreceptor cells.

2008

Contains fulltext : 69178.pdf (Publisher’s version ) (Closed access) The human Usher syndrome (USH) is the most frequent cause of combined deaf-blindness. USH is genetically heterogeneous with at least 12 chromosomal loci assigned to three clinical types, USH1-3. Although these USH types exhibit similar phenotypes in human, the corresponding gene products belong to very different protein classes and families. The scaffold protein harmonin (USH1C) was shown to integrate all identified USH1 and USH2 molecules into protein networks. Here, we analyzed a protein network organized in the absence of harmonin by the scaffold proteins SANS (USH1G) and whirlin (USH2D). Immunoelectron microscopic anal…

Scaffold proteinGenetics and epigenetic pathways of disease [NCMLS 6]XenopusCell Cycle ProteinsNerve Tissue ProteinsBiologyIn Vitro TechniquesNeuroinformatics [DCN 3]TransfectionModels BiologicalReceptors G-Protein-CoupledMiceChlorocebus aethiopsProtein Interaction MappingGeneticsPerception and Action [DCN 1]otorhinolaryngologic diseasesAnimalsHumansNeurosensory disorders [UMCN 3.3]Cell Cycle ProteinMicroscopy ImmunoelectronMolecular BiologyIntegral membrane proteinGenetics (clinical)Adaptor Proteins Signal TransducingRenal disorder [IGMD 9]GeneticsMice KnockoutExtracellular Matrix ProteinsCiliumSignal transducing adaptor proteinMembrane ProteinsGeneral MedicineTransmembrane proteinCell biologyMice Inbred C57BLCytoskeletal ProteinsEctodomainGenetic defects of metabolism [UMCN 5.1]COS CellsNIH 3T3 CellsCervical collarUsher SyndromesFunctional Neurogenomics [DCN 2]Photoreceptor Cells VertebrateSubcellular FractionsImmunity infection and tissue repair [NCMLS 1]
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Novel scaffold of natural compound eliciting sweet taste revealed by machine learning

2020

Abstract Sugar replacement is still an active issue in the food industry. The use of structure-taste relationships remains one of the most rational strategy to expand the chemical space associated to sweet taste. A new machine learning model has been setup based on an update of the SweetenersDB and on open-source molecular features. It has been implemented on a freely accessible webserver. Cellular functional assays show that the sweet taste receptor is activated in vitro by a new scaffold of natural compounds identified by the in silico protocol. The newly identified sweetener belongs to the lignan chemical family and opens a new chemical space to explore.

ScaffoldsweetenerComputer scienceIn silicoMachine learningcomputer.software_genre01 natural sciencesAnalytical ChemistryReceptors G-Protein-Coupled0404 agricultural biotechnologysweet tastenatural compoundsHumans[CHIM]Chemical Sciences[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biologysweet taste receptor2. Zero hungerbusiness.industryNatural compound010401 analytical chemistrydigestive oral and skin physiologySweet taste04 agricultural and veterinary sciencesGeneral Medicine040401 food scienceChemical space0104 chemical sciences[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistrymachine learningSweetening AgentsTasteArtificial intelligencebusinesscomputer[CHIM.CHEM]Chemical Sciences/CheminformaticsFood Science
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Recombinant expression, in vitro refolding, and biophysical characterization of the N-terminal domain of T1R3 taste receptor

2012

Facteur d'impact (5 ans) : 1,617Notoriété à 2 ans : Acceptable (biochem.res.methods); The sweet taste receptor is a heterodimeric receptor composed of the T1R2 and T1R3 subunits, while T1R1 and T1R3 assemble to form the umami taste receptor. T1R receptors belong to the family of class C G-protein coupled receptors (GPCRs). In addition to a transmembrane heptahelical domain, class C GPCRs have a large extracellular N-terminal domain (NTD), which is the primary ligand-binding site. The T1R2 and T1R1 subunits have been shown to be responsible for ligand binding, via their NTDs. However, little is known about the contribution of T1R3-NTD to receptor functions. To enable biophysical characteriza…

TASTE RECEPTORSucroseCircular dichroismcongenital hereditary and neonatal diseases and abnormalitiesProtein Conformation[ SDV.AEN ] Life Sciences [q-bio]/Food and Nutritionumami receptorUmamiSWEETENERmedicine.disease_causeReceptors G-Protein-Coupledtaste03 medical and health sciencesGPCRTaste receptorPROTEIN REFOLDINGexpressionEscherichia colimedicineHumansRECOMBINANT GPCRbacteriaReceptorEscherichia coli030304 developmental biologyG protein-coupled receptorInclusion Bodies0303 health sciencesChemistrysweet receptor030302 biochemistry & molecular biologyRecombinant ProteinsTransmembrane proteinnervous system diseasesResearch NoteBACTERIAL EXPRESSIONBiochemistrysugarElectrophoresis Polyacrylamide GelHeterologous expression[SDV.AEN]Life Sciences [q-bio]/Food and Nutritionrecombinant proteinProtein BindingBiotechnology
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Hypoxia Positively Regulates the Expression of pH-Sensing G-Protein–Coupled Receptor OGR1 (GPR68)

2016

Background & Aims: A novel family of proton-sensing G-proteinâcoupled receptors, including ovarian cancer G-proteinâcoupled receptor 1 (OGR1) (GPR68) has been identified to play a role in pH homeostasis. Hypoxia is known to change tissue pH as a result of anaerobic glucose metabolism through the stabilization of hypoxia-inducible factor-1α. We investigated how hypoxia regulates the expression of OGR1 in the intestinal mucosa and associated cells. Methods: OGR1 expression in murine tumors, human colonic tissue, and myeloid cells was determined by quantitative reverse-transcription polymerase chain reaction. The influence of hypoxia on OGR1 expression was studied in monocytes/macrophages and…

WT wild type0301 basic medicineMM6 MonoMac 6HV healthy volunteerSPARC secreted protein acidic and rich in cysteineNF-κB nuclear factor-κBInflammationBiologyIEC intestinal epithelial cell03 medical and health sciencesIntestinal mucosaTDAG8Ovarian Cancer G-Protein–Coupled ReceptormedicineOGR1 ovarian cancer G-protein–coupled receptor 1 (GPR68)IFN interferonlcsh:RC799-869ReceptorOriginal ResearchTh T-helperInflammationTNF tumor necrosis factorIBD inflammatory bowel diseaseHepatologyRT-qPCR quantitative reverse-transcription polymerase chain reactionAICAR 5-aminoimidazole-4-carboxamide-1-β-4-ribofuranosideTDAG8 T-cell death-associated gene 8 (GPR65)Inflammatory Bowel DiseaseGRP65GastroenterologyHypoxia (medical)Molecular biologyGPR G-protein–coupled receptormRNA messenger RNAIL interleukinChIP chromatin immunoprecipitationHIF hypoxia-inducible factorUC ulcerative colitis030104 developmental biologyHypoxia-inducible factorsCancer researchCD Crohn's diseaselcsh:Diseases of the digestive system. GastroenterologyTumor necrosis factor alphaFCS fetal calf serummedicine.symptomChromatin immunoprecipitationHomeostasisCellular and Molecular Gastroenterology and Hepatology
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Mosaic activating mutations in GNA11 and GNAQ are associated with phakomatosis pigmentovascularis and extensive dermal melanocytosis

2016

Common birthmarks can be an indicator of underlying genetic disease but are often overlooked. Mongolian blue spots (dermal melanocytosis) are usually localized and transient, but they can be extensive, permanent, and associated with extracutaneous abnormalities. Co-occurrence with vascular birthmarks defines a subtype of phakomatosis pigmentovascularis, a group of syndromes associated with neurovascular, ophthalmological, overgrowth, and malignant complications. Here, we discover that extensive dermal melanocytosis and phakomatosis pigmentovascularis are associated with activating mutations in GNA11 and GNAQ, genes that encode Gα subunits of heterotrimeric G proteins. The mutations were det…

WT wild typeDNA Mutational AnalysisMolecular Sequence Datapostzygotic mutationsMutation MissenseSWS Sturge-Weber syndromeDermatologycesioflammeagermlineBiochemistrySkin DiseasesAnimals Genetically Modifiedg-proteinDNA deoxyribonucleic acidMongolian Spotoculodermal melanocytosis[ SDV.MHEP ] Life Sciences [q-bio]/Human health and pathologyGeneticsAnimalsHumansddc:610Phosphorylationchoroidal melanomaMolecular BiologyAllelesZebrafishdiseaseBase SequenceNeurocutaneous Syndromessturge-weberInfantCell Biologymongolian spotPPV phakomatosis pigmentovascularisGTP-Binding Protein alpha SubunitsHEK293 CellsPhenotypeMutationGTP-Binding Protein alpha Subunits Gq-G11Original Articleuveal melanoma[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologySignal Transduction
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Plexin-B1 activates NF-κB and IL-8 to promote a pro-angiogenic response in endothelial cells.

2011

Background The semaphorins and their receptors, the plexins, are proteins related to c-Met and the scatter factors that have been implicated in an expanding signal transduction network involving co-receptors, RhoA and Ras activation and deactivation, and phosphorylation events. Our previous work has demonstrated that Semaphorin 4D (Sema4D) acts through its receptor, Plexin-B1, on endothelial cells to promote angiogenesis in a RhoA and Akt-dependent manner. Since NF-κB has been linked to promotion of angiogenesis and can be activated by Akt in some contexts, we wanted to examine NF-κB in Sema4D treated cells to determine if there was biological significance for the pro-angiogenic phenotype o…

animal structuresRHOAProto-Oncogene Proteins c-aktAngiogenesisSignaling in cellular processesG-protein signalingCancer TreatmentSEMA4Dlcsh:MedicineSignal transductionBiology03 medical and health sciencesMolecular cell biology0302 clinical medicineSemaphorinSettore BIO/10 - BiochimicaAkt Signaling CascadeMembrane Receptor SignalingInterleukin 8lcsh:ScienceBiologyProtein kinase BGTPase signalingRas signaling030304 developmental biology0303 health sciencesMultidisciplinaryMechanisms of Signal Transductionlcsh:RSignaling Cascades3. Good healthCell biologyPlexin B1RNA interferencepro-angiogenicendothelial cellsOncology030220 oncology & carcinogenesisembryonic structuresCancer researchbiology.proteinMedicinelcsh:QAntiangiogenesis TherapyAntiapoptotic signalingSignal transductionResearch ArticlePLoS ONE
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The hedgehog receptor patched is involved in cholesterol transport.

2011

International audience; BACKGROUND: Sonic hedgehog (Shh) signaling plays a crucial role in growth and patterning during embryonic development, and also in stem cell maintenance and tissue regeneration in adults. Aberrant Shh pathway activation is involved in the development of many tumors, and one of the most affected Shh signaling steps found in these tumors is the regulation of the signaling receptor Smoothened by the Shh receptor Patched. In the present work, we investigated Patched activity and the mechanism by which Patched inhibits Smoothened. METHODOLOGY/PRINCIPAL FINDINGS: Using the well-known Shh-responding cell line of mouse fibroblasts NIH 3T3, we first observed that enhancement …

ciliumlcsh:MedicineyeastBiochemistryReceptors G-Protein-CoupledTransmembrane Transport ProteinsMicechemistry.chemical_compound0302 clinical medicineMolecular Cell Biology[SDV.IDA]Life Sciences [q-bio]/Food engineeringMembrane Receptor SignalingBiomacromolecule-Ligand InteractionsSonic hedgehoglcsh:ScienceComputingMilieux_MISCELLANEOUS0303 health sciencesMultidisciplinaryMechanisms of Signal TransductionVeratrum Alkaloids[SDV.IDA] Life Sciences [q-bio]/Food engineeringdrosophilaSmoothened ReceptorLipidsHedgehog signaling pathwayCell biologySterolsSmoothened ReceptorAlimentation et Nutritionembryonic structurescilMembranes and Sorting[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]Signal transductionvesicular traffickingSignal TransductionResearch Articleprimary ciliumPatched ReceptorsPatchedsignal-transductionanimal structuresCyclopamine[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process EngineeringBiophysicsReceptors Cell Surfacepathway activationSaccharomyces cerevisiaetransduction du signalBiology03 medical and health sciencessonic hedgehoglipidAnimalsHumansFood and NutritionHedgehog Proteins[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringBiology030304 developmental biologyPatched Receptorsprotein signalsCell Membranelcsh:RProteinscholesterolBiological TransportTransmembrane Proteinssterol-sensing domainchemistry[ SDV.NEU ] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]NIH 3T3 Cellscholesterol;lipid;cell trafficking; yeast;drosophila;cells ; pathway activation; vesicular trafficking; signal-transduction; sonic hedgehog;sterol-sensing domain; primary cilium;protein signalsbiology.proteincellslcsh:Qcell traffickingSmoothened030217 neurology & neurosurgery
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Light-dependent CK2-mediated phosphorylation of centrins regulates complex formation with visual G-protein.

2008

AbstractCentrins are Ca2+-binding EF-hand proteins. All four known centrin isoforms are expressed in the ciliary apparatus of photoreceptor cells. Cen1p and Cen2p bind to the visual G-protein transducin in a strictly Ca2+-dependent way, which is thought to regulate light driven movements of transducin between photoreceptor cell compartments. These relatively slow motile processes represent a novel paradigm in light adaptation of photoreceptor cells.Here we validated specific phosphorylation as a novel regulator of centrins in photoreceptors. Centrins were differentially phosphorylated during photoreceptor dark adaptation. Inhibitor treatments revealed protein kinase CK2 as the major protein…

genetic structuresLightG proteinVisionChromosomal Proteins Non-HistoneBlotting WesternDark AdaptationBiologySignal transductionMicrotubulesPhotoreceptor cellMass SpectrometryCa2+-binding proteinsSubstrate SpecificityRats Sprague-DawleyMiceHeterotrimeric G proteinmedicineAnimalsCiliaTransducinPhosphorylationProtein kinase ACasein Kinase IIFluorescent Antibody Technique IndirectMicroscopy ImmunoelectronMolecular BiologyCytoskeletonCiliumCalcium-Binding ProteinsCell BiologyCell biologyRatsMice Inbred C57BLmedicine.anatomical_structureCentrinPhosphorylationHeterotrimeric G-proteinCalciumCattleTransducinsense organsMolecular translocationPhotoreceptor Cells VertebrateProtein BindingBiochimica et biophysica acta
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