Search results for "Transfection"

showing 10 items of 581 documents

Transcriptional repression of Bmp2 by p21(Waf1/Cip1) links quiescence to neural stem cell maintenance.

2013

Relative quiescence and self renewal are defining features of adult stem cells, but their potential coordination remains unclear. Subependymal neural stem cells (NSCs) lacking cyclin-dependent kinase (CDK) inhibitor (CKI) 1a (p21) exhibit rapid expansion that is followed by their permanent loss later in life. Here we demonstrate that transcription of the gene encoding bone morphogenetic protein 2 (Bmp2) in NSCs is under the direct negative control of p21 through actions that are independent of CDK. Loss of p21 in NSCs results in increased levels of secreted BMP2, which induce premature terminal differentiation of multipotent NSCs into mature non-neurogenic astrocytes in an autocrine and/or …

Cyclin-Dependent Kinase Inhibitor p21Time FactorsCellular differentiationBone Morphogenetic Protein 2Nerve Tissue ProteinsBiologyTransfectionParacrine signallingMiceNeural Stem CellsCyclin-dependent kinaseTransduction GeneticSubependymal zoneAnimalsCell Line TransformedRegulation of gene expressionMice KnockoutGeneral NeuroscienceNeurogenesisCell CycleAge FactorsCell DifferentiationNeural stem cellCell biologyKi-67 AntigenBromodeoxyuridineGene Expression RegulationMutagenesisCulture Media Conditionedbiology.proteinNeoplastic Stem CellsCarrier ProteinsNeuroscienceAdult stem cellSubcellular FractionsNature neuroscience
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A p16INK4a-insensitive CDK4 mutant targeted by cytolytic T lymphocytes in a human melanoma.

1995

A mutated cyclin-dependent kinase 4 (CDK4) was identified as a tumor-specific antigen recognized by HLA-A2. 1-restricted autologous cytolytic T lymphocytes (CTLs) in a human melanoma. The mutated CDK4 allele was present in autologous cultured melanoma cells and metastasis tissue, but not in the patient's lymphocytes. The mutation, an arginine-to-cysteine exchange at residue 24, was part of the CDK4 peptide recognized by CTLs and prevented binding of the CDK4 inhibitor p16INK4a, but not of p21 or of p27KIP1. The same mutation was found in one additional melanoma among 28 melanomas analyzed. These results suggest that mutation of CDK4 can create a tumor-specific antigen and can disrupt the ce…

Cyclin-Dependent Kinase Inhibitor p21Tumor suppressor geneMutantMolecular Sequence DataCell Cycle ProteinsBiologyProtein Serine-Threonine Kinasesmedicine.disease_causeTransfectionPolymerase Chain ReactionMetastasisCell LineAntigenCyclinsProto-Oncogene ProteinsHLA-A2 AntigenmedicineTumor Cells CulturedAnimalsHumansPoint MutationAmino Acid SequenceCloning MolecularneoplasmsMelanomaCyclin-Dependent Kinase Inhibitor p16Cyclin-Dependent Kinase Inhibitor p15MutationMultidisciplinaryintegumentary systemBase SequenceMelanomaTumor Suppressor ProteinsCyclin-Dependent Kinase 4Cell cyclemedicine.diseaseCyclin-Dependent KinasesCytolysisCancer researchCarrier ProteinsMicrotubule-Associated ProteinsCyclin-Dependent Kinase Inhibitor p27T-Lymphocytes CytotoxicScience (New York, N.Y.)
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Cytoglobin is a respiratory protein in connective tissue and neurons, which is up-regulated by hypoxia.

2004

Cytoglobin is a recently discovered vertebrate globin distantly related to myoglobin, and its function is unknown. Here we present the first detailed analysis of the distribution and expression of cytoglobin. Northern and Western blotting experiments show the presence of cytoglobin mRNA and protein in a broad range of tissues. Quantitative PCR demonstrates an up-regulation of cytoglobin mRNA levels in rat heart and liver under hypoxic conditions (22 and 44 h of 9% oxygen). Immunofluorescence studies with three antibodies directed against different epitopes of the protein consistently show cytoglobin in connective tissue fibroblasts as well as in hepatic stellate cells. Cytoglobin is also pr…

CytoplasmRespiratory SystemFluorescent Antibody TechniqueBiochemistryMiceAntibody SpecificityChlorocebus aethiopsRespiratory functionHypoxiaNeuronsMice Inbred BALB CReverse Transcriptase Polymerase Chain ReactionCytoglobinNuclear ProteinsImmunohistochemistryGlobinsRespiratory proteinTracheamedicine.anatomical_structureLiverConnective TissueNeuroglobinRecombinant Fusion ProteinsGreen Fluorescent ProteinsMolecular Sequence DataConnective tissueBiologyTransfectionAntibodiesBone and BonesmedicineAnimalsHumansGlobinAmino Acid SequenceRNA MessengerMolecular BiologyVero CellsCell NucleusMessenger RNAMyocardiumCytoglobinCell BiologyFibroblastsMolecular biologyPeptide FragmentsRatsOxygenLuminescent ProteinsGene Expression RegulationHepatic stellate cellHeLa CellsThe Journal of biological chemistry
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Amyloid Precursor-like Protein 1 Influences Endocytosis and Proteolytic Processing of the Amyloid Precursor Protein

2005

Ectodomain shedding of the amyloid precursor protein (APP) is a key regulatory step in the generation of the Alzheimer disease amyloid beta peptide (Abeta). The molecular mechanisms underlying the control of APP shedding remain little understood but are in part dependent on the low density lipoprotein receptor-related protein (LRP), which is involved in APP endocytosis. Here, we show that the APP homolog APLP1 (amyloid precursor-like protein 1) influences APP shedding. In human embryonic kidney 293 cells expression of APLP1 strongly activated APP shedding by alpha-secretase and slightly reduced beta-secretase cleavage. As revealed by domain deletion analysis, the increase in APP shedding re…

CytoplasmTime FactorsRecombinant Fusion ProteinsAmino Acid MotifsBlotting WesternGenetic VectorsEndocytic cycleCHO CellsTransfectionEndocytosisBiochemistryCell LineAmyloid beta-Protein PrecursorGenes ReporterCricetinaeChlorocebus aethiopsEndopeptidasesmental disordersAmyloid precursor proteinAnimalsAspartic Acid EndopeptidasesHumansImmunoprecipitationAPLP1Molecular BiologyModels GeneticbiologyChemistryHEK 293 cellsP3 peptideCell BiologyEndocytosisProtein Structure TertiaryMicroscopy FluorescenceBiochemistryAlpha secretaseEctodomainCOS Cellsbiology.proteinAmyloid Precursor Protein SecretasesPeptidesGene DeletionPlasmidsJournal of Biological Chemistry
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ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1).

2000

The Myc promoter-binding protein-1 (MBP-1) is a 37-38 kDa protein that binds to the c-myc P2 promoter and negatively regulates transcription of the protooncogene. MBP-1 cDNA shares 97% similarity with the cDNA encoding the glycolytic enzyme alpha-enolase and both genes have been mapped to the same region of human chromosome 1, suggesting the hypothesis that the two proteins might be encoded by the same gene. We show here data indicating that a 37 kDa protein is alternatively translated from the full-length alpha-enolase mRNA. This shorter form of alpha-enolase is able to bind the MBP-1 consensus sequence and to downregulate expression of a luciferase reporter gene under the control of the c…

CytoplasmTranscriptional repressionRecombinant Fusion ProteinsBiophysicsEnolaseCodon InitiatorDown-RegulationBiologyAlternative translationResponse ElementsTransfectionBiochemistryCell LineGene productHSPA4Proto-Oncogene Proteins c-mycStructural BiologyHSPA2GeneticsBiomarkers TumorE2F1AnimalsHumansSOCS6Genes Tumor SuppressorDNA bindingPromoter Regions GeneticMolecular BiologyYY1Tumor Suppressor ProteinsNuclear ProteinsCell BiologyDNAMolecular biologyGPS2Neoplasm ProteinsDNA-Binding ProteinsMolecular WeightRepressor ProteinsAlternative SplicingGATAD2BChromosomes Human Pair 1Phosphopyruvate HydrataseProtein BiosynthesisPeptidesProtein BindingFEBS letters
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Interaction of Mitogen-activated Protein Kinases with the Kinase Interaction Motif of the Tyrosine Phosphatase PTP-SL Provides Substrate Specificity …

1999

ERK1 and ERK2 associate with the tyrosine phosphatase PTP-SL through a kinase interaction motif (KIM) located in the juxtamembrane region of PTP-SL. A glutathione S-transferase (GST)-PTP-SL fusion protein containing the KIM associated with ERK1 and ERK2 as well as with p38/HOG, but not with the related JNK1 kinase or with protein kinase A or C. Accordingly, ERK2 showed in vitro substrate specificity to phosphorylate GST-PTP-SL in comparison with GST-c-Jun. Furthermore, tyrosine dephosphorylation of ERK2 by the PTP-SLDeltaKIM mutant was impaired. The in vitro association of ERK1/2 with GST-PTP-SL was highly stable; however, low concentrations of nucleotides partially dissociated the ERK1/2.P…

Cytoplasmanimal structuresProtein Kinase C-alphaRecombinant Fusion ProteinsCèl·lulesNerve Tissue ProteinsProtein tyrosine phosphataseMitogen-activated protein kinase kinaseTransfectionenvironment and public healthBiochemistrySH3 domainReceptor tyrosine kinaseMAP2K7Substrate SpecificitySerineAnimalsc-RafAmino Acid SequenceMolecular BiologyProtein Kinase CSequence DeletionMitogen-Activated Protein Kinase 1Binding SitesMitogen-Activated Protein Kinase 3biologyCyclin-dependent kinase 2Intracellular Signaling Peptides and ProteinsJNK Mitogen-Activated Protein KinasesCell BiologyCyclic AMP-Dependent Protein KinasesIsoenzymesenzymes and coenzymes (carbohydrates)KineticsBiochemistryAmino Acid SubstitutionCOS CellsCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedCyclin-dependent kinase 9CattleMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesProteïnes
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A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase

1999

Protein tyrosine phosphatase PTP-SL retains mitogen-activated protein (MAP) kinases in the cytoplasm in an inactive form by association through a kinase interaction motif (KIM) and tyrosine dephosphorylation. The related tyrosine phosphatases PTP-SL and STEP were phosphorylated by the cAMP-dependent protein kinase A (PKA). The PKA phosphorylation site on PTP-SL was identified as the Ser231 residue, located within the KIM. Upon phosphorylation of Ser231, PTP-SL binding and tyrosine dephosphorylation of the MAP kinases extracellular signal–regulated kinase (ERK)1/2 and p38α were impaired. Furthermore, treatment of COS-7 cells with PKA activators, or overexpression of the Cα catalytic subunit …

Cytoplasmanimal structuresRecombinant Fusion ProteinsCèl·lulesAmino Acid MotifsNerve Tissue ProteinsProtein tyrosine phosphataseSH2 domainTransfectionenvironment and public healthModels Biologicalp38 Mitogen-Activated Protein KinasesReceptor tyrosine kinaseSH3 domainCell LinePhosphoserinetyrosine phosphatasesAnimalsHumansProtein phosphorylationPKAReceptor-Like Protein Tyrosine Phosphatases Class 7PhosphorylationPTP-SLCell NucleusMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3biologyBrief ReportIntracellular Signaling Peptides and ProteinsBiological TransportCell BiologyProtein Tyrosine Phosphatases Non-ReceptorCyclic AMP-Dependent Protein KinasesEnzyme Activationenzymes and coenzymes (carbohydrates)MAP kinasesBiochemistryMitogen-activated protein kinaseCOS CellsMutationbiology.proteinPhosphorylationMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesEnzimssignal transductionProto-oncogene tyrosine-protein kinase Src
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T cells engineered to express a T-cell receptor specific for glypican-3 to recognize and kill hepatoma cells in vitro and in mice

2015

Background & Aims Cancer therapies are being developed based on our ability to direct T cells against tumor antigens. Glypican-3 (GPC3) is expressed by 75% of all hepatocellular carcinomas (HCC), but not in healthy liver tissue or other organs. We aimed to generate T cells with GPC3-specific receptors that recognize HCC and used them to eliminate GPC3-expressing xenograft tumors grown from human HCC cells in mice. Methods We used mass spectrometry to obtain a comprehensive peptidome from GPC3-expressing hepatoma cells after immune-affinity purification of human leukocyte antigen (HLA)-A2 and bioinformatics to identify immunodominant peptides. To circumvent GPC3 tolerance resulting from feta…

Cytotoxicity ImmunologicCancer Immunotherapy ; Immune Response ; Liver Cancer ; Tumor-associated AntigensCarcinoma HepatocellularTime FactorsCell SurvivalMice SCIDCD8-Positive T-LymphocytesBiologyLymphocyte ActivationTransfectionImmunotherapy AdoptiveInterferon-gammaInterleukin 21GlypicansHLA-A2 AntigenAnimalsHumansCytotoxic T cellIL-2 receptorAntigen-presenting cellInterleukin 3HepatologyImmunodominant EpitopesZAP70Liver NeoplasmsGastroenterologyDendritic CellsHep G2 CellsNatural killer T cellXenograft Model Antitumor AssaysMolecular biologyCoculture TechniquesGenes T-Cell ReceptorInterleukin 12FemaleGenetic Engineering
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Cytotoxic T lymphocytes define multiple peptide isoforms derived from the melanoma-associated antigen MART-1/Melan-A

1999

Peptides derived from the melanoma-associated MART-1/Melan-A antigen are currently implemented in immunotherapy for inducing or augmenting T-cell responses directed against peptides expressed by autologous tumor cells in HLA-A2+ patients with melanoma. Here, we describe the specificity of the T-cell clone SK29-FFM1.1, which secretes GM-CSF in response to a panel of synthetic MART-1/Melan-A-derived peptides, including the naturally presented ILTVILGVL32–40, but exhibits cytotoxicity and IFN-γ secretion exclusively to the MART-1/Melan-A derived peptide AAGIGILTV27–35. In addition, cytotoxic T-lymphocyte (CTL) clone SK29-FFM1.1 recognizes 3 different naturally processed and presented peptides …

Cytotoxicity ImmunologicCancer ResearchCellular immunityReceptors Antigen T-Cell alpha-betaT-Lymphocytesmedicine.medical_treatmentBiologyTransfectionEpitopeInterferon-gammaMART-1 AntigenImmune systemAntigenAntigens NeoplasmHLA-A2 AntigenTumor Cells CulturedmedicineHumansProtein IsoformsCytotoxic T cellAmino Acid SequenceMelanomaneoplasmsintegumentary systemReverse Transcriptase Polymerase Chain ReactionImmunotherapyMolecular biologyRecombinant ProteinsClone CellsNeoplasm ProteinsCTL*OncologyImmunologyClone (B-cell biology)T-Lymphocytes CytotoxicInternational Journal of Cancer
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Cloning and expression of the complement receptor glycoprotein C from Herpesvirus simiae (herpes B virus): protection from complement-mediated cell l…

2003

Simian herpes B virus (SHBV) is the herpes simplex virus (HSV) homologue for the species MACACA: Unlike in its natural host, and unlike other animal herpesviruses, SHBV causes high mortality in accidentally infected humans. SHBV-infected cells, like those infected with HSV-1 and equine herpesvirus types 1 and 4, express complement C3 receptor activity. To study immunoregulatory functions involved in susceptibility/resistance against interspecies transmission, the SHBV glycoprotein C (gC(SHBV)) gene (encoding 467 aa) was isolated. Sequence analysis revealed amino acid identity with gC proteins from HSV-2 (46.9 %), HSV-1 (44.5 %) and pseudorabies virus (21.2 %). Highly conserved cysteine resi…

Cytotoxicity ImmunologicHerpes B virusvirusesComplement Pathway AlternativeMolecular Sequence DataHerpesvirus 1 CercopithecineComplement receptorBiologyTransfectionmedicine.disease_causeVirusCell LineViral Envelope ProteinsVirologymedicineAnimalsHumansAmino Acid SequenceCloning MolecularPeptide sequenceSequence Analysis DNAbiology.organism_classificationVirologyComplement systemHerpes simplex virusCell cultureComplement C3bReceptors Complement 3bAlternative complement pathwayJournal of General Virology
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