Search results for "Signaling"

showing 10 items of 1125 documents

Exosomal Heat Shock Proteins as New Players in Tumour Cell-to-cell Communication

2014

Exosomes have recently been proposed as novel elements in the study of intercellular communication in normal and pathological conditions. The biomolecular composition of exosomes reflects the specialized functions of the original cells. Heat shock proteins (Hsps) are a group of chaperone proteins with diverse biological roles. In recent years, many studies have focused on the extracellular roles played by Hsps that appear to be involved in cancer development and immune system stimulation. Hsps localized on the surface of exosomes, secreted by normal and tumour cells, could be key players in intercellular cross-talk, particularly during the course of different diseases, such as cancer. Exoso…

Cell signalingBiochemistry (medical)Clinical BiochemistryCancerCell CommunicationBiologylcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensmedicine.diseaseExososomes HspsHeat Shock Proteinslcsh:RC254-282MicrovesiclesCell biologyExtracellular VesiclesImmune systemHeat shock proteinDrug deliveryExtracellularmedicineIntracellularextracellular vesicles; heat shock proteins; cell communicationJournal of Circulating Biomarkers
researchProduct

Relationship between signal transduction and PPAR alpha-regulated genes of lipid metabolism in rat hepatic-derived Fao cells.

2001

The goal of this study was to characterize phosphorylated proteins and to evaluate the changes in their phosphorylation level under the influence of a peroxisome proliferator (PP) with hypolipidemic activity of the fibrate family. The incubation of rat hepatic derived Fao cells with ciprofibrate leads to an overphosphorylation of proteins, especially one of 85 kDa, indicating that kinase (or phosphatase) activities are modified. Moreover, immunoprecipitation of 32P-labeled cell lysates shows that the nuclear receptor, PP-activated receptor, alpha isoform, can exist in a phosphorylated form, and its phosphorylation is increased by ciprofibrate. This study shows that PP acts at different step…

Cell signalingBiophysicsPeroxisome proliferator-activated receptorReceptors Cytoplasmic and NuclearBiologyBiochemistryCell LinemedicineAnimalschemistry.chemical_classificationKinaseLipid metabolismCell BiologyGeneral MedicineLipid MetabolismRatschemistryBiochemistryNuclear receptorGene Expression RegulationLiverPeroxisome proliferator-activated receptor alphaCiprofibrateSignal transductionmedicine.drugSignal TransductionTranscription FactorsCell biochemistry and biophysics
researchProduct

Risk Factors and Molecular Features Associated with Bladder Cancer Development

2017

Bladder cancer remains a global epidemiologic problem, with a strong male predominance and association with tobacco smoking. However, several other risk factors have also been associated with development of this disease, which is characterized by alterations in multiple molecular pathways. Development of the more prevalent, less aggressive, recurrent, noninvasive tumors is characterized by constitutive activation of the Ras–MAPK pathway. The less common but more aggressive invasive tumors, which have a higher mortality rate, are characterized by alterations in the p53 and retinoblastoma pathways. Alterations in pathways involved in cell-cycle regulation, apoptosis, cell signaling, angiogene…

Cell signalingBladder cancerRetinoblastomabusiness.industryAngiogenesisMortality rate030232 urology & nephrologyDiseaseCell cyclemedicine.diseaseBioinformatics03 medical and health sciences0302 clinical medicineApoptosis030220 oncology & carcinogenesismedicinebusiness
researchProduct

Microparticles: Modulators and biomarkers of liver disease

2012

Division of Molecular and Translational Medicine,Dept. of Medicine I, Johannes Gutenberg University, Mainz, GermanyEmerging role of microparticlesMicroparticles (MP) have gained increasing attention as biomark-ers for various diseases. First described as platelet dust, MP wereregarded as unspecific debris [1]. However, it has become appar-ent that cell derived MP or ectosomes represent a novel route ofhorizontal communication between cells. MP are between 100–1000 nm in size and generated through cell membrane shedding(ectocytosis), a process that can be triggered by the activation ofthe complement C5b-9 complex, as shown for platelet derivedMP, or by inhibition of flippase activitythroughCa

Cell signalingCD14+MacrophageT cellCellApoptosisCell CommunicationBiologyMonocyteExosomeAnnexin VCD4+Cell membraneCell-Derived MicroparticlesmedicineHumansMacrophageEctosomeCD41+InflammationHepatologyLiver DiseasesMonocytePlateletNASHT cellBiomarkerDendritic cellCD8+FibrosisHepatitis CCell biologyExosomemedicine.anatomical_structureLiverMicroparticleBiochemistryNAFLiNKTBiomarkersDendritic cellJournal of Hepatology
researchProduct

Extracellular Vesicles from Neural Stem Cells Transfer IFN-γ via Ifngr1 to Activate Stat1 Signaling in Target Cells

2014

The idea that stem cell therapies work only via cell replacement is challenged by the observation of consistent intercellular molecule exchange between the graft and the host. Here we defined a mechanism of cellular signaling by which neural stem/precursor cells (NPCs) communicate with the microenvironment via extracellular vesicles (EVs), and we elucidated its molecular signature and function. We observed cytokine-regulated pathways that sort proteins and mRNAs into EVs. We described induction of interferon gamma (IFN-γ) pathway in NPCs exposed to proinflammatory cytokines that is mirrored in EVs. We showed that IFN-γ bound to EVs through Ifngr1 activates Stat1 in target cells. Finally, we…

Cell signalingCell CommunicationBiologyArticle3T3 cellsProinflammatory cytokineInterferon-gammaMiceTh2 CellsNeural Stem CellsPrecursor cellmedicineAnimalsInterferon gammaRNA MessengerTransport VesiclesMolecular BiologyReceptors InterferonInflammationBiological Transport3T3 CellsCell BiologyTh1 CellsNeural stem cellCell biologySTAT1 Transcription Factormedicine.anatomical_structureCellular MicroenvironmentSignal transductionStem cellSignal Transductionmedicine.drugMolecular Cell
researchProduct

Heat shock protein 10 and signal transduction: a “capsula eburnea” of carcinogenesis?

2006

To date, little is known either about the physical interactions of heat shock protein 10 (Hsp10) with other proteins within the cell or its involvement in signal transduction pathways. Hsp10 has been considered mainly as a partner of Hsp60 in the Hsp60/10 protein folding machine. Only recently, Hsp10 was reported to interact with proteins involved in deoxyribonucleic acid checkpoint inactivation, termination of M-phase, messenger ribonucleic acid export, import of nuclear proteins, nucleocytoplasmic transport, and pheromone signaling pathways. At the same time, Hsp10 expression can be up-regulated in cancer cells, because it accumulates as the cell transformation progresses. Recent data sug…

Cell signalingColonCellular differentiationApoptosisChaperonin 60Cell BiologyBiologyCell cycleBiochemistryCell biologyFungal ProteinsBiochemistryHsp10 carcinogenesisNucleocytoplasmic TransportNeoplasmsHeat shock proteinColonic NeoplasmsChaperonin 10HumansHSP60MinireviewNuclear proteinSignal transductionSignal Transduction
researchProduct

The translocation of signaling molecules in dark adapting mammalian rod photoreceptor cells is dependent on the cytoskeleton.

2008

In vertebrate rod photoreceptor cells, arrestin and the visual G-protein transducin move between the inner segment and outer segment in response to changes in light. This stimulus dependent translocation of signalling molecules is assumed to participate in long term light adaptation of photoreceptors. So far the cellular basis for the transport mechanisms underlying these intracellular movements remains largely elusive. Here we investigated the dependency of these movements on actin filaments and the microtubule cytoskeleton of photoreceptor cells. Co-cultures of mouse retina and retinal pigment epithelium were incubated with drugs stabilizing and destabilizing the cytoskeleton. The actin a…

Cell signalingCytochalasin Dgenetic structuresLightPaclitaxelPhalloidineDark AdaptationBiologyHeterocyclic Compounds 4 or More RingsMicrotubulesRetinaMiceStructural BiologyMicrotubuleRetinal Rod Photoreceptor CellsCytoskeletal drugsThiabendazolemedicineArrestinAnimalsTransducinCytoskeletonMicroscopy ImmunoelectronActinCytoskeletonVision OcularMice KnockoutRetinal pigment epitheliumArrestinHomozygoteCell BiologyDarknessRod Cell Outer Segmenteye diseasesActinsCell biologyMice Inbred C57BLActin CytoskeletonProtein Transportmedicine.anatomical_structureMicroscopy Fluorescencesense organsTransducinCell Migration AssaysSignal TransductionCell motility and the cytoskeleton
researchProduct

Molecular evolution of the metazoan extracellular matrix: cloning and expression of structural proteins from the demosponges Suberites domuncula and …

2000

One crucial event during evolution to multicellularity was the development of either direct cell–cell contact or indirect interaction via extracellular matrix (ECM) molecules. The identification of those polypeptides provides conclusive data on the phylogenetic relationship of metazoan phyla and helps us to understand the position of the Metazoa among the other kingdoms. Recently it became evident that the ECM of sponges is amazingly complex; it is composed of fibrous molecules, e.g., collagen, and their corresponding receptors, which are highly similar to those existing in other metazoan phyla. While these data already support the view of monophyly of Metazoa, additional studies are requir…

Cell signalingDNA ComplementaryDermatopontinMolecular Sequence DataGene ExpressionBiologyBioinformaticsTransplantation AutologousExtracellular matrixEvolution MolecularMyotrophinGeneticsAnimalsAmino Acid SequenceCloning MoleculareducationGrowth SubstancesMolecular BiologyPeptide sequenceEcology Evolution Behavior and SystematicsPhylogenyCell Aggregationeducation.field_of_studyExtracellular Matrix ProteinsBase SequenceSequence Homology Amino AcidReceptor Protein-Tyrosine Kinasesbiology.organism_classificationRecombinant ProteinsCell biologyPoriferaSuberites domunculaTransplantationChondroitin Sulfate ProteoglycansIntercellular Signaling Peptides and ProteinsCollagenCarrier ProteinsCell Adhesion MoleculesFunction (biology)Journal of molecular evolution
researchProduct

Comparative analysis of virtual screening approaches in the search for novel EphA2 receptor antagonists

2015

The EphA2 receptor and its ephrin-A1 ligand form a key cell communication system, which has been found overexpressed in many cancer types and involved in tumor growth. Recent medicinal chemistry efforts have identified bile acid derivatives as low micromolar binders of the EphA2 receptor. However, these compounds suffer from poor physicochemical properties, hampering their use in vivo. The identification of compounds able to disrupt the EphA2-ephrin-A1 complex lacking the bile acid scaffold may lead to new pharmacological tools suitable for in vivo studies. To identify the most promising virtual screening (VS) protocol aimed at finding novel EphA2 antagonists, we investigated the ability of…

Cell signalingDatabases Pharmaceuticaldrug designPharmaceutical ScienceComputational biologyBiologyCrystallography X-RayMolecular Docking SimulationArticleAnalytical Chemistrylcsh:QD241-441Structure-Activity RelationshipUser-Computer Interfacelcsh:Organic chemistryPPI inhibitorsDrug Discoveryshape screeningStructure–activity relationshipPhysical and Theoretical ChemistryReceptorProtein Kinase InhibitorsVirtual screeningMolecular StructureDrug discoveryReceptor EphA2EphA2 antagonistOrganic ChemistryEphrin-A1virtual screeningEPH receptor A2C700Combinatorial chemistryMolecular Docking SimulationUniPR129Chemistry (miscellaneous)Docking (molecular)dockingMolecular Medicinepharmacophore search
researchProduct

α-Secretase Activity of the Disintegrin Metalloprotease ADAM 10: Influences of Domain Structure

2001

Disintegrin metalloproteases from different organisms form the ADAM (a disintegrin and metalloprotease) family. All members display a common domain organization and possess four potential functions: proteolysis, cell adhesion, cell fusion, and cell signaling. Members of the ADAM family are responsible for the proteolytic cleavage of transmembrane proteins and release of their extracellular domain. The proteolytic process is referred to as ectodomain shedding, which is activated by phorbol esters and inhibited by hydroxamic acid-based inhibitors. We have shown that the disintegrin metalloprotease ADAM 10 has both constitutive and regulated alpha-secretase activity. Expression of a dominant n…

Cell signalingDisintegrinsMolecular Sequence DataProtein domainBiologyGeneral Biochemistry Genetics and Molecular BiologyADAM10 ProteinAmyloid beta-Protein PrecursorHistory and Philosophy of ScienceEndopeptidasesDisintegrinAnimalsAspartic Acid EndopeptidasesHumansProtease InhibitorsAmino Acid SequenceCell adhesionMetalloproteinaseGeneral NeuroscienceHEK 293 cellsMembrane ProteinsMetalloendopeptidasesRecombinant ProteinsTransmembrane proteincarbohydrates (lipids)ADAM ProteinsBiochemistryEctodomainbiology.proteinAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalAnnals of the New York Academy of Sciences
researchProduct