Search results for "Isoforms"

showing 10 items of 185 documents

Hepatitis C Virus Core Protein Inhibits Tumor Suppressor Protein Promyelocytic Leukemia Function in Human Hepatoma Cells

2005

Abstract Tumor suppressor protein promyelocytic leukemia (PML) is implicated in apoptosis regulation and antiviral response. PML localizes predominantly to PML-nuclear bodies (PML-NB), nuclear macromolecular complexes regulating tumor suppressor protein p53 activity. Consistent with the function of PML in the cellular antiviral response, PML-NBs represent preferential targets in viral infections. In the case of hepatitis C virus (HCV) infection, important characteristics are nonresponsiveness to IFN therapy and development of hepatocellular carcinoma. However, the mechanisms which lead to the development of hepatocellular carcinoma are largely unknown. Here, we show that HCV core protein lo…

Cancer ResearchCarcinoma HepatocellularTumor suppressor genevirusesApoptosisPromyelocytic Leukemia ProteinBiologyTransfectionmedicine.disease_causePromyelocytic leukemia proteinCell Line TumorCoactivatormedicineHumansProtein IsoformsPhosphorylationCell NucleusTumor Suppressor ProteinsViral Core ProteinsLiver NeoplasmsNuclear Proteinsvirus diseasesAcetylationFas receptorHepatitis Cdigestive system diseasesNeoplasm ProteinsOncologyApoptosisAcetylationbiology.proteinCancer researchPhosphorylationTumor Suppressor Protein p53CarcinogenesisTranscription FactorsCancer Research
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Type I keratin cDNAs from the rainbow trout: independent radiation of keratins in fish

2002

Five different type I keratins from a teleost fish, the rainbow trout Oncorhynchus mykiss, have been sequenced by cDNA cloning and identified at the protein level by peptide mass mapping using MALDI-MS. This showed that the entire range of type I keratins detected biochemically in this fish has now been sequenced. Three of the keratins are expressed in the epidermis (subtype Ie), whereas the other two occur in simple epithelia and mesenchymal cells (subtype Is). Among the Is keratins is an ortholog of human K18; the second Is polypeptide is clearly distinct from K18. We raised a new monoclonal antibody (F1F2, subclass IgG1) that specifically recognizes trout Is keratins, with negative react…

Cancer ResearchDNA Complementaryanimal structuresType I keratinMolecular Sequence Datamacromolecular substancesBiologyPeptide MappingEvolution MolecularMesodermSpecies SpecificityAntibody SpecificityKeratinAnimalsHumansProtein IsoformsAmino Acid SequenceCloning MolecularMolecular BiologyZebrafishPhylogenyZebrafishMammalschemistry.chemical_classificationGeneticsMultiple sequence alignmentSequence Homology Amino Acidintegumentary systemPhylogenetic treeLampreyAntibodies MonoclonalLampreysEpithelial CellsCell Biologybiology.organism_classificationProtein Structure TertiaryTroutchemistryOrgan SpecificityOncorhynchus mykissSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationSharksKeratinsRainbow troutEpidermisSequence AlignmentDevelopmental BiologyDifferentiation
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The AC133 epitope, but not the CD133 protein, is lost upon cancer stem cell differentiation.

2010

Abstract Colon cancer stem cells (CSC) can be identified with AC133, an antibody that detects an epitope on CD133. However, recent evidence suggests that expression of CD133 is not restricted to CSCs, but is also expressed on differentiated tumor cells. Intriguingly, we observed that detection of the AC133 epitope on the cell surface decreased upon differentiation of CSC in a manner that correlated with loss of clonogenicity. However, this event did not coincide with a change in CD133 promoter activity, mRNA, splice variant, protein expression, or even cell surface expression of CD133. In contrast, we noted that with CSC differentiation, a change occured in CD133 glycosylation. Thus, AC133 …

Cancer ResearchGlycosylationGlycosylationCellular differentiationCellAC 133 EpitopeDown-RegulationMice SCIDEpitopechemistry.chemical_compoundEpitopesMiceCancer stem cellAntigens CDMice Inbred NODProminin-1medicineTumor Cells CulturedAnimalsHumansProtein IsoformsAC133 AntigenRNA MessengerPromoter Regions GeneticneoplasmsGlycoproteinsbiologyCell DifferentiationMolecular biologycarbohydrates (lipids)Gene Expression Regulation Neoplasticmedicine.anatomical_structureOncologychemistryembryonic structuresColonic Neoplasmsbiology.proteinNeoplastic Stem CellsAntibodyStem cellPeptidesCancer research
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Highly specific auto-antibodies against claudin-18 isoform 2 induced by a chimeric HBcAg virus-like particle vaccine kill tumor cells and inhibit the…

2011

Abstract Strategies for antibody-mediated cancer immunotherapy, such as active immunization with virus-like particle (VLP)-based vaccines, are gaining increasing attention. We developed chimeric hepatitis B virus core antigen (HBcAg)-VLPs that display a surface epitope of the highly selective tumor-associated cell lineage marker claudin-18 isoform 2 (CLDN18.2) flanked by a mobility-increasing linker. Auto-antibodies elicited by immunization with these chimeric HBcAg-VLPs in 2 relevant species (mouse and rabbit) bind with high precision to native CLDN18.2 at physiologic densities on the surface of living cells but not to the corresponding epitope of the CLDN18.1 splice variant that differs b…

Cancer ResearchHepatitis B virusLung Neoplasmsmedicine.medical_treatmentMolecular Sequence DataCHO CellsAdenocarcinomaActive immunizationCancer VaccinesEpitopeMiceCricetulusAntigenVirus-like particleCancer immunotherapyAntibody SpecificityStomach NeoplasmsCell Line TumorCricetinaemedicineAnimalsHumansProtein IsoformsAmino Acid SequenceVaccines Virus-Like ParticleAutoantibodiesMice Inbred BALB Cbiologybusiness.industryAntibody-Dependent Cell CytotoxicityMembrane ProteinsVirologyMolecular biologyHepatitis B Core AntigensHBcAgHEK293 CellsOncologyCell cultureClaudinsbiology.proteinRabbitsAntibodybusinessCancer research
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Claudin-18 splice variant 2 is a pan-cancer target suitable for therapeutic antibody development

2008

Abstract Purpose: Antibody-based cancer therapies have emerged as the most promising therapeutics in oncology. The purpose of this study was to discover novel targets for therapeutic antibodies in solid cancer. Experimental Design: We combined data mining and wet-bench experiments to identify strictly gastrocyte lineage–specific cell surface molecules and to validate them as therapeutic antibody targets. Results: We identified isoform 2 of the tight junction molecule claudin-18 (CLDN18.2) as a highly selective cell lineage marker. Its expression in normal tissues is strictly confined to differentiated epithelial cells of the gastric mucosa, but it is absent from the gastric stem cell zone. …

Cancer ResearchPathologymedicine.medical_specialtymicemedicine.drug_classMolecular Sequence DataGene ExpressionBiologyMonoclonal antibodyMalignant transformationAntigenmedicineProtein IsoformsAnimalsHumansNeoplasms Glandular and EpithelialMembrane Proteins/geneticsAntibodies Monoclonal/immunologyProtein Isoforms/immunologyBase SequenceReverse Transcriptase Polymerase Chain ReactionNeoplasms Glandular and Epithelial/drug therapyAntibodies MonoclonalImmunotherapy ActiveMembrane ProteinsCancermedicine.diseaseFlow CytometryImmunohistochemistryImmunotherapy Active/methodsOncologyCancer cellClaudinsbiology.proteinCancer researchImmunohistochemistryAntibodyStem cell
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Involvement of protein kinase Cdelta in contact-dependent inhibition of growth in human and murine fibroblasts.

2001

There is evidence that protein kinase C delta (PKCdelta) is a tumor suppressor, although its physiological role has not been elucidated so far. Since important anti-proliferative signals are mediated by cell-cell contacts we studied whether PKCdelta is involved in contact-dependent inhibition of growth in human (FH109) and murine (NIH3T3) fibroblasts. Cell-cell contacts were imitated by the addition of glutardialdehyde-fixed cells to sparsely seeded fibroblasts. Downregulation of the PKC isoforms alpha, delta, epsilon, and mu after prolonged treatment with 12-O-tetradecanoylphorbol-13-acetate (TPA, 0.1 microM) resulted in a significant release from contact-inhibition in FH109 cells. Bryosta…

Cancer ResearchTime FactorsBryostatin 1ImmunoprecipitationActive Transport Cell NucleusDown-RegulationBiologychemistry.chemical_compoundFixativesLactonesMiceDownregulation and upregulationGeneticsmedicineAnimalsHumansProtein IsoformsBenzopyransEnzyme InhibitorsFibroblastProtein kinase AMolecular BiologyProtein kinase CProtein Kinase CChemotaxisCell CycleAcetophenones3T3 CellsFibroblastsBryostatinsMolecular biologyBlotIsoenzymesProtein Kinase C-deltamedicine.anatomical_structurechemistryGlutaralTetradecanoylphorbol AcetateMacrolidesMitogensRottlerinCell DivisionProtein BindingOncogene
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Do not stress, just differentiate: role of stress proteins in hematopoiesis

2015

Hematopoiesis permits the constant regeneration of the blood system and is a permanent example of cell differentiation. Defects in its tight regulation can lead to either cell death or abnormal proliferation and may translate into multiple types of blood disorders, including leukemia. Heat shock proteins (HSPs), the expression of which is controlled by heat shock factors (HSFs, currently four known members),1 are a set of highly conserved proteins induced in response to a wide variety of physiological and environmental stress. HSP/HSF overexpression or mislocalization has been described in many cancers, particularly in hematology, and other diseases. Therefore, the involvement of HSFs/HSPs …

Cancer Researchmedicine.medical_specialtyCellular differentiationImmunologyBiologyMiceCellular and Molecular NeuroscienceHeat Shock Transcription FactorsInternal medicineHeat shock proteinmedicineAnimalsProtein IsoformsRNA MessengerHeat shockTranscription factorHeat-Shock ProteinsHematologyCell DifferentiationNews and CommentaryCell BiologyHematopoiesisCell biologyDNA-Binding ProteinsHeat shock factorHaematopoiesisCaspasesHSP60Heat-Shock ResponseTranscription FactorsCell Death & Disease
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Induction of apoptosis and inhibition of cell growth in human hepatocellular carcinoma cells by COX-2 inhibitors

2005

The aim of the present study was to examine the effects of nonselective (indomethacin) and selective cyclooxygenase-2 (COX-2) inhibitors (NS-398, nimesulide, and CAY10404) on cell growth, cell cycle distribution, and apoptosis in three human hepatocellular carcinoma cell lines (HepG2, HuH-6, and HA22T/VGH) with different characteristics of differentiation and biological behavior. The four COX inhibitors showed a dose-dependent growth-inhibitory effect in all the cell lines. No substantial arrests in the progression of the cells through the cell cycle were observed after treatment of HuH-6 or HA22T/VGH for 48 h with the various inhibitors. On the other hand, there were significant increases …

Carcinoma HepatocellularTime FactorsApoptosisPharmacologyBiologyGeneral Biochemistry Genetics and Molecular BiologyFlow cytometryInhibitory Concentration 50History and Philosophy of ScienceCell Line TumorCarcinomamedicineHumansProtein IsoformsCyclooxygenase InhibitorsEnzyme InhibitorsCell ProliferationCyclooxygenase 2 InhibitorsDose-Response Relationship DrugNeovascularization Pathologicmedicine.diagnostic_testReverse Transcriptase Polymerase Chain ReactionCell growthGeneral NeuroscienceAnti-Inflammatory Agents Non-SteroidalCell CycleMembrane Proteinsantineoplastic activity apoptosis cancer cell cultureCell cycleFlow Cytometrymedicine.diseaseCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesCell cultureApoptosisHepatocellular carcinomaNimesulidemedicine.drug
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Cloning of a rat-specific long PCP4/PEP19 isoform

2007

We report the identification of a cDNA that encodes a putative protein of 94 amino acids and expected molecular weight of 10.7 kDa, the C-terminal half of which is identical to that of PEP19, a small, brain-specific protein involved in Ca++/calmodulin signaling. The novel rat-specific protein, tentatively named long PEP19 isoform (LPI), is the product of alternative splicing of the rat PCP4 gene encoding PEP19. We found that antibodies raised against the first 13 N-terminal amino acids of LPI, not present in PEP19, recognize a protein enriched in the developing rat brain.

Cell ExtractsGene isoformProtein isoformDNA ComplementaryCalmodulinMolecular Sequence DataNerve Tissue ProteinsAntibodiesRats Sprague-DawleyMiceExonComplementary DNAGeneticsAnimalsHumansProtein IsoformsAmino Acid SequenceRNA MessengerCloning MolecularPeptide sequencechemistry.chemical_classificationBase SequencebiologyGene Expression ProfilingAlternative splicingBrainGene Expression Regulation DevelopmentalRNA-Binding ProteinsExonsGeneral MedicineMolecular biologyIntronsRatsAmino acidchemistryBiochemistrybiology.proteinCalmodulin-Binding ProteinsPeptidesInternational Journal of Molecular Medicine
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ALS-linked FUS mutations confer loss and gain of function in the nucleus by promoting excessive formation of dysfunctional paraspeckles

2019

Mutations in the FUS gene cause amyotrophic lateral sclerosis (ALS-FUS). Mutant FUS is known to confer cytoplasmic gain of function but its effects in the nucleus are less understood. FUS is an essential component of paraspeckles, subnuclear bodies assembled on a lncRNA NEAT1. Paraspeckles may play a protective role specifically in degenerating spinal motor neurons. However it is still unknown how endogenous levels of mutant FUS would affect NEAT1/paraspeckles. Using novel cell lines with the FUS gene modified by CRISPR/Cas9 and human patient fibroblasts, we found that endogenous levels of mutant FUS cause accumulation of NEAT1 isoforms and paraspeckles. However, despite only mild cytoplasm…

Cell NucleusResearchAmyotrophic Lateral SclerosisIntranuclear Inclusion BodiesNEAT1lcsh:RC346-429Cell LineLoss of Function MutationCell Line TumorFused in sarcoma (FUS)ParaspeckleHumansProtein IsoformsRNA-Binding Protein FUSRNA Long NoncodingAmyotrophic lateral sclerosis (ALS)CRISPR-Cas Systemslcsh:Neurology. Diseases of the nervous systemActa Neuropathologica Communications
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