Search results for " Mitogen-Activated Protein Kinases"

showing 10 items of 175 documents

Complement Protein C1q Binds to Hyaluronic Acid in the Malignant Pleural Mesothelioma Microenvironment and Promotes Tumor Growth

2017

C1q is the first recognition subcomponent of the complement classical pathway, which acts towards the clearance of pathogens and apoptotic cells. C1q is also known to modulate a range of functions of immune and non-immune cells, including their involvement in placental development and sensorial synaptic pruning. We have recently shown that C1q can promote tumour by encouraging their adhesion, migration and proliferation in addition to angiogenesis and metastasis. In this study, we have examined the role of C1q in the microenvironment of malignant pleuric mesothelioma (MPM), a rare form of cancer commonly associated with exposure to asbestos. We found that C1q was highly expressed in all MPM…

lcsh:Immunologic diseases. Allergy0301 basic medicineComplement system; Malignant pleural mesothelioma; Hyaluronic acid; Mesothelioma cells; C1q; CancerAngiogenesisMPMp38 mitogen-activated protein kinasesImmunologyHAchemical and pharmacologic phenomenaBiologyMetastasisMesothelioma cell03 medical and health sciencesClassical complement pathwaychemistry.chemical_compound0302 clinical medicineImmune systemhyaluronic acidHyaluronic acidmedicinemalignant pleural mesotheliomacancerImmunology and AllergyCell adhesioncomplement systemC1qcomplement system; MPM; HA; Mesothelioma cells; C1q and cancerOriginal ResearchC1q and cancermedicine.diseaseComplement system030104 developmental biologyC1q; Cancer; Complement system; Hyaluronic acid; Malignant pleural mesothelioma; Mesothelioma cells; Immunology and Allergy; Immunologychemistrymesothelioma cells030220 oncology & carcinogenesisImmunologyCancer researchlcsh:RC581-607Frontiers in Immunology
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eIF2α confers cellular tolerance to S. aureus α-toxin

2015

We report on the role of conserved stress-response pathways for cellular tolerance to a pore forming toxin. First, we observed that small molecular weight inhibitors including of eIF2α-phosphatase, jun-N-terminal kinase (JNK), and PI3-kinase sensitized normal mouse embryonal fibroblasts (MEFs) to the small pore forming S. aureus α-toxin. Sensitization depended on expression of mADAM10, the murine ortholog of a proposed high-affinity receptor for α-toxin in human cells. Similarly, eIF2α (S51A/S51A) MEFs, which harbor an Ala knock-in mutation at the regulated Ser51 phosphorylation site of eukaryotic translation initiation factor 2α, were hyper-sensitive to α-toxin. Inhibition of translation w…

lcsh:Immunologic diseases. AllergyMAPK/ERK pathwayImmunologyeIF2αBiologyCycloheximide03 medical and health scienceschemistry.chemical_compoundCellular toleranceImmunology and AllergyInitiation factorpore forming toxinsReceptorOriginal Research030304 developmental biologyGenetics0303 health sciencesKinase030302 biochemistry & molecular biologyJNK Mitogen-Activated Protein KinasesADAM10Translation (biology)MAPKCell biologyEIF2AK4chemistryPhosphorylationCytolysinS. aureus α-toxinlcsh:RC581-607Frontiers in Immunology
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Amphiregulin activates human hepatic stellate cells and is upregulated in non alcoholic steatohepatitis

2015

AbstractAmphiregulin (AR) involvement in liver fibrogenesis and hepatic stellate cells (HSC) regulation is under study. Non-alcoholic fatty liver disease (NAFLD) and its more severe form non-alcoholic steatohepatitis (NASH) may progress to cirrhosis and hepatocellular cancer (HCC). Our aim was to investigate ex vivo the effect of AR on human primary HSC (hHSC) and verify in vivo the relevance of AR in NAFLD fibrogenesis. hHSC isolated from healthy liver segments were analyzed for expression of AR and its activator, TNF-α converting enzyme (TACE). AR induction of hHSC proliferation and matrix production was estimated in the presence of antagonists. AR involvement in fibrogenesis was also ass…

medicine.medical_specialtyBiopsyGene ExpressionADAM17 ProteinBiologyAmphiregulinSeverity of Illness Indexp38 Mitogen-Activated Protein Kinasesdigestive systemArticleMicePhosphatidylinositol 3-Kinases03 medical and health sciences0302 clinical medicineDownregulation and upregulationAmphiregulinGrowth factor receptorNon-alcoholic Fatty Liver DiseaseInternal medicineHepatic Stellate CellsmedicineAnimalsHumansProtein Kinase CPI3K/AKT/mTOR pathwayCell Proliferation030304 developmental biology0303 health sciencesMultidisciplinaryFatty livernutritional and metabolic diseasesmedicine.diseaseFibrosisActinsdigestive system diseases3. Good healthEnzyme ActivationErbB ReceptorsADAM ProteinsDisease Models AnimalEndocrinologyHepatic stellate cellCancer research030211 gastroenterology & hepatologyTumor necrosis factor alphaCollagenSteatohepatitisSignal TransductionScientific Reports
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Dual specificity phosphatase 1 knockout mice show enhanced susceptibility to anaphylaxis but are sensitive to glucocorticoids.

2007

Dual specificity phosphatase DUSP1 (otherwise known as mitogen-activated phosphatase 1 or MKP-1) dephosphorylates MAPKs, particularly p38, and negatively regulates innate immunity. Recent studies have shown that the DUSP1 gene is transcriptionally up-regulated by glucocorticoids (GCs) and that the antiinflammatory action of GCs is impaired in DUSP1-/- mice. Here we show that GC-mediated dephosphorylation of ERK-1 and ERK-2 activated by IgE receptor cross-linking is unimpaired in bone marrow-derived mast cells (BMMCs) of DUSP1-/- mice. Dephosphorylation of phospho-p38 MAPK is impaired but only at early times of GC treatment. Proinflammatory cytokine and chemokine gene expression (CCL2, IL-6,…

medicine.medical_specialtyChemokinePhosphataseImmunoglobulin Ep38 Mitogen-Activated Protein KinasesProinflammatory cytokineDephosphorylationMiceEndocrinologyInternal medicineSepsisDual-specificity phosphatasemedicineAnimalsGenetic Predisposition to DiseaseMolecular BiologyAnaphylaxisGlucocorticoidsMice KnockoutMitogen-Activated Protein Kinase 1Mice Inbred C3HMitogen-Activated Protein Kinase 3biologyInterleukin-6Tumor Necrosis Factor-alphaDegranulationDual Specificity Phosphatase 1General MedicineMice Inbred C57BLEndocrinologyGene Expression RegulationMice Inbred DBAbiology.proteinCytokinesTumor necrosis factor alphaMolecular endocrinology (Baltimore, Md.)
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Neuroendocrine Regulation Of The IL-27-Dependent Immune Response In Macrophages

2013

Abstract The central nervous system has the ability for modulating immune responses, but the molecular mechanisms of such interactions are only partly understood. Interleukin-27 (IL-27) is a heterodimeric protein and structurally related to the IL-12 family of cytokines. IL-27 is composed of the subunits EBI3 and p28. The biological functions of IL-27 have been described as either anti-inflammatory or pro-inflammatory depending on the experimental models studied. In the current study, we investigated how production of Interleukin-27 (IL-27) is regulated by neuroendocrine hormones. We focused our work on the subunit p28, since EBI3 is also present in IL-35 and therefore is not a specific com…

medicine.medical_specialtyLipopolysaccharidebiologyp38 mitogen-activated protein kinasesmedicine.medical_treatmentImmunologyInflammationCell BiologyHematologyBiochemistrychemistry.chemical_compoundEndocrinologyCytokineImmune systemchemistryIntegrin alpha MInternal medicinemedicinebiology.proteinmedicine.symptomReceptorHormoneBlood
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Mechanisms of C-reactive protein-induced blood-brain barrier disruption.

2009

Background and Purpose— Increased mortality after stroke is associated with brain edema formation and high plasma levels of the acute phase reactant C-reactive protein (CRP). The aim of this study was to examine whether CRP directly affects blood–brain barrier stability and to analyze the underlying signaling pathways. Methods— We used a cell coculture model of the blood–brain barrier and the guinea pig isolated whole brain preparation. Results— We could show that CRP at clinically relevant concentrations (10 to 20 μg/mL) causes a disruption of the blood–brain barrier in both approaches. The results of our study further demonstrate CRP-induced activation of surface Fcγ receptors CD16/32 fo…

medicine.medical_specialtyMyosin light-chain kinaseMyosin Light ChainsGuinea PigsBrain Edemamedicine.disease_causeBlood–brain barrierp38 Mitogen-Activated Protein KinasesMyosin light chain kinase activityTight JunctionsInternal medicineMyosinmedicineAnimalsPhosphorylationReceptorCells CulturedAdvanced and Specialized Nursingbusiness.industryReceptors IgGCoculture TechniquesCell biologyRatsStrokeEndocrinologymedicine.anatomical_structureC-Reactive ProteinBlood-Brain BarrierPhosphorylationNeurology (clinical)Endothelium VascularSignal transductionCardiology and Cardiovascular MedicinebusinessReactive Oxygen SpeciesOxidative stressSignal TransductionStroke
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POLYPHENOLS FROM RED WINE MODULATE IMMUNE RESPONSIVENESS: BIOLOGICAL AND CLINICAL SIGNIFICANCE.

2008

Many studies have been conducted on the effects of red wine polyphenols on certain diseases, primarily, coronary heart disease (CHD) and, in this respect, evidence has been demonstrated that intake of red wine is associated with a reduction of CHD symptomatology. In this framework, the purpose of this review is to illustrate the effects of polyphenols on immune cells from human healthy peripheral blood. Data will show that polyphenols are able to stimulate both innate and adaptive immune responses. In particular, the release of cytokines such as interleukin (IL)-12, interferon (IFN)-gamma, and IL-10 as well as immunoglobulins may be important for host protection in different immune related …

medicine.medical_treatmentImmunoglobulinsCoronary DiseaseWineImmunoglobulin ENitric OxidePeripheral blood mononuclear cellp38 Mitogen-Activated Protein KinasesNitric oxidePOLYPHENOLSIMMUNE SYSTEMCYTOKINESIMMUNOGLOBULINSNITRIC OXIDEATHEROSCLEROSISRED WINEchemistry.chemical_compoundImmune systemPhenolsInterferonDrug DiscoverymedicineAnimalsHumansPharmacologyFlavonoidsSettore MED/04 - Patologia Generalebiologybusiness.industryImmunityfood and beveragesInterleukinPolyphenolsCytokinechemistryImmunologyChronic Diseasebiology.proteinLeukocytes MononuclearCytokinesAntibodybusinessmedicine.drug
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Myeloperoxidase mediates neutrophil activation by association with CD11b/CD18 integrins.

2004

Recruitment and activation of polymorphonuclear neutrophils (PMNs) reflects a primary immunological response to invading pathogens and has also emerged as a hallmark of vascular inflammation. One of the principal enzymes released upon PMN activation is myeloperoxidase (MPO), a heme protein that not only generates cytotoxic oxidants but also impacts deleteriously on nitric oxide-dependent signaling cascades within the vasculature. Because MPO also associates with the membrane of PMN, we evaluated whether MPO could also function as an autocrine modulator of PMN activation. The extent of PMN membrane-associated MPO was elevated in patients with acute inflammatory vascular disease compared with…

medicine.medical_treatmentanimal diseasesCD18p38 Mitogen-Activated Protein KinasesCell DegranulationNeutrophil ActivationProinflammatory cytokinechemistry.chemical_compoundSuperoxidesmedicineHumansPhosphorylationPeroxidaseMultidisciplinaryCD11b AntigenbiologySuperoxideElastaseDegranulationNF-kappa Bhemic and immune systemsBiological SciencesMolecular biologyCytokineIntegrin alpha MchemistryMyeloperoxidaseCD18 AntigensImmunologybiology.proteinProceedings of the National Academy of Sciences of the United States of America
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Activation of the p38MAPK cascade is associated with upregulation of TNF alpha receptors in the spinal motor neurons of mouse models of familial ALS.

2005

Phosphorylated p38 mitogen-activated protein kinase (p38MAPK), but not activated c-jun-N-terminal kinase (JNK), increases in the motor neurons of transgenic mice overexpressing ALS-linked SOD1 mutants at different stages of the disease. This effect is associated with a selective increase of phosphorylated MKK3-6, MKK4 and ASK1 and a concomitant upregulation of the TNFalpha receptors (TNFR1 and TNFR2), but not IL1beta and Fas receptors. Activation of both p38 MAPK and JNK occurs in the activated microglial cells of SOD1 mutant mice at the advanced stage of the disease; however, this effect is not accompanied by the concomitant activation of the upstream kinases ASK1 and MKK3,4,6, while both …

p38 mitogen-activated protein kinasesMAP Kinase Kinase 3Mice TransgenicMAP Kinase Kinase 6BiologyMAP Kinase Kinase Kinase 5p38 Mitogen-Activated Protein KinasesReceptors Tumor Necrosis FactorCellular and Molecular NeuroscienceMiceSuperoxide Dismutase-1Downregulation and upregulationAnimalsHumansASK1RNA Messengerfas ReceptorPhosphorylationReceptorProtein kinase AMolecular BiologyP38MAPK cascadeMotor NeuronsKinaseSuperoxide DismutaseTumor Necrosis Factor-alphaAmyotrophic Lateral SclerosisJNK Mitogen-Activated Protein KinasesReceptors Interleukin-1Cell BiologyCell biologyEnzyme ActivationMice Inbred C57BLDisease Models AnimalTumor Necrosis Factor Decoy ReceptorsSpinal CordReceptors Tumor Necrosis Factor Type IDisease ProgressionTumor necrosis factor alphaSignal TransductionMolecular and cellular neurosciences
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Protein Phosphorylation by Peroxisome Proliferators: Species-specific Stimulation of Protein Kinases and Its Role in PP-induced Transcriptional Activ…

1996

p38 mitogen-activated protein kinasesMicrobodiesGene Expression Regulation EnzymologicGeneral Biochemistry Genetics and Molecular BiologyMAP2K7Retinoblastoma-like protein 1History and Philosophy of ScienceAnimalsHumansProtein phosphorylationClofibrateRNA MessengerAcetyl-CoA C-AcetyltransferaseProtein kinase ACells CulturedProtein Kinase CHypolipidemic AgentsbiologyChemistryKinaseGeneral NeuroscienceGRB10Autophagy-related protein 13PhosphoproteinsStaurosporineRats Inbred F344RatsCell biologybiology.proteinProtein KinasesAnnals of the New York Academy of Sciences
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