Search results for "ligand"

showing 10 items of 2559 documents

Agonist-induced formation of FGFR1 homodimers and signaling differ among members of the FGF family

2011

Fibroblast growth factor receptor 1 (FGFR1) is known to be activated by homodimerization in the presence of both the FGF agonist ligand and heparan sulfate glycosaminoglycan. FGFR1 homodimers in turn trigger a variety of downstream signaling cascades via autophosphorylation of tyrosine residues in the cytoplasmic domain of FGFR1. By means of Bioluminescence Energy Resonance Transfer (BRET) as a sign of FGFR1 homodimerization, we evaluated in HEK293T cells the effects of all known FGF agonist ligands on homodimer formation. A significant correlation between BRET(2) signaling and ERK1/2 phosphorylation was observed, leading to a further characterization of the binding and signaling properties…

AgonistMAPK/ERK pathwaymedicine.drug_classBiophysicsSettore BIO/11 - Biologia MolecolareBiologyLigandsFibroblast growth factorSettore BIO/09 - FisiologiaBiochemistrychemistry.chemical_compoundFluorescence Resonance Energy TransfermedicineHumansReceptor Fibroblast Growth Factor Type 1Molecular BiologyMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Fibroblast growth factor receptor 1HEK 293 cellsAutophosphorylationCell BiologyHeparan sulfateFibroblast growth factors FGFR1 Homodimerization BRET MAPKCell biologyFibroblast Growth Factorsstomatognathic diseasesHEK293 CellschemistrySettore BIO/14 - FarmacologiaPhosphorylationHeparitin SulfateProtein MultimerizationBiochemical and Biophysical Research Communications
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Actions of two GABAA receptor benzodiazepine-site ligands that are mediated via non-γ2-dependent modulation.

2011

The potent sedative-hypnotic zolpidem and the convulsant methyl-6,7-dimethoxy-4-ethyl-β-carboline-3-carboxylate (DMCM) act primarily by binding to the benzodiazepine site of the main inhibitory neurotransmitter receptor, the pentameric γ-aminobutyric acid type A receptor (GABA(A)). This binding depends critically on the wild-type F77 residue of the GABA(A) receptor γ2 subunit. Mice with γ2 subunit F77I point mutation (γ2I77 mouse line) lose the high-affinity nanomolar binding of these ligands as well as their most robust behavioral actions at low doses. Interestingly, the γ2I77 mice offer a tool to study the actions of these substances mediated via other possible binding sites of the GABA(A…

AgonistMaleZolpidemAzidesmedicine.drug_classPyridinesConvulsantsPharmacologyLigandsGABAA-rho receptor03 medical and health scienceschemistry.chemical_compoundBenzodiazepinesMice0302 clinical medicineDMCMmedicineAnimalsHumansHypnotics and SedativesBinding site030304 developmental biologyPharmacology0303 health sciencesBenzodiazepineBinding SitesBehavior AnimalGABAA receptorBrainLigand (biochemistry)Receptors GABA-AMice Inbred C57BLZolpidemProtein SubunitsHEK293 CellschemistryAutoradiographyFemale030217 neurology & neurosurgerymedicine.drugCarbolinesProtein BindingEuropean journal of pharmacology
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Coupling between agonist and chloride ionophore sites of the GABA(A) receptor: agonist/antagonist efficacy of 4-PIOL.

2000

Eight gamma-aminobutyric acid (GABA) mimetics were tested on their ability to differentiate native GABA(A) receptor subtypes present in various rat brain regions. In rat brain cryostat sections, little regional variations by the agonistic actions of muscimol, thiomuscimol, 4,5,6,7-tetrahydroisoazolo(5,4-c)pyridin-3-ol, piperidine-4-sulphonic acid, taurine and beta-alanine on [35S]t-butylbicyclophosphorothionate ([35S]TBPS) binding to GABA(A) receptor channels were found. They were very similar to those found for GABA itself and indicated no direct correlation with single subunit distributions for any of these compounds. Only the low-efficacy GABA mimetic 5-(4-piperidyl)isoxazol-3-ol (4-PIOL…

AgonistMalemedicine.medical_specialtyAgonist-antagonistmedicine.drug_classBiologyLigandsPartial agonistGABAA-rho receptorCell Linechemistry.chemical_compoundPiperidinesInternal medicinemedicineAnimalsHumansRats WistarReceptorGABA AgonistsPharmacologyIonophoresGABAA receptorBrainIsoxazolesBridged Bicyclo Compounds HeterocyclicReceptors GABA-ARatsEndocrinologyMuscimolchemistryThiomuscimolEuropean journal of pharmacology
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Exploring kainate receptor pharmacology using molecular dynamics simulations.

2010

Ionotropic glutamate receptors (iGluRs) are enticing targets for pharmaceutical research; however, the search for selective ligands is a laborious experimental process. Here we introduce a purely computational procedure as an approach to evaluate ligand–iGluR pharmacology. The ligands are docked into the closed ligand-binding domain and during the molecular dynamics (MD) simulation the bi-lobed interface either opens (partial agonist/antagonist) or stays closed (agonist) according to the properties of the ligand. The procedure is tested with closely related set of analogs of the marine toxin dysiherbaine bound to GluK1 kainate receptor. The modeling is set against the abundant binding data …

AgonistModels Molecularmedicine.drug_classProtein ConformationIn silicoKainate receptorPharmacologyMolecular Dynamics SimulationLigandsPartial agonistArticleTurn (biochemistry)Cellular and Molecular NeuroscienceStructure-Activity RelationshipReceptors Kainic AcidmedicineStructure–activity relationshipPharmacologyAlanineMolecular StructureChemistryBridged Bicyclo Compounds HeterocyclicIonotropic glutamate receptorMarine ToxinsMarine toxinProtein BindingNeuropharmacology
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Structural Mechanism of N-Methyl-D-Aspartate Receptor Type 1 Partial Agonism

2012

N-methyl-D-aspartate (NMDA) receptors belong to a family of ionotropic glutamate receptors that contribute to the signal transmission in the central nervous system. NMDA receptors are heterotetramers that usually consist of two GluN1 and GluN2 monomers. The extracellular ligand-binding domain (LBD) of a monomer is comprised of discontinuous segments that form the functional domains D1 and D2. While the binding of a full agonist glycine to LBD of GluN1 is linked to cleft closure and subsequent ion-channel opening, partial agonists are known to activate the receptor only sub-maximally. Although the crystal structures of the LBD of related GluA2 receptor explain the mechanism for the partial a…

AgonistProtein Structuremedicine.drug_classGlycineMolecular ConformationBiophysicslcsh:MedicineMolecular Dynamics SimulationLigandsta3111Receptors N-Methyl-D-AspartateBiochemistryBiophysics Simulationsta3112Partial agonistIon ChannelsChemical BiologyMacromolecular Structure AnalysismedicineBiomacromolecule-Ligand Interactionslcsh:ScienceReceptorBiologyta116Ion channelCrystallographyMultidisciplinaryChemistrylcsh:Rta1182Glutamate receptorProteinsComputational BiologyNeurotransmittersProtein Structure TertiaryTransmembrane ProteinsBiochemistryCycloserineBiophysicsNMDA receptorLigand-gated ion channellcsh:Qhormones hormone substitutes and hormone antagonistsProtein BindingResearch ArticleNeuroscienceIonotropic effectPLoS ONE
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Homodimeric murine interleukin-3 agonists indicate that ligand dimerization is important for high-affinity receptor complex formation.

1994

Homodimeric murine interleukin 3 (mIL-3) agonists were generated by intermolecular cystine-bonding. Steady-state binding assays and association kinetics performed at 4 degrees C using these agonists revealed specific binding to both the high- and low-affinity receptor. DSS-mediated crosslinking studies performed at 4 degrees C with agonist concentrations compatible with high-affinity receptor complex formation allowed to detect protein complexes of the alpha chain, the beta chain(s) and the high-affinity receptor complex migrating with apparent molecular weights of 90 kDa, 140 kDa, and above 180 kDa, respectively. In contrast, monomeric mIL-3 was crosslinked to the alpha chain receptor only…

AgonistReceptor complexmedicine.drug_classMacromolecular SubstancesClinical BiochemistryInterleukin-17 receptorLigandsProtein Structure SecondaryCell LineMiceEndocrinologymedicineAnimalsReceptorProtease-activated receptor 2Interleukin 3Cell Line TransformedMolecular massChemistryGranulocyte-Macrophage Colony-Stimulating FactorCell BiologyLigand (biochemistry)Receptors Interleukin-3Recombinant ProteinsKineticsBiochemistryCystineBiological AssayElectrophoresis Polyacrylamide GelInterleukin-3Interleukin-5Cell DivisionThymidineGrowth factors (Chur, Switzerland)
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Selection and characterization of a novel agonistic human recombinant anti-Trail-R2 minibody with anti-leukemic activity

2009

Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is a promising natural anticancer therapeutic agent because through its “death receptors”, TRAIL-R1 and TRAIL-R2, it induces apoptosis in many transformed tumor cells, but not in the majority of normal cells. Hence, agonistic compounds directed against TRAIL death receptors have the potential of being excellent cancer therapeutic agents, with minimal cytotoxicity in normal tissues. Here, we report the selection and characterization of a new single-chain fragment variable (scFv) to TRAIL-R2 receptor isolated from a human phage-display library, produced as minibody (MB), and characterized for the in vitro anti-leukemic tumoricid…

Agonistmedicine.drug_classTRAIL; TRAIL-R2; minibody; anticancer therapyImmunologylymphoma; therapy; recombinant antibodyTRAILApoptosislymphomaCHO CellsCricetulusPeptide LibraryTRAIL-R2CricetinaeImmunoglobulin FragmentmedicineAnimalsHumansImmunology and Allergyrecombinant antibodyanticancer therapyReceptorCytotoxicityImmunoglobulin FragmentsPharmacologytherapyLeukemiaChemistryAnimalChinese hamster ovary cellAntibody-Dependent Cell CytotoxicityminibodyApoptosiIn vitroRecombinant ProteinsReceptors TNF-Related Apoptosis-Inducing LigandCHO CellCell cultureApoptosisImmunologyCancer researchTumor necrosis factor alphaCricetuluHuman
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Subtype-Specific Desensitization of Human Endothelin ETA and ETB Receptors Reflects Differential Receptor Phosphorylation

1997

Endothelins regulate blood pressure in mammals through G protein-coupled receptors. Two receptor subtypes, ETA and ETB, exist which differ by their agonist profiles. Here we show subtype-specific differences in the inactivation of these endothelin receptors. Using a modified inositol phosphate accumulation assay, we found that stimulation of ETA by endothelin-1 results in sustained activation of the subtype, retaining >30% of its initial activity even 20 min after agonist administration, whereas the ETB rapidly deactivated after agonist stimulation, losing >80% of its initial activity within 5 min after endothelin application. The discrepancy in receptor inactivation is reflected by subtype…

Agonistmedicine.hormonemedicine.medical_specialtyEndothelin receptor type Amedicine.drug_classmedia_common.quotation_subjectStimulationCHO CellsPalmitic AcidsSpodopteraLigandsBiochemistryEndothelinsCricetinaeInternal medicinemedicineAnimalsHumansPhosphorylationInternalizationReceptorProtein Kinase Cmedia_commonReceptors EndothelinChemistryImmune Serarespiratory systemReceptor Endothelin AReceptor Endothelin BKineticsEndocrinologycardiovascular systemPhosphorylationEndothelin receptorcirculatory and respiratory physiologyBiochemistry
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Altered atypical coupling of γ-aminobutyrate type A receptor agonist and convulsant binding sites in subunit-deficient mouse lines

2001

We searched for subunit correlations for GABA(A) receptor-associated atypically GABA-insensitive [35S]TBPS binding. The homomeric beta3 subunit receptors could be excluded, as GABA-insensitive [35S]TBPS binding was present in beta3-/- mice. Localization of GABA-insensitive [35S]TBPS binding correlated best with those of delta, alpha4 and alpha6 subunit mRNAs. The amounts of GABA-insensitive [35S]TBPS binding components were increased in delta-/- mice, but dramatically reduced in alpha6-/- mice, suggesting a role for alpha6 but excluding delta subunits.

Agonistmedicine.medical_specialtymedicine.drug_classProtein subunitMolecular Sequence DataConvulsantsBiologySulfur Radioisotopesmedicine.disease_causeMiceRadioligand AssayCellular and Molecular NeuroscienceInternal medicinemedicineAnimalsHomomericRNA MessengerBinding siteReceptorGABA AgonistsMolecular BiologyBrain ChemistryMice KnockoutMutationBinding SitesGABAA receptorBridged Bicyclo Compounds HeterocyclicReceptors GABA-AMolecular biologyEndocrinologynervous systemConvulsantMolecular Brain Research
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Galantamine is an allosterically potentiating ligand of neuronal nicotinic but not of muscarinic acetylcholine receptors.

2003

Galantamine (Reminyl), an approved treatment for Alzheimer's disease (AD), is a potent allosteric potentiating ligand (APL) of human alpha 3 beta 4, alpha 4 beta 2, and alpha 6 beta 4 nicotinic receptors (nAChRs), and of the chicken/mouse chimeric alpha 7/5-hydroxytryptamine3 receptor, as was shown by whole-cell patch-clamp studies of human embryonic kidney-293 cells stably expressing a single nAChR subtype. Galantamine potentiates agonist responses of the four nAChR subtypes studied in the same window of concentrations (i.e., 0.1-1 microM), which correlates with the cerebrospinal fluid concentration of the drug at the recommended daily dosage of 16 to 24 mg. At concentrations10 microM, gal…

Agonistmedicine.medical_specialtymedicine.drug_classRecombinant Fusion ProteinsAllosteric regulationPhenylcarbamatesRivastigminePharmacologyReceptors NicotinicMiceAllosteric RegulationPiperidinesInternal medicineMuscarinic acetylcholine receptormedicineGalantamineAnimalsHumansDonepezilReceptorTrichlorfonCells CulturedPharmacologyNeuronsChemistryGalantamineLigand (biochemistry)Receptors MuscarinicEndocrinologyNicotinic agonistIndansTacrineMolecular MedicineCholinergicCarbamatesCholinesterase Inhibitorsmedicine.drugThe Journal of pharmacology and experimental therapeutics
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