Search results for "binding"

showing 10 items of 3896 documents

Interaction between cannabinoid CB1 receptors and endogenous ATP in the control of spontaneous mechanical activity in mouse ileum

2009

Background and purpose Although it is well accepted that cannabinoids modulate intestinal motility by reducing cholinergic neurotransmission mediated by CB(1) receptors, it is not known whether the endocannabinoids are involved in more complex circuits and if they interact with other systems. The aim of the present study was to examine possible interactions between cannabinoid CB(1) receptors and purines in the control of spontaneous contractility of longitudinal muscle in mouse ileum. Experimental approach The mechanical activity of longitudinally oriented ileal segments from mice was recorded as isometric contractions. Key results The selective CB(1) receptor agonist, N-(2-chloroethyl)5,8…

AgonistMalemedicine.medical_specialtyP2Y receptormedicine.drug_classmedicine.medical_treatmentCB(1) receptorArachidonic AcidsP2 receptorBiologyIn Vitro TechniquesSettore BIO/09 - FisiologiaMiceAdenosine TriphosphateReceptor Cannabinoid CB1IleumInternal medicinemedicineAnimalsReceptorP2X receptors: enteric nervous systemcholinergic transmissionPharmacologypurineDose-Response Relationship DrugPurinergic receptorcannabinoidReceptor antagonistAdenosine receptorResearch PapersBiomechanical PhenomenaATPMice Inbred C57BLEndocrinologyCannabinoidGastrointestinal MotilityProtein Binding
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Intra-Nasally Administered Oligopeptide Lunasin Acts as a Possible Anti-Psychotic Agent in Mice Models

2019

Background and Objectives: Previously we have shown that synthetic lunasin, a 43 amino acid residue-containing peptide, after its central (intracisternal) administration in mice demonstrated antagonism against dopaminergic drug behavioural effects, indicating a putative antipsychotic/anti-schizophrenic profile of lunasin. The aims of the present studies were: to test whether lunasin would show an influence on the dopaminergic system after intranasal administration, and to examine the effect(s) of lunasin on serotonin and glutamatergic systems, which could play an essential role in antipsychotic action. Materials and Methods: Lunasin was administered intra-nasally at doses 0.1 and 1 nmol/mou…

AgonistMedicine (General)medicine.drug_classreceptor bindingbrain monoaminesPharmacologyMotor ActivityLunasinArticleintranasal administration03 medical and health sciencesMiceR5-9200302 clinical medicinehyper-locomotionmedicineAnimalslunasin; intranasal administration; hyper-locomotion; brain monoamines; receptor bindingAmphetaminePhencyclidine5-HT receptorAdministration IntranasalMice Inbred ICRChemistrylunasinAmphetaminesGeneral MedicineDisease Models AnimalMonoamine neurotransmitter030220 oncology & carcinogenesisNMDA receptorSerotoninOligopeptides030217 neurology & neurosurgerymedicine.drugAntipsychotic AgentsMedicina; Volume 55; Issue 7; Pages: 393
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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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Extracellular Domains of the Bradykinin B2 Receptor Involved in Ligand Binding and Agonist Sensing Defined by Anti-peptide Antibodies

1996

Many of the physiological functions of bradykinin are mediated via the B2 receptor. Little is known about binding sites for bradykinin on the receptor. Therefore, antisera against peptides derived from the putative extracellular domains of the B2 receptor were raised. The antibodies strongly reacted with their corresponding antigens and cross-reacted both with the denatured and the native B2 receptor. Affinity-purified antibodies to the various extracellular domains were used to probe the contact sites between the receptor and its agonist, bradykinin or its antagonist HOE140. Antibodies to extracellular domain 3 (second loop) efficiently interfered, in a concentration-dependent manner, with…

AgonistReceptor Bradykinin B2medicine.drug_classMolecular Sequence DataFluorescent Antibody TechniqueCHO CellsSpodopteraBradykininTransfectionBiochemistryAntibodiesProtein Structure SecondaryCell LineCricetinaeExtracellularmedicineAnimalsHumansAmino Acid SequenceBradykinin receptorBinding siteReceptorMolecular BiologyChemistryReceptors BradykininCell MembraneCell BiologyMolecular biologyPeptide FragmentsRecombinant ProteinsRatsCell biologyModels StructuralEctodomainCompetitive antagonistIntracellularJournal of Biological Chemistry
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Agonist potency differentiates G protein activation and Ca2+ signalling by the orexin receptor type 1.

2005

The G protein coupling characteristics of a flag epitope-tagged orexin receptor type 1 (OX1R) was investigated in HEK293 cells. Immunoprecipitation of the OX1R and immunoblotting revealed interactions with Gq/G11 proteins as well as with Gs and Gi proteins. Stimulation with orexin-A did not affect the ability of the OX1R to coprecipitate Gq/G11 proteins, but it robustly elevated the intracellular concentration of Ca2+, [Ca2+]i. No changes in cAMP levels could be detected upon receptor stimulation. To get further insight into the functional correlation of G protein activation and Ca2+ signalling, we used baculovirus transduction to express chimeric G proteins, containing the Galphas protein …

AgonistReceptors Neuropeptidemedicine.drug_classG proteinBiologyKidneyBiochemistryCell LineReceptors G-Protein-CoupledGTP-binding protein regulatorsGTP-Binding ProteinsOrexin ReceptorsTransduction GeneticMuscarinic acetylcholine receptormedicineCyclic AMPHumansCalcium SignalingPharmacologyReceptor Muscarinic M3Neurotransmitter AgentsOrexinsDose-Response Relationship DrugNeuropeptidesIntracellular Signaling Peptides and ProteinsMuscarinic acetylcholine receptor M3Fusion proteinOrexin receptorCell biologyBiochemistryCalciumSignal transductionBaculoviridaeSignal TransductionBiochemical pharmacology
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Induction of Transglutaminase 2 by a Liver X Receptor/Retinoic Acid Receptor α Pathway Increases the Clearance of Apoptotic Cells by Human Macrophages

2009

Rationale: Liver X receptors (LXRs) are oxysterol-activated nuclear receptors that are involved in the control of cholesterol homeostasis and inflammatory response. Human monocytes and macrophages express high levels of these receptors and are appropriate cells to study the response to LXR agonists. Objective: The purpose of this study was to identify new LXR targets in human primary monocytes and macrophages and the consequences of their activation. Methods and Results: We show that LXR agonists significantly increase the mRNA and protein levels of the retinoic acid receptor (RAR)α in primary monocytes and macrophages. LXR agonists promote RARα gene transcription through binding to a spec…

Agonistmedicine.medical_specialtyReceptors Retinoic AcidPhysiologymedicine.drug_classResponse elementReceptors Cytoplasmic and NuclearApoptosisBiologyCell LinePhagocytosisGTP-Binding ProteinsInternal medicinemedicineHumansMacrophageProtein Glutamine gamma Glutamyltransferase 2ReceptorLiver X receptorLiver X ReceptorsTransglutaminasesMacrophagesRetinoic Acid Receptor alphaMacrophage ActivationAtherosclerosisOrphan Nuclear ReceptorsCell biologyDNA-Binding ProteinsRetinoic acid receptorEndocrinologyNuclear receptorRetinoic acid receptor alphaEnzyme InductionCardiology and Cardiovascular MedicineCirculation Research
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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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LXR antagonists induce ABCD2 expression

2014

X-linked adrenoleukodystrophy (X-ALD) is a rare neurodegenerative disorder characterized by the accumulation of very-long-chain fatty acids resulting from a beta-oxidation defect. Oxidative stress and inflammation are also key components of the pathogenesis. X-ALD is caused by mutations in the ABCDI gene, which encodes for a peroxisomal half ABC transporter predicted to participate in the entry of VLCFA-CoA into the peroxisome, the unique site of their beta-oxidation. Two homologous peroxisomal ABC transporters, ABCD2 and ABCD3 have been proven to compensate for ABCD1 deficiency when overexpressed. Pharmacological induction of these target genes could therefore represent an alternative ther…

Agonistx-ald;very-long-chain fatty acid;lxr;hydroxycholesterol;abcd2medicine.medical_specialtymedicine.drug_classx-aldEndogenyContext (language use)ATP-binding cassette transporterBiologyATP Binding Cassette Transporter Subfamily DInternal medicinemedicineHumanslxr[ SDV.BDD ] Life Sciences [q-bio]/Development BiologyhydroxycholesterolLiver X receptorAdrenoleukodystrophyMolecular Biology[SDV.BDD]Life Sciences [q-bio]/Development BiologyLiver X ReceptorsFatty AcidsBiologie du développementNeurosciencesCell BiologyHep G2 CellsPeroxisomemedicine.diseaseOrphan Nuclear ReceptorsDevelopment BiologyHydroxycholesterolsvery-long-chain fatty acidOxidative StressEndocrinologyGene Expression RegulationCell cultureabcd2Neurons and Cognition[ SDV.NEU ] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]Cancer researchlipids (amino acids peptides and proteins)AdrenoleukodystrophyATP-Binding Cassette Transporters[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]
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Shared midgut binding sites for Cry1A.105, Cry1Aa, Cry1Ab, Cry1Ac and Cry1Fa proteins from Bacillus thuringiensis in two important corn pests, Ostrin…

2013

First generation of insect-protected transgenic corn (Bt-corn) was based on the expression of Cry1Ab or Cry1Fa proteins. Currently, the trend is the combination of two or more genes expressing proteins that bind to different targets. In addition to broadening the spectrum of action, this strategy helps to delay the evolution of resistance in exposed insect populations. One of such examples is the combination of Cry1A.105 with Cry1Fa and Cry2Ab to control O. nubilalis and S. frugiperda. Cry1A.105 is a chimeric protein with domains I and II and the C-terminal half of the protein from Cry1Ac, and domain III almost identical to Cry1Fa. The aim of the present study was to determine whether the c…

Agricultural BiotechnologyApplied MicrobiologyCoated vesiclePlant SciencePlasma protein bindingMothsBiochemistryOstriniaPlagues ControlBacillus thuringiensisBiomacromolecule-Ligand InteractionsPlant PestsMultidisciplinaryMicrovillibiologyGenetically Modified OrganismsQRAgricultureRecombinant ProteinsBiochemistryLarvaMedicineDisease SusceptibilityAgrochemicalsResearch ArticleBiotechnologyProtein BindingScienceProtein domainBiotecnologia agrícolaBacillus thuringiensisCoated VesiclesCerealsCropsSpodopteraSpodopteraMicrobiologyBinding CompetitiveZea maysBacterial ProteinsBotanyAnimalsPesticidesBinding siteProtein InteractionsBiologyTransgenic PlantsfungiProteinsPlant Pathologybiology.organism_classificationFusion proteinMaizeGastrointestinal TractKineticsPlant BiotechnologyPest ControlProteïnes
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