Search results for "Protein S"

showing 10 items of 1431 documents

Tif1γ regulates the TGF-β1 receptor and promotes physiological aging of hematopoietic stem cells.

2014

The hematopoietic system declines with age. Myeloid-biased differentiation and increased incidence of myeloid malignancies feature aging of hematopoietic stem cells (HSCs), but the mechanisms involved remain uncertain. Here, we report that 4-mo-old mice deleted for transcription intermediary factor 1γ (Tif1γ) in HSCs developed an accelerated aging phenotype. To reinforce this result, we also show that Tif1γ is down-regulated in HSCs during aging in 20-mo-old wild-type mice. We established that Tif1γ controls TGF-β1 receptor (Tgfbr1) turnover. Compared with young HSCs, Tif1γ(-/-) and old HSCs are more sensitive to TGF-β signaling. Importantly, we identified two populations of HSCs specifical…

AgingMyeloidReceptor Transforming Growth Factor-beta Type IReceptors Cell SurfaceCell SeparationBiologyProtein Serine-Threonine KinasesTransforming Growth Factor beta1MiceSignaling Lymphocytic Activation Molecule Family Member 1Antigens CDmedicineAnimalsMyeloid CellsRNA MessengerPolyubiquitinTranscription factorCellular SenescenceRegulation of gene expressionMultidisciplinaryUbiquitinationhemic and immune systemsBiological SciencesHematopoietic Stem CellsCell biologyHematopoiesisHaematopoiesismedicine.anatomical_structurePhysiological AgingPhenotypeGene Expression RegulationSignal transductionStem cellCell agingReceptors Transforming Growth Factor betaSignal TransductionTranscription FactorsProceedings of the National Academy of Sciences of the United States of America
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HSF1-controlled and age-associated chaperone capacity in neurons and muscle cells of C. elegans.

2010

Protein stability under changing conditions is of vital importance for the cell and under the control of a fine-tuned network of molecular chaperones. Aging and age-related neurodegenerative diseases are directly associated with enhanced protein instability. Employing C. elegans expressing GFP-tagged luciferase as a reporter for evaluation of protein stability we show that the chaperoning strategy of body wall muscle cells and neurons is significantly different and that both are differently affected by aging. Muscle cells of young worms are largely resistant to heat stress, which is directly mediated by the stress response controlled through Heat Shock Transcription Factor 1. During recover…

AgingProteomeGreen Fluorescent Proteinslcsh:MedicineBiologyBiochemistryBiochemistry/Protein FoldingAnimals Genetically ModifiedHeat shock proteinAnimalsMyocyteHeat shockCaenorhabditis elegansCaenorhabditis elegans ProteinsHSF1lcsh:ScienceDNA PrimersNeuronsMultidisciplinaryBase SequenceMuscleslcsh:RCell Biology/Cellular Death and Stress ResponsesMolecular biologyCell biologyHeat shock factorMicroscopy FluorescenceChaperone (protein)biology.proteinProtein foldinglcsh:QProtein stabilizationResearch ArticleMolecular ChaperonesTranscription FactorsPLoS ONE
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Differential cysteine depletion in respiratory chain complexes enables the distinction of longevity from aerobicity.

2010

Mitochondrially encoded proteins in long-lived animals exhibit a characteristic anomaly on the amino acid usage level: they abstain from the use of cysteine in a lifespan-dependent fashion. Here, we have further investigated this phenomenon by analyzing respiratory chain complex subunits individually. We find that complex I cysteine depletion is the almost exclusive carrier of the cysteine-lifespan correlation, whereas complex IV cysteine depletion is uniform in all aerobic animals, unrelated to longevity, but even more pronounced than complex I cysteine depletion in the longest-lived species. In nuclear encoded subunits of the respiratory chain, we find lifespan-independent cysteine deplet…

AgingTime FactorsProtein ConformationRespiratory chainBiologyProtein oxidationProtein Structure SecondaryElectron TransportProtein structureOxygen ConsumptionAnimalsHumansCysteineSulfhydryl CompoundsPhylogenychemistry.chemical_classificationCell NucleusRespiratory chain complexMembrane ProteinsAerobiosisAmino acidMitochondriaProtein Structure TertiaryTransmembrane domainOxidative StressBiochemistrychemistryMembrane proteinDevelopmental BiologyCysteineMechanisms of ageing and development
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ADAM-10 over-expression increases cortical synaptogenesis.

2006

Cortical cholinergic, glutamatergic and GABAergic terminals become upregulated during early stages of the transgenic amyloid pathology. Abundant evidence suggests that sAPP alpha, the product of the non-amyloidogenic alpha-secretase pathway, is neurotrophic both in vitro and when exogenously applied in vivo. The disintegrin metalloprotease ADAM-10 has been shown to have alpha-secretase activity in vivo. To determine whether sAPP alpha has an endogenous biological influence on cortical presynaptic boutons in vivo, we quantified cortical cholinergic, glutamatergic and GABAergic presynaptic bouton densities in either ADAM-10 moderate expressing (ADAM-10 mo) transgenic mice, which moderately ov…

Agingmedicine.medical_specialtySynaptogenesisPresynaptic TerminalsAlpha (ethology)Mice TransgenicBiologyReceptors Metabotropic GlutamateGlutamatergicADAM10 ProteinMiceReceptors GABAInternal medicinemedicineAnimalsHumansReceptors CholinergicCerebral CortexGeneral NeuroscienceGene Expression Regulation DevelopmentalMembrane Proteinscarbohydrates (lipids)ADAM Proteinsmedicine.anatomical_structureEndocrinologyCerebral cortexSynaptic plasticitySynapsesbiology.proteinGABAergicCholinergicCattleNeurology (clinical)Geriatrics and GerontologyAmyloid Precursor Protein SecretasesDevelopmental BiologyNeurotrophinNeurobiology of aging
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Histaprodifens: synthesis, pharmacological in vitro evaluation, and molecular modeling of a new class of highly active and selective histamine H(1)-r…

2000

A new class of histamine analogues characterized by a 3, 3-diphenylpropyl substituent at the 2-position of the imidazole nucleus has been prepared outgoing from 4,4-diphenylbutyronitrile (4b) via cyclization of the corresponding methyl imidate 5b with 2-oxo-4-phthalimido-1-butyl acetate or 2-oxo-1,4-butandiol in liquid ammonia, followed by standard reactions. The title compounds displayed partial agonism on contractile H(1) receptors of the guinea-pig ileum and endothelium-denuded aorta, respectively, except 10 (histaprodifen; 2-[2-(3, 3-diphenylpropyl)-1H-imidazol-4-yl]ethanamine) which was a full agonist in the ileum assay. While 10 was equipotent with histamine (1), methylhistaprodifen (…

AgonistMaleModels MolecularRhodopsinRanidaeStereochemistrymedicine.drug_classGuinea PigsSubstituentIleumHistamine H1 receptorIn Vitro TechniquesChemical synthesis/dk/atira/pure/sustainabledevelopmentgoals/clean_water_and_sanitationHistamine Agonistschemistry.chemical_compoundStructure-Activity RelationshipIleumDrug DiscoverymedicineImidazoleAnimalsHumansVasoconstrictor AgentsReceptors Histamine H1Rats WistarAortaChemistryMethylhistaminesMuscle SmoothIn vitroProtein Structure TertiaryRatsReceptors Neurotransmittermedicine.anatomical_structureMolecular MedicineEndothelium VascularSDG 6 - Clean Water and SanitationHistamineMuscle ContractionJournal of medicinal chemistry
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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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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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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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ATP and endogenous agonists inhibit evoked [3H]-noradrenaline release in rat iris via A1 and P2y-like purinoceptors.

1993

Effects of ATP, adenosine and purinoceptor antagonists on field stimulation-evoked (3 Hz, 2 min) [3H]-noradrenaline overflow were investigated in the rat isolated iris. ATP and adenosine inhibited the evoked overflow of [3H]-noradrenaline. 1,3-Dipropyl-8-cyclopentylxanthine (DPCPX) shifted the concentration-response curve of ATP to the right in a concentration-dependent manner, but with a potency (-log KB = 7.88) much lower than expected for an A1 adenosine receptor. In the continuous presence of DPCPX, the ATP-induced prejunctional inhibition was unaffected by suramin (100 mumol/l) and DIDS (4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid, 50 mumol/l) but was antagonized by the P2Y-rece…

Agonistmedicine.medical_specialtyAdenosinemedicine.drug_classSuraminIrisSuraminBiologyP2 receptor44'-Diisothiocyanostilbene-22'-Disulfonic AcidIn Vitro TechniquesSynaptic Transmissionchemistry.chemical_compoundNorepinephrineAdenosine TriphosphateInternal medicinemedicinePurinergic P2 Receptor AntagonistsAnimalsRats WistarPharmacologyProtein Synthesis InhibitorsReceptors Purinergic P2TriazinesPurinergic receptorReceptors Purinergic P1General MedicineAdenosine receptorAdenosineElectric StimulationRatsEndocrinologychemistryPurinergic P1 Receptor AntagonistsDIDSXanthinesAutoreceptormedicine.drugNaunyn-Schmiedeberg's archives of pharmacology
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