Search results for "Signaling."

showing 10 items of 1102 documents

Polarity factor 'Frizzled' in the demosponge Suberites domuncula: identification, expression and localization of the receptor in the epithelium/pinac…

2003

Until recently, it was assumed that polarity and axis formation have evolved only in metazoan phyla higher than Cnidaria. One key molecule involved in the signal transduction causing tissue polarity is Frizzled, a seven-transmembrane receptor that is activated by the Wnt family of secreted proteins. We report the isolation and characterization of a Frizzled gene from the demosponge Suberites domuncula (Sd-Fz). The deduced polypeptide comprises all characteristic domains known from Frizzled receptors of higher metazoans. In situ hybridization studies show that Sd-Fz is expressed in cells close to the surface of the sponges and in the pinacocytes of some canals. Northern blot analysis demonst…

FrizzledMolecular Sequence DataBiophysicsPinacodermReceptors Cell SurfaceBiochemistryEpitheliumDemospongeStructural BiologyGeneticsAnimalsNorthern blotAmino Acid SequenceMolecular BiologyIn Situ HybridizationPhylogenyCell AggregationbiologySequence Homology Amino AcidWnt signaling pathwayCell BiologyAnatomybiology.organism_classificationBlotting NorthernCell biologyPoriferaProtein Structure TertiaryUp-RegulationSuberites domunculaSpongeSignal transductionSignal TransductionFEBS letters
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Isolation and characterization of Wnt pathway-related genes from Porifera.

2006

The Wnt signal acts by binding to Frizzled receptors, with the subsequent activation of two different signal transduction cascades, the canonical and the non-canonical Wnt pathways, involved in cell growth, differentiation, migration and fate. The canonical pathway functions through the translocation of beta-catenin to the nucleus and the activation of TCF/LEF transcription factors; it plays an important role in developmental patterning and cell fate decisions during embryogenesis. The non-canonical Wnt pathway is responsible for the planar cell polarity process in invertebrates, and for the convergent-extension movements during vertebrate gastrulation. The final effect of the non-canonical…

FrizzledMyosin Light ChainsMolecular Sequence DataGTPaseCell fate determinationGlycogen Synthase Kinase 3AnimalsAmino Acid Sequencecdc42 GTP-Binding ProteinCells CulturedPhylogenybiologyGene Expression ProfilingWnt signaling pathwayIntracellular Signaling Peptides and ProteinsLRP6LRP5Cell BiologyGeneral Medicinebiology.organism_classificationFrizzled ReceptorsCell biologyPoriferaSuberites domunculaWnt ProteinsGene Expression RegulationSignal transductionTCF Transcription FactorsrhoA GTP-Binding ProteinCell biology international
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Regional and modular expression of morphogenetic factors in the demosponge Lubomirskia baicalensis

2008

Some sponges [phylum Porifera], e.g. the demosponges Lubomirskia baicalensis or Axinella polypoides, show an arborescent growth form. In the freshwater sponge L. baicalensis this morphotype is seen mostly in depths below 4 m while in more shallow regions it grows as a crust. The different growth forms are determined in nature very likely by water current and/or light. The branches of this species are composed of modules, arranged along the apical-basal axis. The modules are delimited by a precise architecture of the spicule bundles; longitudinal bundles originate from the apex of the earlier module, while at the basis of each module these bundles are cross-linked by traverse bundles under f…

FrizzledSpiculeMolecular Sequence DataGeneral Physics and AstronomyMyotrophinDemospongeStructural BiologyEpidermal growth factorBotanyMorphogenesisAnimalsGeneral Materials ScienceAmino Acid SequenceeducationGeneeducation.field_of_studyEpidermal Growth FactorbiologyReverse Transcriptase Polymerase Chain ReactionWnt signaling pathwayCell BiologyBlotting Northernbiology.organism_classificationFrizzled ReceptorsPoriferaCell biologySpongeIntercellular Signaling Peptides and ProteinsMicron
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Galectin-3 Impairment of MYCN-Dependent Apoptosis-Sensitive Phenotype Is Antagonized by Nutlin-3 in Neuroblastoma Cells

2012

MYCN amplification occurs in about 20-25% of human neuroblastomas and characterizes the majority of the high-risk cases, which display less than 50% prolonged survival rate despite intense multimodal treatment. Somehow paradoxically, MYCN also sensitizes neuroblastoma cells to apoptosis, understanding the molecular mechanisms of which might be relevant for the therapy of MYCN amplified neuroblastoma. We recently reported that the apoptosis-sensitive phenotype induced by MYCN is linked to stabilization of p53 and its proapoptotic kinase HIPK2. In MYCN primed neuroblastoma cells, further activation of both HIPK2 and p53 by Nutlin-3 leads to massive apoptosis in vitro and to tumor shrinkage an…

Galectin 3Cancer TreatmentGene Dosagelcsh:MedicineApoptosisProtein-Serine-Threonine KinaseBiochemistryPiperazineschemistry.chemical_compoundNeuroblastoma0302 clinical medicineMolecular Cell BiologyBasic Cancer ResearchSignaling in Cellular Processeslcsh:ScienceEnergy-Producing OrganellesApoptotic SignalingNuclear ProteinOncogene Proteins0303 health sciencesN-Myc Proto-Oncogene ProteinMultidisciplinaryCell DeathImidazolesOncogene ProteinNuclear ProteinsTransfectionNutlin3. Good healthGene Expression Regulation NeoplasticProtein TransportCell killingPhenotypeOncologyGalectin-3030220 oncology & carcinogenesisGene Knockdown TechniquesMedicineResearch ArticleSignal TransductionHumanBiologyBioenergeticsProtein Serine-Threonine KinasesN-Myc Proto-Oncogene ProteinModels Biological03 medical and health sciencesNeuroblastomaCell Line TumormedicineHumansBiologyImidazolePiperazineneoplasms030304 developmental biologylcsh:RGene AmplificationChemotherapy and Drug Treatmentmedicine.diseasechemistryCell cultureApoptosisPediatric OncologyCytoprotectionGene Knockdown TechniqueCancer researchlcsh:QTumor Suppressor Protein p53Carrier ProteinsCarrier ProteinDNA Damage
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Oxidative stress inhibits IFN-α-induced antiviral gene expression by blocking the JAK–STAT pathway

2006

Abstract BACKGROUND/AIMS: Unresponsiveness to IFN-alpha is common in chronic hepatitis C. Since conditions associated with an increased oxidative stress (advanced age, steatosis, fibrosis, iron overload, and alcohol consumption) reduce the likelihood of response, we hypothesized that oxidative stress may affect the antiviral actions of IFN-alpha. METHODS: We examined in a human hepatocellular carcinoma cell line (Huh-7) the effect of hydrogen peroxide (H2O2), as a generator of oxidative stress, on the IFN-alpha signaling pathway. RESULTS: Pretreatment of Huh-7 cells with 0.5-1 mM H2O2 resulted in the suppression of the IFN-alpha-induced antiviral protein MxA and of IRF-9 mRNA expression. Th…

Gene Expression Regulation ViralMyxovirus Resistance ProteinsCarcinoma HepatocellularBlotting WesternAntiviral proteinProtein tyrosine phosphataseInterferon alpha-2Biologymedicine.disease_causechemistry.chemical_compoundGTP-Binding ProteinsCell Line TumormedicineHumansRNA NeoplasmHepatologyTyk-2Reverse Transcriptase Polymerase Chain ReactionSTATLiver NeoplasmsInterferon-alphaJAK-STAT signaling pathwayTyrosine phosphorylationHydrogen PeroxideJanus Kinase 1Flow CytometryInterferon-Stimulated Gene Factor 3 gamma SubunitRecombinant ProteinsIFN-aJAK-1Oxidative StressSTAT Transcription FactorsHydrogen peroxide; IFN-a; STAT; JAK-1; Tyk-2chemistryImmunologySTAT proteinCancer researchSignal transductionTyrosine kinaseOxidative stressSignal TransductionJournal of Hepatology
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Epigenetic modifiers are necessary but not sufficient for reprogramming non-myelinating cells into myelin gene-expressing cells.

2010

Background Modifications on specific histone residues and DNA methylation play an essential role in lineage choice and cellular reprogramming. We have previously shown that histone modifications or combinatorial codes of transcription factors (TFs) are critical for the differentiation of multipotential progenitors into myelinating oligodendrocytes. In this study we asked whether combining global manipulation of DNA methylation and histone acetylation together with the expression of oligodendrocyte- specific TFs, was sufficient to switch the identity of fibroblasts into myelin gene-expressing cells. Methodology/Principal Findings Transfection of six oligodendrocyte-specific TFs (Olig1, Olig2…

Gene Expressionlcsh:MedicineBiologyCell LineEpigenesis GeneticHistones03 medical and health sciencesMice0302 clinical medicineHistone H1Histone methylationHistone H2ANeuroscience/Neuronal Signaling MechanismsHistone codeAnimalsCell Lineagelcsh:ScienceCells Cultured030304 developmental biologyEpigenomics0303 health sciencesMultidisciplinaryNeuroscience/Neuronal and Glial Cell BiologyMultipotent Stem Cellslcsh:RAcetylationCell DifferentiationDNA MethylationFibroblastsMolecular biologyChromatinChromatinRatsOligodendrogliaHomeobox Protein Nkx-2.2Histone methyltransferaseNIH 3T3 Cellslcsh:QNeuroscience/Neurobiology of Disease and RegenerationChromatin immunoprecipitation030217 neurology & neurosurgeryMyelin ProteinsResearch ArticleNeuroscienceTranscription FactorsPLoS ONE
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RSPO2 gene rearrangement: a powerful driver of β-catenin activation in liver tumours

2019

ObjectiveWe aimed at the identification of genetic alterations that may functionally substitute for CTNNB1 mutation in ß-catenin-activated hepatocellular adenomas (HCAs) and hepatocellular carcinoma (HCC).DesignLarge cohorts of HCA (n=185) and HCC (n=468) were classified using immunohistochemistry. The mutational status of the CTNNB1 gene was determined in ß-catenin-activated HCA (b-HCA) and HCC with at least moderate nuclear CTNNB1 accumulation. Ultra-deep sequencing was used to characterise CTNNB1wild-type and ß-catenin-activated HCA and HCC. Expression profiling of HCA subtypes was performed.ResultsA roof plate-specific spondin 2 (RSPO2) gene rearrangement resulting from a 46.4 kb microd…

Gene expression profilingGastroenterologyCancer researchWnt signaling pathwayTelomerase reverse transcriptaseGene rearrangementHCCSBiologyRSPO2Malignant transformationRSPO2 GeneGut
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New perspectives on the renal slit diaphragm protein podocin.

2011

Podocin is a critical component of the glomerular filtration barrier, its mutations causing recessive steroid-resistant nephrotic syndrome. A GenBank analysis of the human podocin (NPHS2) gene resulted in the possible existence of a new splice variant of podocin in the kidney, missing the in-frame of exon 5, encoding the prohibitin homology domain. Using RT–polymerase chain reaction and immunoblotting followed by sequence analysis, we are for the first time able to prove the expression of a novel podocin isoform (isoform 2), exclusively and constitutively expressed in human podocytes. Furthermore, we reveal singular extrarenal podocin expression in human and murine testis. Our data show the…

Gene isoformAdultMalePathologymedicine.medical_specialtyendocrine systemkidneySertoli cellsBlotting WesternImmunoblottingMolecular Sequence Datatestisurologic and male genital diseasesReal-Time Polymerase Chain ReactionFilamentous actinPathology and Forensic MedicineSertoli cell-only syndromeMiceYoung AdultmedicineAnimalsHumansProtein IsoformsSertoli cell-only syndromeAmino Acid SequenceProhibitinAgedKidneyMicroscopy ConfocalbiologyBase Sequenceurogenital systemPodocytesGene Expression ProfilingIntracellular Signaling Peptides and ProteinsMembrane ProteinsisoformMiddle Agedmedicine.diseaseSertoli cellfemale genital diseases and pregnancy complicationsWT-1medicine.anatomical_structureSlit diaphragmPodocinbiology.proteinOriginal ArticlepodocinModern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc
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Interaction mechanism of endogenous PP2A inhibitor protein ENSA with PP2A

2022

The vast diversity of protein phosphatase 2A (PP2A) holoenzyme composition ensures its multifaceted role in the regulation of cellular growth and signal transduction. In several pathological conditions, such as cancer, PP2A is inhibited by endogenous inhibitor proteins. Several PP2A inhibitor proteins have been identified, one of which is α-endosulfine (ENSA). ENSA inhibits PP2A activity when it is phosphorylated at Ser67 by Greatwall (Gwl) kinase. The role of ENSA in PP2A inhibition is rather well characterized, but knowledge of the mechanism of inhibition is scarce. In this study, we have performed comprehensive structural characterization of ENSA, and its interaction with PP2A A- and var…

Gene isoformMitosisEndogenymacromolecular substancesProtein Serine-Threonine KinasesPP2A inhibitor protein010402 general chemistry01 natural sciencesBiochemistryenvironment and public health03 medical and health sciencesX-Ray DiffractionNeoplasmsScattering Small AngleHumansProtein Phosphatase 2DPsPhosphorylationNMR-spektroskopiaMolecular BiologyNuclear Magnetic Resonance Biomolecular030304 developmental biologyinhibiittoritsoluviestintä0303 health sciencesChemistryKinaseCell growthCell CycleCell BiologyProtein phosphatase 2Inhibitor proteinSAXSPhosphoproteinsNMR3. Good health0104 chemical sciencesCell biologyPP2Aenzymes and coenzymes (carbohydrates)ENSAPhosphorylationIntercellular Signaling Peptides and ProteinsproteiinitSignal transductionMicrotubule-Associated ProteinsProtein Processing Post-TranslationalSignal TransductionFEBS Journal
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The b1 isoform of protocadherin-gamma (Pcdhgamma) interacts with the microtubule-destabilizing protein SCG10.

2004

Due to their structural characteristics and their diversity, the 22 members of the protocadherin-gamma (Pcdhgamma) family have been suggested to contribute to the establishment of specific connections in the nervous system. Here, we focus on a single isoform, Pcdhgamma-b1. Its expression is found in different brain regions and in developing spinal cord it is restricted to scattered cells, whereas all cells are labeled using an antibody that recognizes all Pcdhgamma isoforms. As a first step to understanding the signaling mechanisms downstream of Pcdhgamma, we identify the microtubule-destabilizing protein SCG10 as a cytoplasmic interactor for Pcdhgamma-b1 and other isoforms of the Pcdhgamma…

Gene isoformNervous systemSubfamilyRecombinant Fusion ProteinsBiophysicsTwo-hybridProtocadherinCadherin Related ProteinsBiologyBiochemistryMicrotubulesMiceProtocadherinStructural BiologyMicrotubuleTwo-Hybrid System TechniquesChlorocebus aethiopsGeneticsmedicineAnimalsProtein IsoformsInteractorNerve Growth FactorsGrowth coneMolecular BiologyNeuronsProtocadherin-gammaCalcium-Binding ProteinsIntracellular Signaling Peptides and ProteinsBrainCell BiologySCGIOCadherinsMolecular biologyCell biologySCG10medicine.anatomical_structureCytoplasmCOS CellsStathminGrowth coneSignal TransductionFEBS letters
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