Search results for "binding"

showing 10 items of 3896 documents

Cytotoxicity and inhibition of P-glycoprotein by selected medicinal plants from Thailand.

2014

Abstract Ethnopharmacological relevance Thai medicine has a long tradition of tonifying medicinal plants. In the present investigation, we studied the flower extracts of Jasminum sambac, Mammea siamensis, Mesua ferrea, Michelia alba, Mimusops elengi, and Nelumbo nucifera and speculated that these plants might influence metabolism and substance flow in the body. Materials and methods Isolation of porcine brain capillary endothelial cells (PBCECs) as well as multidrug-resistance CEM/ADR5000 leukemia cells, MDA-M;B-231 breast cancer, U-251 brain tumor, and HCT-116 colon cancer cells were used. The calcein-acetoxymethylester (AM) assay was used to measure inhibition of P-glycoprotein transport.…

SwineMesua ferreaMimusops elengiFlowersPharmacologyBlood–brain barrierchemistry.chemical_compoundCell Line TumorNeoplasmsDrug DiscoverymedicineAnimalsHumansATP Binding Cassette Transporter Subfamily B Member 1CytotoxicityP-glycoproteinPharmacologyMedicine East Asian TraditionalPlants MedicinalbiologyTraditional medicinePlant ExtractsMammeaBrainEndothelial Cellsmedicine.diseasebiology.organism_classificationThailandAntineoplastic Agents PhytogenicDrug Resistance MultipleLeukemiamedicine.anatomical_structurechemistryBlood-Brain BarrierDrug Resistance Neoplasmbiology.proteinEndothelium VascularGrowth inhibitionJournal of ethnopharmacology
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Towards a fully synthetic MUC1-based anticancer vaccine: efficient conjugation of glycopeptides with mono-, di-, and tetravalent lipopeptides using c…

2011

Abstract The membrane-bound tumor-associated glycoprotein MUC1 is aberrantly glycosylated in cancer cells compared with normal cells, and is therefore considered an attractive target for cancer immunotherapy. However, tumor-associated glycopeptides from MUC1 do not elicit a sufficiently robust immune response. Therefore, antitumor vaccines were developed, which consist of MUC1 glycopeptides as the B epitopes and immune-stimulating toll-like receptor 2 (TLR 2) lipopeptide ligands. These fully synthetic vaccine candidates were prepared by solid-phase synthesis of the MUC1 glycopeptides. The Pam(3) Cys lipopeptide, also synthesized on solid-phase, was C-terminally coupled to oligovalent lysine…

Synthetic vaccineMagnetic Resonance SpectroscopyCarbohydrate chemistryMolecular Sequence DataAntineoplastic AgentsCancer VaccinesCatalysisEpitopeCell Linechemistry.chemical_compoundLipopeptidesMiceSolid-phase synthesisAnimalsHumansAntigens Tumor-Associated CarbohydrateVaccines SyntheticMembrane GlycoproteinsMolecular StructureOrganic ChemistryMucin-1GlycopeptidesLipopeptideGeneral ChemistryCombinatorial chemistryGlycopeptidechemistryClick chemistryClick ChemistryConjugateProtein BindingChemistry (Weinheim an der Bergstrasse, Germany)
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Autoimmunity to the p53 protein is a feature of systemic lupus erythematosus (SLE) related to anti-DNA antibodies.

2001

The induction of anti-DNA autoantibodies in systemic lupus erythematosus (SLE) patients is problematic because mammalian DNA is poorly immunogenic at best. Here we demonstrate a chain of connected antibodies in SLE patient sera that could account for the induction of anti-DNA antibody, and possibly for some of the pathogenic features of SLE. We now report that SLE patients, in addition to anti-DNA, produce antibodies to the carboxy-terminal domain of the tumour suppressor molecule p53; this p53 domain recognizes damaged DNA. Hence, these anti-p53 antibodies could mimic damaged DNA immunologically. Indeed, SLE sera do contain anti-idiotypic antibodies to a prototypic anti-p53 antibody. Moreo…

Systemic diseaseAnti-nuclear antibodyImmunologyBiologymedicine.disease_causeProtein Structure SecondaryAutoimmunityImmunoglobulin Idiotypesimmune system diseasesmedicineImmunology and AllergyHumansLupus Erythematosus Systemicskin and connective tissue diseasesAutoantibodiesAutoimmune diseaseLupus erythematosusMolecular MimicryAutoantibodymedicine.diseaseDNA-Binding ProteinsMolecular mimicryAntibodies AntinuclearImmunologyCancer researchbiology.proteinAntibodyTumor Suppressor Protein p53PeptidesJournal of autoimmunity
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The role of NF-AT transcription factors in T cell activation and differentiation11We dedicate this review to Prof. Dr. Rigomar Rieger (Gatersleben), …

2000

AbstractThe family of genuine NF-AT transcription factors consists of four members (NF-AT1 [or NF-ATp], NF-AT2 [or NF-ATc], NF-AT3 and NF-AT4 [or NF-ATx]) which are characterized by a highly conserved DNA binding domain (is designated as Rel similarity domain) and a calcineurin binding domain. The binding of the Ca2+-dependent phosphatase calcineurin to this region controls the nuclear import and exit of NF-ATs. This review deals (1) with the structure of NF-AT proteins, (2) the DNA binding of NF-AT factors and their interaction with AP-1, (3) NF-AT target genes, (4) signalling pathways leading to NF-AT activation: the role of protein kinases and calcineurin, (5) the nuclear entry and exit …

T cell activationCellular differentiationT cell differentiationCell BiologyDNA-binding domainCell cycleBiologyInterleukinNFATC Transcription FactorsAP-1Molecular biologyCalcineurinCyclosporin AT cell differentiationNF-AT transcription factorNuclear proteinMolecular BiologyTranscription factorBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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Identification of HLA-A*0201-Restricted T Cell Epitopes Derived from the Novel Overexpressed Tumor Antigen Calcium-Activated Chloride Channel 2

2002

Abstract Vaccination against tumor Ags may become a promising treatment modality especially in cancer types where other therapeutic approaches fail. However, diversity of tumors requires that a multitude of Ags become available. Differential expression in normal vs cancerous tissues, both at the mRNA and the protein level, may identify Ag candidates. We have previously compared transcripts from squamous cell lung cancer and normal lung tissue using differential display analysis, and found a transcript that was overexpressed in malignant cells and was identical with the calcium-activated chloride channel 2 (CLCA2) gene. We have now selected HLA-A2-restricted peptides from CLCA2, and have gen…

T cellImmunologyAntigen presentationEpitopes T-LymphocyteStreptamerCD8-Positive T-LymphocytesBiologyEpitopeCell LineInterleukin 21AntigenAntigens NeoplasmChloride ChannelsHLA-A2 AntigenmedicineHumansImmunology and AllergyCytotoxic T cellAntigen-presenting cellAllelesAntigen PresentationHLA-A AntigensMolecular biologyCoculture TechniquesPeptide FragmentsPancreatic Neoplasmsmedicine.anatomical_structureCalciumOligopeptidesProtein BindingThe Journal of Immunology
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An innate cell-mediated, murine ulcerative colitis-like syndrome in the absence of nuclear factor of activated T cells.

2004

Abstract Background & Aims: Nuclear factor of activated T cells transcription factors plays a central role in immunity by regulating the expression of multiple cytokines and other regulatory molecules, many of which have been heavily implicated in the pathogenesis of inflammatory bowel disease. However, few studies have directly investigated the nuclear factor of activated T cells proteins in inflammatory bowel disease. We describe here a specific role for nuclear factor of activated T cells c2 in the pathogenesis of murine inflammatory bowel disease. Methods: Mice deficient for nuclear factor of activated T cells c2, recombinase activating gene-2, or both and transgenic or nontransgenic fo…

T-LymphocytesBiologyInterleukin 21MicemedicineImmune ToleranceCytotoxic T cellAnimalsIL-2 receptorB-LymphocytesImmunity CellularMice Inbred BALB CHepatologyNFATC Transcription FactorsZAP70Innate lymphoid cellGastroenterologyNuclear ProteinsT helper cellRectal ProlapseNatural killer T cellAcquired immune systemMice Mutant StrainsDNA-Binding ProteinsMice Inbred C57BLmedicine.anatomical_structureImmunologyCancer researchColitis UlcerativeTranscription FactorsGastroenterology
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Inefficient Termination of Antigen Responses in NF-ATp-Deficient Mice

1998

In order to elucidate the role of NF-ATp, one of the most prominent members of family of NF-AT transcription factors in peripheral T lymphocytes, in T cell activation and differentiation we created NF-ATp-deficient mice by gene targeting. Such NF-ATp-/- mice are born and appear to develop a normal immune system. Apart from clear-cut defects in the synthesis of mRNAs for Th2-type lymphokines, such as IL-4, IL-5, IL-10 and IL-13, in primary and secondary stimulations of spleen cells in vitro, of a distinct impaired deletion of V beta 11+/CD4+ T lymphocytes from these mice was detected after superantigen injection. Moreover, NF-ATp-/- mice older than 6 weeks show an 2-5 fold increase in number…

T-LymphocytesT cellImmunologyApoptosisCell CountEnterotoxinsMiceImmune systemAntigenSuperantigenmedicineAnimalsHumansImmunology and AllergyCell Line TransformedB-LymphocytesLymphokinesSuperantigensNFATC Transcription FactorsbiologyCD44LymphokineNuclear ProteinsGene targetingHematologyMolecular biologyDNA-Binding Proteinsmedicine.anatomical_structureCell culturebiology.proteinGene DeletionTranscription FactorsImmunobiology
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Different Efficiency of Heat Shock Proteins (HSP) to Activate Human Monocytes and Dendritic Cells: Superiority of HSP60

2002

Abstract One essential immunoregulatory function of heat shock protein (HSP) is activation of the innate immune system. We investigated the activation of human monocytes and monocyte-derived dendritic cells (DC) by recombinant human HSP60, human inducible HSP72, and preparations of human gp96 and HSP70 under stringent conditions, in the absence of serum and with highly purified monocytes. HSP60 induced human DC maturation and activated human DC to secrete proinflammatory cytokines. HSP72 induced DC maturation to a lesser extent, but activated human monocytes and immature DC as efficiently as HSP60 to release proinflammatory cytokines. The independence of the effects of HSP60 and HSP72 from …

T-Lymphocytesmedicine.medical_treatmentImmunologyHSP72 Heat-Shock ProteinsPeptide bindingBiologyLymphocyte ActivationMonocytesProinflammatory cytokineAntigens NeoplasmHeat shock proteinmedicineHumansImmunology and AllergyHSP70 Heat-Shock ProteinsSecretionHeat-Shock ProteinsInnate immune systemCell DifferentiationChaperonin 60Dendritic CellsMolecular biologyCoculture TechniquesRecombinant ProteinsHsp70CytokineCytokinesHSP60Inflammation MediatorsSignal TransductionThe Journal of Immunology
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Recombinant expression, in vitro refolding, and biophysical characterization of the N-terminal domain of T1R3 taste receptor

2012

Facteur d'impact (5 ans) : 1,617Notoriété à 2 ans : Acceptable (biochem.res.methods); The sweet taste receptor is a heterodimeric receptor composed of the T1R2 and T1R3 subunits, while T1R1 and T1R3 assemble to form the umami taste receptor. T1R receptors belong to the family of class C G-protein coupled receptors (GPCRs). In addition to a transmembrane heptahelical domain, class C GPCRs have a large extracellular N-terminal domain (NTD), which is the primary ligand-binding site. The T1R2 and T1R1 subunits have been shown to be responsible for ligand binding, via their NTDs. However, little is known about the contribution of T1R3-NTD to receptor functions. To enable biophysical characteriza…

TASTE RECEPTORSucroseCircular dichroismcongenital hereditary and neonatal diseases and abnormalitiesProtein Conformation[ SDV.AEN ] Life Sciences [q-bio]/Food and Nutritionumami receptorUmamiSWEETENERmedicine.disease_causeReceptors G-Protein-Coupledtaste03 medical and health sciencesGPCRTaste receptorPROTEIN REFOLDINGexpressionEscherichia colimedicineHumansRECOMBINANT GPCRbacteriaReceptorEscherichia coli030304 developmental biologyG protein-coupled receptorInclusion Bodies0303 health sciencesChemistrysweet receptor030302 biochemistry & molecular biologyRecombinant ProteinsTransmembrane proteinnervous system diseasesResearch NoteBACTERIAL EXPRESSIONBiochemistrysugarElectrophoresis Polyacrylamide GelHeterologous expression[SDV.AEN]Life Sciences [q-bio]/Food and Nutritionrecombinant proteinProtein BindingBiotechnology
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A Regulatory Mechanism Involving TBP-1/Tat-Binding Protein 1 and Akt/PKB in the Control of Cell Proliferation

2011

Abstract TBP-1 /Tat-Binding Protein 1 (also named Rpt-5, S6a or PSMC3) is a multifunctional protein, originally identified as a regulator of HIV-1-Tat mediated transcription. It is an AAA-ATPase component of the 19S regulative subunit of the proteasome and, as other members of this protein family, fulfils different cellular functions including proteolysis and transcriptional regulation. We and others reported that over expression of TBP-1 diminishes cell proliferation in different cellular contexts with mechanisms yet to be defined. Accordingly, we demonstrated that TBP-1 binds to and stabilizes the p14ARF oncosuppressor increasing its anti-oncogenic functions. However, TBP-1 restrains cell…

TBP-1/Tat-Binding Protein 1lcsh:Medicinemacromolecular substancesBiologymTORC2Cell GrowthTBP-1/Tat-Binding Protein 1; cell proliferationp14arfMolecular Cell BiologyGeneticsCancer GeneticsTranscriptional regulationGene Networkslcsh:ScienceBiologyProtein kinase BPI3K/AKT/mTOR pathwayMultidisciplinaryCell growthAKTBinding proteinlcsh:RMolecular biologySignaling CascadesCell biologyTBP-1enzymes and coenzymes (carbohydrates)cell proliferationbiology.proteinMdm2lcsh:QCell DivisionResearch ArticleSignal TransductionPLoS ONE
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