Search results for "CYTOKINES"

showing 10 items of 845 documents

The Abundant Tegument Protein pUL25 of Human Cytomegalovirus Prevents Proteasomal Degradation of pUL26 and Supports Its Suppression of ISGylation

2018

The tegument of human cytomegalovirus (HCMV) virions contains proteins that interfere with both the intrinsic and the innate immunity. One protein with a thus far unknown function is pUL25. The deletion of pUL25 in a viral mutant (Towne-ΔUL25) had no impact on the release of virions and subviral dense bodies or on virion morphogenesis. Proteomic analyses showed few alterations in the overall protein composition of extracellular particles. A surprising result, however, was the almost complete absence of pUL26 in virions and dense bodies of Towne-ΔUL25 and a reduction of the large isoform pUL26-p27 in mutant virus-infected cells. pUL26 had been shown to inhibit protein conjugation with the in…

Proteomics0301 basic medicineIntrinsic immunityHuman cytomegalovirusImmunoprecipitationvirusesImmunologyMutantCytomegalovirusBiologyVirus ReplicationMicrobiologyViral Matrix ProteinsViral Proteins03 medical and health sciencesInterferonVirologymedicineHumansUbiquitinsCells CulturedInnate immune systemvirus diseasesViral tegumentFibroblastsbiochemical phenomena metabolism and nutritionPhosphoproteinsmedicine.diseaseISG15Immunity InnateVirus-Cell InteractionsCell biology030104 developmental biologyInsect ScienceMutationProteolysisCytokinesmedicine.drugJournal of Virology
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In Vitro Phenotypic, Genomic and Proteomic Characterization of a Cytokine-Resistant Murine β-TC3 Cell Line

2012

Type 1 diabetes mellitus (T1DM) is caused by the selective destruction of insulin-producing β-cells. This process is mediated by cells of the immune system through release of nitric oxide, free radicals and pro-inflammatory cytokines, which induce a complex network of intracellular signalling cascades, eventually affecting the expression of genes involved in β-cell survival. The aim of our study was to investigate possible mechanisms of resistance to cytokine-induced β-cell death. To this purpose, we created a cytokine-resistant β-cell line (β-TC3R) by chronically treating the β-TC3 murine insulinoma cell line with IL-1β + IFN-γ. β-TC3R cells exhibited higher proliferation rate and resistan…

ProteomicsAnatomy and Physiologymedicine.medical_treatmentCell Culture Techniqueslcsh:MedicineApoptosisSettore MED/13 - EndocrinologiaMiceEndocrinologyImmune PhysiologyInsulin-Secreting CellsMolecular Cell BiologySOCS3lcsh:ScienceMultidisciplinaryCell DeathDiabetes mellitus cytokines. apoptosis SUMO4 NF-kBCell CycleNF-kappa BGenomicsCell cycleImmunohistochemistryCell biologyPhenotypeCytokineMedicineCytokinesResearch ArticleProgrammed cell deathCell SurvivalImmunologyDown-RegulationBiologyAutoimmune DiseasesCell LineDownregulation and upregulationmedicineAnimalsGene SilencingBiologyCell ProliferationDiabetic EndocrinologyEndocrine PhysiologyCell growthlcsh:RCell cultureApoptosisImmune SystemClinical ImmunologyInsulinomalcsh:QPLoS ONE
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The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10

2012

The in vivo roles of meprin metalloproteases in pathophysiological conditions remain elusive. Substrates define protease roles. Therefore, to identify natural substrates for human meprin α and β we employed TAILS (terminal amine isotopic labeling of substrates), a proteomics approach that enriches for N-terminal peptides of proteins and cleavage fragments. Of the 151 new extracellular substrates we identified, it was notable that ADAM10 (a disintegrin and metalloprotease domain-containing protein 10)—the constitutive α-secretase—is activated by meprin β through cleavage of the propeptide. To validate this cleavage event, we expressed recombinant proADAM10 and after preincubation with meprin…

Proteomicsalpha-2-HS-Glycoproteinmedicine.medical_treatmentADAM10ADAM10 ProteinMice0302 clinical medicine610 Medicine & healthMice KnockoutExtracellular Matrix Proteins0303 health sciencesMetalloproteinaseDegradomeMetalloendopeptidasesMeprinADAM10Terminal amine isotopic labeling of substratesADAM ProteinsElafinBiochemistryTAILSCytokinesMolecular MedicineElafinResearch Article610 Medicine & healthBiologyCell Line03 medical and health sciencesCellular and Molecular NeurosciencemedicineDisintegrinAnimalsHumansAmino Acid SequenceCystatin CMolecular Biology030304 developmental biologyPharmacologyProteaseMeprin; ADAM10; Metalloproteases; Proteomics; TAILS; DegradomeMembrane ProteinsCell BiologyADAM ProteinsHEK293 CellsMembrane proteinbiology.proteinMetalloproteases570 Life sciences; biologyAmyloid Precursor Protein SecretasesCaco-2 Cells030217 neurology & neurosurgery
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Soot-exposed mononuclear cells increase inflammatory cytokine mRNA expression and protein secretion in cocultured bronchial epithelial cells.

2000

<i>Background:</i> Soot particles are air pollutants capable of inducing airway and lung parenchymal injury. Mononuclear and bronchial epithelial cells are central to the maintenance of homeostasis and inflammation in the airways. <i>Objectives:</i> The aim of this study was to evaluate the contribution of mononuclear cells to the release of inflammatory mediators by bronchial epithelial cells. <i>Methods:</i> To model the in vivo situation, an in vitro system of cocultured blood monocytes and BEAS-2B cells was established in a transwell system. Blood monocytes were exposed to soot particles (FR 101) at concentrations of up to 100 μg/10<sup>6</su…

Pulmonary and Respiratory MedicineAdultMaleInflammationBronchiEnzyme-Linked Immunosorbent AssayBiologycomplex mixturesPeripheral blood mononuclear cellSensitivity and SpecificityMonocytesAir pollutantsParenchymamedicineHumansRNA MessengerSoot particlesCells CulturedAir PollutantsLungInterleukin-6Reverse Transcriptase Polymerase Chain ReactionInterleukin-8Epithelial CellsBlood Proteinsrespiratory systemCarbonCoculture Techniquesrespiratory tract diseasesCell biologymedicine.anatomical_structureSecretory proteinCytokinesCytokine mrnaFemalemedicine.symptomInflammation MediatorsRespiration; international review of thoracic diseases
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Epithelial-mesenchymal communication in the pathogenesis of chronic asthma.

2005

Although Th-2-mediated inflammation is a key therapeutic target in asthma, its relationship to altered structure and functions of the airways is largely unknown. In addition to inflammation, asthma is a disorder involving the airway epithelium that is more vulnerable to environmental injury and responds to this by impaired healing. This establishes a chronic wound scenario that is capable of sustaining chronic inflammation as well as remodeling. This response occurs as a consequence of activation of the epithelial-mesenchymal unit, involving reciprocal activities of growth factors belonging to the fibroblast growth factor, epidermal growth factor, and transforming growth factor-beta familie…

Pulmonary and Respiratory MedicineChronic woundInflammationBiologyFibroblast growth factorPathogenesisTh2 CellsEpidermal growth factormedicineHumansGrowth Substancesasthma InflammationAsthmaInflammationWound HealingMesenchymal stem cellModels ImmunologicalEpithelial CellsMuscle SmoothFibroblastsmedicine.diseaseAsthmarespiratory tract diseasesImmunologyChronic DiseaseRespiratory Physiological PhenomenaRespiratory epitheliumCytokinesmedicine.symptom
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Molecular Mechanisms Leading from Periodontal Disease to Cancer

2022

Periodontitis is prevalent in half of the adult population and raises critical health concerns as it has been recently associated with an increased risk of cancer. While information about the topic remains somewhat scarce, a deeper understanding of the underlying mechanistic pathways promoting neoplasia in periodontitis patients is of fundamental importance. This manuscript presents the literature as well as a panel of tables and figures on the molecular mechanisms of Porphyromonas gingivalis and Fusobacterium nucleatum, two main oral pathogens in periodontitis pathology, involved in instigating tumorigenesis. We also present evidence for potential links between the RANKL–RANK signaling axi…

QH301-705.5periodontal diseaseReviewOdontologi<i>Porphyromonas gingivalis</i>Catalysisimmune responseInorganic ChemistrycancerHumansBiology (General)Physical and Theoretical ChemistryImmune responseQD1-999Molecular BiologySpectroscopyPeriodontal DiseasesCancerCancer och onkologiRANK ligandFusobacterium nucleatumReceptor Activator of Nuclear Factor-kappa B<i>Fusobacterium nucleatum</i>Organic ChemistryGeneral MedicineComputer Science ApplicationsChemistrytumorigenesisGene Expression RegulationDentistryCancer and OncologyTumorigenesisDisease ProgressionCytokinesMouth NeoplasmsPeriodontal diseasePorphyromonas gingivalisSignal Transduction
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p38α deficiency and oxidative stress cause cytokinesis failure in hepatocytes.

2015

Cytokinesis is the last step in mitosis and it implies re-organization of the actin cytoskeleton. Its failure is one of the major mechanisms of polyploidy and binucleation in mammals. Our aims were 1) to assess the role of redox-sensitive p38α MAPK in cytokinesis by studying the liver of wild type mice or liver-specific p38α knock-out mice; 2) to assess the role of oxidative stress associated with hepatocyte isolation on cytokinesis. When p38α was down-regulated in hepatocytes, MK2 phosphorylation on threonine 334 was completely abrogated. Activation of MNK-1, required for abscission of the intercellular bridge, was diminished. Key proteins of the RhoA pathway (phospho-PRK2, nuclear phospho…

RHOAmacromolecular substancesBiologyCell cycleCofilinActin cytoskeletonBiochemistryCell biologyCytosolPhysiology (medical)biology.proteinMitosisCytokinesisActinFree radical biologymedicine
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A New Type of Cytokine Receptor Antagonist Directly Targeting gp130

1998

The interleukin-6-type family of cytokines bind to receptor complexes that share gp130 as a common signal-transducing subunit. So far, receptor antagonists for interleukin-6-type cytokines have been constructed that still bind to the specific ligand binding subunit of the receptor complex, but have lost the ability to stimulate gp130. Such receptor antagonists compete for a specific receptor of a member of the cytokine family. Interleukin-6 only binds to gp130 when complexed with the interleukin-6 receptor that exists as a membrane bound and soluble molecule. Here we have constructed fusion proteins that consist of the soluble form of the human interleukin-6 receptor covalently linked to in…

Receptor complexRecombinant Fusion ProteinsNerve Tissue ProteinsOncostatin MBiologyLeukemia Inhibitory FactorBiochemistryAntigens CDCytokine Receptor gp130Enzyme-linked receptorHumansPoint Mutation5-HT5A receptorCiliary Neurotrophic FactorMolecular BiologyProtease-activated receptor 2Common gamma chainLymphokinesMembrane GlycoproteinsDose-Response Relationship DrugJanus kinase 1Interleukin-6digestive oral and skin physiologyCell BiologyReceptors Interleukin-6Growth Inhibitorsbiological factorsBiochemistryInterleukin-21 receptorCytokinesPeptidesCytokine receptorProtein BindingJournal of Biological Chemistry
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The polypyrimidine tract-binding protein (PTB) is involved in the post-transcriptional regulation of human inducible nitric oxide synthase expression.

2006

Human inducible nitric oxide synthase (iNOS) expression is regulated by transcriptional and post-transcriptional mechanisms. We have recently shown that the multifunctional RNA-binding proteins KH-type splicing regulatory protein and tristetraprolin are critically involved in the post-transcriptional regulation of human iNOS expression. Several reports have shown that KH-type splicing regulatory protein colocalizes with the polypyrimidine tract-binding protein (PTB), and both RNA-binding proteins seem to interact with the same mRNAs. Therefore we analyzed the involvement of PTB in human iNOS expression. In human DLD-1 cells, cytokine incubation necessary to induce iNOS expression did not ch…

Recombinant Fusion ProteinsTristetraprolinGreen Fluorescent ProteinsNitric Oxide Synthase Type IImacromolecular substancesBiologyIn Vitro TechniquesTransfectionenvironment and public healthBiochemistryGene Expression Regulation EnzymologicCell LineCell Line TumorHumansPolypyrimidine tract-binding proteinRNA MessengerEnzyme InhibitorsPromoter Regions GeneticMolecular BiologyPost-transcriptional regulationRegulation of gene expressionMessenger RNAintegumentary systemCarcinomaEpithelial CellsCell BiologyTransfectionMolecular biologyNitric oxide synthaseRNA splicingColonic Neoplasmsbiology.proteinCytokinesRNA InterferenceProtein Processing Post-TranslationalDichlororibofuranosylbenzimidazolePolypyrimidine Tract-Binding ProteinThe Journal of biological chemistry
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Early stress response of human nasal respiratory epithelia after exposure to 1-methoxypropanol-2

2007

To evaluate the impact of 1-methoxypropanol-2 (MEP) for the stimulation of an inflammatory response in human respiratory mucosa, we exposed 22 primary cell cultures of nasal respiratory epithelia of healthy individuals to MEP concentrations at the level of the German MAK-value (100 ppm) and to the 10-fold concentration (1000 ppm). After 4 and 24h we analyzed the transcription of TNF-alpha, IL-1beta, IL-6, IL-8, MCP-1, GMCSF, Cox-1 and Cox-2 by quantitative PCR as well as the release of the respective cytokines by ELISA. At both MEP concentrations we observed a significant increase of TNF-alpha-, IL-1beta-, IL-6- and Cox-2-transcripts after 4h. After 24h cytokine transcription of TNF-alpha, …

Respiratory Mucosamedicine.medical_specialtyTranscription Geneticmedicine.medical_treatmentInflammationStimulationAir Pollutants OccupationalBiologyGranulocyteToxicologyProinflammatory cytokineInternal medicinemedicineHumansRNA MessengerRespiratory systemCells CulturedGeneral MedicineNasal MucosaCytokineEndocrinologymedicine.anatomical_structurePropylene GlycolsImmunologySolventsCytokinesmedicine.symptomRespiratory tractToxicology Letters
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