Search results for "cell line"

showing 10 items of 2924 documents

Bradykinin-induced Internalization of the Human B2Receptor Requires Phosphorylation of Three Serine and Two Threonine Residues at Its Carboxyl Tail

1999

The binding of bradykinin (BK) to B2 receptor triggers the internalization of the agonist-receptor complex. To investigate the mechanisms and the receptor structures involved in this fundamental process of receptor regulation, the human B2 receptor was mutated within its cytoplasmic tail by complementary strategies of truncation, deletion, and amino acid substitution. Ligand binding, signal transduction, internalization as well as phosphorylation were studied for the mutated receptors expressed in COS, CHO, and HEK 293 cells. Truncation of 44 out of 55 amino acid residues of the receptor's cytoplasmic tail corresponding to positions 321-364 did not alter the kinetics of BK binding and the r…

ThreonineReceptor Bradykinin B2media_common.quotation_subjectMolecular Sequence DataCHO CellsBiologyBradykininTransfectionBiochemistryCell LineSerineCricetinaeSerineAnimalsHumans5-HT5A receptorAmino Acid SequencePhosphorylationInternalizationReceptorMolecular BiologyPeptide sequenceDNA Primersmedia_commonBase SequenceReceptors BradykininCoated Pits Cell-MembraneCell BiologyInterleukin-13 receptorClathrinEndocytosisRecombinant ProteinsCell biologyKineticsBiochemistryCOS CellsPhosphorylationSignal transductionJournal of Biological Chemistry
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JNK phosphorylation relieves HDAC3-dependent suppression of the transcriptional activity of c-Jun

2003

The AP-1 transcription factor c-Jun is a prototypical nuclear effector of the JNK signal transduction pathway. The integrity of JNK phosphorylation sites at serines 63/73 and at threonines 91/93 in c-Jun is essential for signal-dependent target gene activation. We show that c-Jun phosphorylation mediates dissociation of an inhibitory complex, which is associated with histone deacetylase 3 (HDAC3). The subsequent events that ultimately cause increased mRNA synthesis are independent of c-Jun phosphorylation and its interaction with JNK. These findings provide an 'activation by de-repression' model as an explanation for the stimulatory function of JNK on c-Jun.

ThreonineTranscriptional ActivationTranscription GeneticMAP Kinase Kinase 4Proto-Oncogene Proteins c-junRecombinant Fusion ProteinsMitogen-activated protein kinase kinaseHistone DeacetylasesGeneral Biochemistry Genetics and Molecular BiologyCell LinePhosphorylation cascadeMiceSuppression GeneticGenes ReporterSerineAnimalsHumansRNA MessengerPhosphorylationMolecular BiologyTranscription factorSequence DeletionMitogen-Activated Protein Kinase KinasesGeneral Immunology and MicrobiologybiologyGeneral Neurosciencec-junJNK Mitogen-Activated Protein KinasesArticles3T3 CellsHDAC3Molecular biologyProtein Structure TertiaryMitogen-activated protein kinaseMutationMutagenesis Site-Directedbiology.proteinPhosphorylationSignal transductionProtein BindingThe EMBO Journal
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Discovery and validation of small-molecule heat-shock protein 90 inhibitors through multimodality molecular imaging in living subjects.

2012

Up-regulation of the folding machinery of the heat-shock protein 90 (Hsp90) chaperone protein is crucial for cancer progression. The two Hsp90 isoforms (α and β) play different roles in response to chemotherapy. To identify isoform-selective inhibitors of Hsp90(α/β)/cochaperone p23 interactions, we developed a dual-luciferase (Renilla and Firefly) reporter system for high-throughput screening (HTS) and monitoring the efficacy of Hsp90 inhibitors in cell culture and live mice. HTS of a 30,176 small-molecule chemical library in cell culture identified a compound, N -(5-methylisoxazol-3-yl)-2-[4-(thiophen-2-yl)-6-(trifluoromethyl)pyrimidin-2-ylthio]acetamide (CP9), that binds to Hsp90(α/β) an…

Thymidine kinase activityProtein FoldingImmunoprecipitationLactams MacrocyclicBlotting WesternMice NudeThiophenesBiologyThioacetamideTritiumSmall Molecule LibrariesMiceco-chaperone p23Luciferases FireflyHeat shock proteinCell Line TumorNeoplasmsAcetamidesDrug DiscoveryBenzoquinonesAnimalsHumansImmunoprecipitationProtein IsoformsLuciferaseHSP90 Heat-Shock ProteinsLuciferases RenillaProstaglandin-E SynthasesMultidisciplinaryCell growthImidazolesbioluminescence imagingHsp90Small moleculeMolecular biologydrug developmentHigh-Throughput Screening Assayssmall-molecule inhibitorsIntramolecular OxidoreductasesLeadPNAS PlusCell culturePositron-Emission TomographyPyrazinesbiology.proteinPET/computed tomography imagingTomography X-Ray ComputedProceedings of the National Academy of Sciences of the United States of America
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Aβ Oligomers and Fibrillar Aggregates Induce Different Apoptotic Pathways in LAN5 Neuroblastoma Cell Cultures

2009

Fibril deposit formation of amyloid beta-protein (Abeta) in the brain is a hallmark of Alzheimer's disease (AD). Increasing evidence suggests that toxicity is linked to diffusible Abeta oligomers, which have been found in soluble brain extracts of AD patients, rather than to insoluble fibers. Here we report a study of the toxicity of two distinct forms of recombinant Abeta small oligomers and fibrillar aggregates to simulate the action of diffusible Abeta oligomers and amyloid plaques on neuronal cells. Different techniques, including dynamic light scattering, fluorescence, and scanning electron microscopy, have been used to characterize the two forms of Abeta. Under similar conditions and …

Time FactorsAmyloidCell SurvivalBiophysicsApoptosisBiologyFibrilCaspase 8Substrate SpecificityNeuroblastomaCytosolCell Line TumormedicineHumansEnzyme InhibitorsProtein Structure QuaternaryCaspase-9Amyloid beta-PeptidesDose-Response Relationship DrugProteinCytochrome cNeurodegenerationCytochromes cHydrogen-Ion Concentrationmedicine.diseaseCaspase InhibitorsPeptide FragmentsCell biologyProtein TransportCytosolApoptosisMicroscopy Electron Scanningbiology.proteinProtein MultimerizationProtein BindingSignal TransductionBiophysical Journal
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Gold Nanoparticles Supported on Nanoparticulate Ceria as a Powerful Agent against Intracellular Oxidative Stress

2012

Ceria-supported gold nanoparticles are prepared exhibiting peroxidase activity and acting as radical traps. Au/CeO2 shows a remarkable biocompatibility as demonstrated by measuring cellular viability, proliferation, and lack of apoptosis for two human cell lines (Hep3B and HeLa). The antioxidant activity of Au/CeO2 against reactive oxygen species (ROS) is demonstrated by studying the cellular behavior of Hep3B and HeLa in a model of cellular oxidative stress. It is determined that Au/CeO2 exhibits higher antioxidant activity than glutathione, the main cytosolic antioxidant compound, and its CeO2 carrier. Overall the result presented here shows the potential of implementing well-established …

Time FactorsAntioxidantMaterials scienceBiocompatibilityCell SurvivalPolymersPeroxidase activitymedicine.medical_treatmentMetal NanoparticlesApoptosisBiocompatible MaterialsIntracellular oxidative stressmedicine.disease_causeAntioxidantsCatalysisCell LineBiomaterialsHeLachemistry.chemical_compoundCeriaQUIMICA ORGANICAmedicineHumansNanotechnologyGold nanoparticlesGeneral Materials ScienceCell Proliferationchemistry.chemical_classificationReactive oxygen speciesbiologyGeneral ChemistryGlutathionebiology.organism_classificationOxidative StressNanomedicinePeroxidasesBiochemistrychemistryColloidal goldNanoparticlesGoldReactive Oxygen SpeciesIntracellularOxidative stressHeLa CellsBiotechnologySmall
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The actin-based motility of intracellularListeria monocytogenesis not controlled by small GTP-binding proteins of the Rho- and Ras-subfamilies

1999

In this study, we analyzed whether the actin-based motility of intracellular Listeria monocytogenes is controlled by the small GTP-binding proteins of the Rho- and Ras-subfamilies. These signalling proteins are key regulatory elements in the control of actin dynamics and their activity is essential for the maintenance of most cellular microfilament structures. We used the Clostridium difficile toxins TcdB-10463 and TcdB-1470 to specifically inactivate these GTP-binding proteins. Treatment of eukaryotic cells with either of these toxins led to a dramatic breakdown of the normal actin cytoskeleton, but did not abrogate the invasion of epithelial cells by L. monocytogenes and had no effect on …

Time FactorsArp2/3 complexClostridium difficile toxin Bmacromolecular substancesBiologyMicrofilamentMicrobiologyCell LineBacterial ProteinsGTP-Binding ProteinsGeneticsMolecular BiologyMicroscopy ConfocalMicroscopy VideoClostridioides difficileActin remodelingActin cytoskeletonListeria monocytogenesActinsCell biologyEndotoxinsProfilinParacytophagyMicroscopy Electron Scanningras Proteinsbiology.proteinMDia1FEMS Microbiology Letters
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PHEA-graft-polybutylmethacrylate copolymer microparticles for delivery of hydrophobic drugs.

2012

Abstract Polymeric microparticles encapsulating two model hydrophobic drugs, beclomethasone dipropionate (BDP) and flutamide (FLU) were prepared by using the high pressure homogenization-solvent evaporation method starting from a oil-in-water emulsion. For the preparation of polymeric microparticles a α,β-poly(N-2-hydroxyethyl)- d , l -aspartamide (PHEA) graft copolymer with comb like structure was properly synthesized via grafting from atom transfer radical polymerization (ATRP) technique, by using two subsequent synthetic steps. In the first step a polymeric multifunctional macroinitiator was obtained by the conjugation of a proper number of 2-bromoisobutyryl bromide (BIB) residues to the…

Time FactorsBioadhesivePharmaceutical ScienceCell LineDrug Delivery SystemsPolymethacrylic AcidsPolymer chemistryMucoadhesionCopolymerSide chainHumansPhea polybutylmethacrylate microparticles drug deliveryParticle SizeGlucocorticoidsDrug CarriersDose-Response Relationship DrugChemistryAtom-transfer radical-polymerizationBeclomethasoneAdhesivenessAndrogen AntagonistsGraftingFlutamideMicrospheresPolymerizationDelayed-Action PreparationsEmulsionSolventsNanoparticlesEmulsionsCaco-2 CellsPeptidesHydrophobic and Hydrophilic InteractionsInternational journal of pharmaceutics
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Expression and possible functions of the cholinergic system in a murine embryonic stem cell line.

2007

The expression of a cholinergic system during embryonic development is a widespread phenomenon. However, no precise function could be assigned to it during early pre-neural stages and there are only few studies that document when it precisely starts to be expressed. Here, we examined the expression of cholinergic components in a murine embryonic stem cell line by RT-PCR, histochemistry, and enzyme activity measurements; the acetylcholine (ACh) content was measured by HPLC. We have demonstrated that embryonic stem cells express ACh, acetylcholine receptors, choline acetyltransferase (ChAT), acetyl- and butyryl-cholinesterase (AChE and BChE). Butyryl-cholinesterase (BChE) expression was highe…

Time FactorsBiologyGeneral Biochemistry Genetics and Molecular BiologyCell LineCholine O-AcetyltransferaseMicemedicineAnimalsCholinesterasesReceptors CholinergicGeneral Pharmacology Toxicology and PharmaceuticsEmbryonic Stem CellsAcetylcholine receptorCell ProliferationTetraisopropylpyrophosphamideReverse Transcriptase Polymerase Chain ReactionGene Expression ProfilingGeneral MedicineBenzenaminium 44'-(3-oxo-15-pentanediyl)bis(NN-dimethyl-N-2-propenyl-) DibromideCholine acetyltransferaseEmbryonic stem cellMolecular biologyAcetylcholineCell cultureButyrylcholinesteraseAcetylcholinesteraseCholinergicCholinesterase InhibitorsStem cellAcetylcholineAdult stem cellmedicine.drugLife sciences
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Erythropoietin mediates tissue protection through an erythropoietin and common beta-subunit heteroreceptor

2004

The cytokine erythropoietin (Epo) is tissue-protective in preclinical models of ischemic, traumatic, toxic, and inflammatory injuries. We have recently characterized Epo derivatives that do not bind to the Epo receptor (EpoR) yet are tissue-protective. For example, carbamylated Epo (CEpo) does not stimulate erythropoiesis, yet it prevents tissue injury in a wide variety ofin vivoandin vitromodels. These observations suggest that another receptor is responsible for the tissue-protective actions of Epo. Notably, prior investigation suggests that EpoR physically interacts with the common β receptor (βcR), the signal-transducing subunit shared by the granulocyte-macrophage colony stimulating fa…

Time FactorsBiologyMotor ActivityHeteroreceptorNeuroprotectionCell LineMicemedicineReceptors ErythropoietinAnimalsVentricular Functionerythropoietin receptor; common beta receptor; tissue injury; CytokinesReceptorErythropoietinAortaCells CulturedSpinal Cord InjuriesMice KnockoutMultidisciplinaryCell MembraneBiological SciencesErythropoietin Erythropoietin receptor neuroprotectionErythropoietin receptorCell biologyMice Inbred C57BLProtein SubunitsErythrocyte maturationErythropoietinKnockout mouseImmunologyErythropoiesismedicine.drug
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Detoxifying antitumoral drugs via nanoconjugation: the case of gold nanoparticles and cisplatin

2021

Nanoparticles (NPs) have emerged as a potential tool to improve cancer treatment. Among the proposed uses in imaging and therapy, their use as a drug delivery scaffold has been extensively highlighted. However, there are still some controversial points which need a deeper understanding before clinical application can occur. Here the use of gold nanoparticles (AuNPs) to detoxify the antitumoral agent cisplatin, linked to a nanoparticle via a pH-sensitive coordination bond for endosomal release, is presented. The NP conjugate design has important effects on pharmacokinetics, conjugate evolution and biodistribution and results in an absence of observed toxicity. Besides, AuNPs present unique o…

Time FactorsCancer TreatmentMetal Nanoparticleslcsh:MedicinePharmacologyMiceNanotechnologyTissue Distributionlcsh:Sciencemedia_commonDrug DistributionDrug CarriersMultidisciplinaryChemistryDNA NeoplasmOrgan SizeHydrogen-Ion ConcentrationEndocytosisOncologyColloidal goldDrug deliveryInactivation MetabolicMedicinemedicine.drugResearch ArticleBiotechnologyDrugBiodistributionDrugs and Devicesmedia_common.quotation_subjectMaterials ScienceAntineoplastic AgentsMaterial by AttributePharmacokineticsCell Line TumormedicineAnimalsHumansPharmacokineticsBiologyNanomaterialsCisplatinUnited States Food and Drug Administrationlcsh:RChemotherapy and Drug TreatmentUnited StatesBionanotechnologylcsh:QGoldNanocarriersCisplatinConjugate
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