Search results for "HEK 293"

showing 10 items of 73 documents

The new radioligand [H-3]-L 748,337 differentially labels human and rat beta(3)-adrenoceptors

2013

As no suitable radioligand exists for the detection of β3-adrenoceptors, we have explored the radioligand binding properties of a tritiated version of the selective β3-adrenoceptor antagonist L 748,337. Kinetic and equilibrium saturation and competition binding experiments were performed with [(3)H]-L 748,337 on membrane fractions of HEK and CHO cells stably transfected with human and rat β-adrenoceptor subtypes. Based on both association/dissociation kinetic and equilibrium saturation binding studies in transfected HEK cells, [(3)H]-L 748,337 exhibited an affinity of approximately 2 nM for human β3-adrenoceptors. Competition studies with agonists and subtype-selective antagonists validated…

MaleStereochemistryUrinary BladderCHO CellsIn Vitro TechniquesAminophenolsBinding CompetitiveRats Sprague-Dawley03 medical and health sciencesRadioligand Assay0302 clinical medicineCricetulusRadioligandAnimalsHumans030304 developmental biologyPharmacology0303 health sciencesSulfonamidesbiologyChemistryChinese hamster ovary cellHEK 293 cellsAntagonistMuscle SmoothTransfectionbiology.organism_classificationMolecular biologyRadioligand AssayRatsMembraneHEK293 CellsReceptors Adrenergic beta-3CricetulusAdrenergic beta-3 Receptor Antagonists030217 neurology & neurosurgeryEuropean Journal of Pharmacology
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The Alzheimer’s disease associated bacterial protease RgpB from P. gingivalis activates the alternative β-secretase meprin β thereby increasing Aβ ge…

2019

AbstractAlzheimer’s disease (AD) is the most common type of dementia and characterized by tau hyperphosphorylation, oxidative stress, reactive microglia and amyloid-β (Aβ) deposits. A recent study revealed that Porphyromonas gingivalis infection is associated with amyloid β generation in Alzheimer’s disease. Increased Aβ levels, tau degradation and neuronal toxicity were observed as a consequence of ginigipain R (RgpB) activity, a cysteine protease constitutively secreted by P. gingivalis. Of note, we previously identified RgpB as a potent activator of the metalloproteinase meprin β. Interestingly, meprin β is an alternative β-secretase of the amyloid precursor protein (APP), which together…

MetalloproteinaseProteasebiologyMicrogliaActivator (genetics)Chemistrymedicine.medical_treatmentHEK 293 cellsbiology.organism_classificationMolecular biologyCysteine proteasemedicine.anatomical_structuremedicineAmyloid precursor proteinbiology.proteinPorphyromonas gingivalis
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FICC-Seq: a method for enzyme-specified profiling of methyl-5-uridine in cellular RNA.

2019

AbstractMethyl-5-uridine (m5U) is one the most abundant non-canonical bases present in cellular RNA, and in yeast is found at position U54 of tRNAs where modification is catalysed by the methyltransferase Trm2. Although the mammalian enzymes that catalyse m5U formation are yet to be identified via experimental evidence, based on sequence homology to Trm2, two candidates currently exist, TRMT2A and TRMT2B. Here we developed a genome-wide single-nucleotide resolution mapping method, Fluorouracil-Induced-Catalytic-Crosslinking-Sequencing (FICC-Seq), in order to identify the relevant enzymatic targets. We demonstrate that TRMT2A is responsible for the majority of m5U present in human RNA, and t…

MethyltransferaseSaccharomyces cerevisiae ProteinsCell SurvivalSaccharomyces cerevisiaeBiology03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRNA TransferYeastsGeneticsHumansNucleotideUridine030304 developmental biologychemistry.chemical_classification0303 health sciencestRNA MethyltransferasesDeoxyribonucleasesHEK 293 cellsRNAHigh-Throughput Nucleotide SequencingYeastUridineEnzymeHEK293 CellsBiochemistrychemistry030220 oncology & carcinogenesisTransfer RNARNAMethods OnlineFluorouracilNucleic acids research
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Modulation of voltage-gated K(+) channels Kv11 and Kv1 4 by forskolin.

2002

Forskolin (FSK) affects voltage-gated K + (Kv) currents in different cell types, but it is not known which of the various subunits form FSK-sensitive Kv channels. We compared the effect of the compound at Kv1.1 and Kv1.4 channels ectopically expressed in HEK 293 cells. Low FSK concentrations induced a phosphorylation-dependent potentiation of Kv1.1 currents. At higher concentrations, this effect was superimposed by a fast, cAMP-independent channel block. Kv1.4 currents were inhibited with lower potency by FSK but were not modified by phosphorylation. The variable effect of the compound might help to distinguish between Kv subunits expressed by native cells.  2002 Elsevier Science Ltd. All …

Patch-Clamp TechniquesPotassium ChannelsStereochemistryBiologyMembrane PotentialsCellular and Molecular Neurosciencechemistry.chemical_compoundmedicineCyclic AMPHumansPatch clampPhosphorylationProtein kinase ACells CulturedPharmacologyFrequency-shift keyingForskolinDose-Response Relationship DrugHEK 293 cellsColforsinCyclic AMP-Dependent Protein KinasesElectrophysiologyElectrophysiologyKineticsMechanism of actionchemistryPotassium Channels Voltage-GatedBiophysicsPhosphorylationKv1.4 Potassium Channelmedicine.symptomKv1.1 Potassium ChannelIon Channel GatingAlgorithmsNeuropharmacology
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Analysis of phosphorylation-dependent modulation of Kv1.1 potassium channels.

2003

The voltage-gated potassium channel Kv1.1 contains phosphorylation sites for protein kinase A (PKA) and protein kinase C (PKC). To study Kv1.1 protein expression and cellular distribution in regard to its level of phosphorylation, the effects of PKA and PKC activation on Kv1.1 were investigated in HEK 293 cells stably transfected with Kv1.1 (HEK 293/1). Without kinase activation, HEK 293/1 cells carry unphosphorylated Kv1.1 protein in the plasma membranes, whereas large amounts of phosphorylated and unphosphorylated Kv1.1 protein were located intracellularly. Activation of PKA resulted in phosphorylation of intracellular Kv1.1 protein, followed by a rapid translocation of Kv1.1 into the pla…

Patch-Clamp TechniquesPotassium Channelscomplex mixturesCell LineCellular and Molecular NeuroscienceHumansnatural sciencesProtein phosphorylationPatch clampPhosphorylationProtein kinase AProtein kinase CProtein Kinase CPharmacologyurogenital systemKinaseChemistryHEK 293 cellsAntibodies MonoclonalCyclic AMP-Dependent Protein KinasesPotassium channelCell biologyEnzyme ActivationKineticsProtein Transportnervous systemBiochemistryPotassium Channels Voltage-GatedPhosphorylationbiological phenomena cell phenomena and immunityKv1.1 Potassium ChannelIon Channel GatingNeuropharmacology
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A role for Rho in receptor- and G protein-stimulated phospholipase C Reduction in phosphatidylinositol 4,5-bisphosphate by Clostridium difficile toxi…

1996

Receptors coupled to heterotrimeric guanine nucleotide-binding proteins (G proteins) activate phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2)-hydrolyzing phospholipase C (PLC) enzymes by activated alpha of free beta gamma subunits of the relevant G proteins. To study whether low molecular weight G proteins of the Rho family are involved in receptor signaling to PLC, we examined the effect of Clostridium difficile toxin B, which glucosylates and thereby inactivates Rho proteins, on the regulation of PLC activity in human embryonic kidney (HEK) cells stably expressing the m3 muscarinic acetylcholine receptor (mAChR) subtype. Toxin B treatment of HEK cells did not affect basal PLC activi…

Phosphatidylinositol 45-DiphosphateBotulinum ToxinsG proteinBacterial ToxinsClostridium difficile toxin AClostridium difficile toxin BBiologychemistry.chemical_compoundBacterial ProteinsGTP-Binding ProteinsHeterotrimeric G proteinHumansPhosphatidylinositolCells CulturedADP Ribose TransferasesPharmacologyPhospholipase CHEK 293 cellsGeneral MedicineReceptors MuscarinicMolecular biologyCell biologychemistryPhosphatidylinositol 45-bisphosphateType C PhospholipasesrhoA GTP-Binding ProteinNaunyn-Schmiedeberg's Archives of Pharmacology
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Restoration of Clostridium difficile toxin-B-inhibited phospholipase D by phosphatidylinositol 4,5-bisphosphate.

1996

Receptor signalling to phospholipase D (PLD) in human embryonic kidney (HEK) cells stably expressing the m3 muscarinic acetylcholine receptor apparently involves Rho proteins. Since phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] has been recognized as an essential cofactor for PLD activity and since activated Rho proteins have been reported to stimulate the synthesis of PtdIns(4,5)P2, we studied whether in HEK cells PLD activity is regulated by PtdIns(4,5)P2 and, in particular, whether PtdIns(4,5)P2 can restore PLD activity inhibited by Clostridium difficile toxin B, which inactivates Rho proteins. Addition of MgATP to permeabilized HEK cells increased basal PLD activity and potentia…

Phosphatidylinositol 45-DiphosphateGTP'Bacterial ToxinsClostridium difficile toxin BBiologyBiochemistryCell Linechemistry.chemical_compoundBacterial ProteinsGTP-Binding ProteinsPhosphatidylcholineRhoB GTP-Binding ProteinPhospholipase DHumansPhosphatidylinositolEnzyme InhibitorsrhoB GTP-Binding ProteinPhospholipase DClostridioides difficileHEK 293 cellsCell MembraneMembrane ProteinsReceptors MuscarinicCell biologyEnzyme Activationenzymes and coenzymes (carbohydrates)chemistryPhosphatidylinositol 45-bisphosphateGuanosine 5'-O-(3-Thiotriphosphate)lipids (amino acids peptides and proteins)European journal of biochemistry
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SUMOylation of Blimp-1 promotes its proteasomal degradation

2011

Abstract B lymphocyte induced maturation protein-1 (Blimp-1) is a transcription repressor of the Krueppel-like family. Blimp-1 plays important roles in developmental processes, such as of germ cells and hair follicle stem cells. In B lymphocytes Blimp-1 orchestrates the terminal differentiation into plasma cells. We discovered that Blimp-1 undergoes SUMOylation by SUMO-1. This SUMOylation is modulated by the SUMO protease SENP1. While Blimp-1 is relatively stable in 293T cells, a fusion with SUMO1 rendered it to rapid proteasomal degradation. Increase in SENP1 activity stabilized Blimp-1, while a decrease promoted its degradation. Our data indicate that SUMOylation of Blimp-1 regulates its …

Proteasome Endopeptidase ComplexSENP1ImmunoprecipitationSUMO-1 ProteinBiophysicsSUMO proteinPlasma cellPlasma cellBiologyBiochemistryCell LineProtein–protein interactionSENP1Structural BiologyEndopeptidasesGeneticsmedicineHumansMolecular BiologyProteasomeProtein StabilityHEK 293 cellsSumoylationCell BiologyCell biologyRepressor ProteinsCysteine Endopeptidasesmedicine.anatomical_structureProteasomeSUMO proteasePositive Regulatory Domain I-Binding Factor 1IntracellularFEBS Letters
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The Cleavage Product of Amyloid-β Protein Precursor sAβPPα Modulates BAG3-Dependent Aggresome Formation and Enhances Cellular Proteasomal Activity

2015

Alzheimer's disease (AD) is the major age-associated form of dementia characterized by gradual cognitive decline. Aberrant cleavage of the amyloid-β protein precursor (AβPP) is thought to play an important role in the pathology of this disease. Two principal AβPP processing pathways exist: amyloidogenic cleavage of AβPP resulting in production of the soluble N-terminal fragment sAβPPβ, amyloid-β (Aβ), which accumulates in AD brain, and the AβPP intracellular domain (AICD) sAβPPα, p3 and AICD are generated in the non-amyloidogenic pathway. Prevalence of amyloidogenic versus non-amyloidogenic processing leads to depletion of sAβPPα and an increase in Aβ. Although sAβPPα is a well-accepted neu…

Proteasome Endopeptidase ComplexTime FactorsCell SurvivalLeupeptinsGreen Fluorescent ProteinsCysteine Proteinase InhibitorsProtein degradationProtein aggregationBiologyTransfectionBAG3Rats Sprague-DawleyAmyloid beta-Protein PrecursorAnimalsHumansRNA MessengerRNA Small InterferingProtein precursorCells CulturedAdaptor Proteins Signal TransducingNeuronsAmyloid beta-PeptidesDose-Response Relationship DrugGeneral NeuroscienceHEK 293 cellsBrainGeneral MedicineFibroblastsEmbryo MammalianRatsCell biologyPsychiatry and Mental healthClinical PsychologyHEK293 CellsProteostasisAggresomeGene Expression RegulationBiochemistryProteasomeProteolysisAmyloid Precursor Protein SecretasesGeriatrics and GerontologyApoptosis Regulatory ProteinsJournal of Alzheimer's Disease
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Cell Susceptibility to Baculovirus Transduction and Echovirus Infection Is Modified by Protein Kinase C Phosphorylation and Vimentin Organization

2013

ABSTRACT Some cell types are more susceptible to viral gene transfer or virus infection than others, irrespective of the number of viral receptors or virus binding efficacy on their surfaces. In order to characterize the cell-line-specific features contributing to efficient virus entry, we studied two cell lines (Ea.hy926 and MG-63) that are nearly nonpermissive to insect-specific baculovirus (BV) and the human enterovirus echovirus 1 (EV1) and compared their characteristics with those of a highly permissive (HepG2) cell line. All the cell lines contained high levels of viral receptors on their surfaces, and virus binding was shown to be efficient. However, in nonpermissive cells, BV and it…

Protein Kinase C-alphaImmunologyVimentinProtein Kinase C-epsilonBiologyModels BiologicalMicrobiologyFilamentous actinCell LineSyndecan 1MiceTransduction (genetics)Transduction GeneticViral entryVirologyAnimalsHumansVimentinPhosphorylationProtein kinase CVirulenceHEK 293 cellsHep G2 CellsVirus InternalizationMolecular biologyvirologyCulture MediaEnterovirus B HumanVirus-Cell InteractionsHEK293 CellsvirologiaCell cultureInsect ScienceHost-Pathogen Interactionsbiology.proteinReceptors VirusSyndecan-1Integrin alpha2beta1BaculoviridaeJournal of Virology
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