Search results for "Mitogen-activated protein kinases"

showing 10 items of 246 documents

MAP kinase p38 and its relation to T cell anergy and suppressor function of regulatory T cells

2008

Diverse regulatory T cell populations (Treg) are important for the control of self tolerance and immune homeostasis. These include naturally occurring CD4+CD25+ Treg (nTreg) and induced Treg (iTreg). Tolerogenic dendritic cells, modulated by IL-10, are able to convert peripheral T cells into iTreg. These are anergic and characterized by a G(1) cell cycle arrest, dependent on elevated levels of the cdk inhibitor p27(Kip1). Novel data revealed a distinct pattern of MAP kinase activation in iTreg different from clonal T cell anergy, with enhanced activation of the p38-MAPKAP-K2/3 pathway. p38 is involved in cell cycle control and its activity is a prerequisite for the induction and maintenance…

Clonal AnergyCell cycle checkpointClonal anergyRegulatory T cellT cellCell CycleCell BiologyBiologyCell cycleT-Lymphocytes Regulatoryp38 Mitogen-Activated Protein KinasesCell biologymedicine.anatomical_structuremedicineAnimalsHumansCytotoxic T cellIL-2 receptorAntigen-presenting cellMolecular BiologyCyclin-Dependent Kinase Inhibitor p27Developmental BiologyCell Cycle
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Heme oxygenase-1 inhibits apoptosis in Caco-2 cells via activation of Akt pathway

2005

Heme oxygenase-1 can play a protective role against cellular stress. In colon cancer cells, these effects would be relevant to oncogenesis and resistance to chemotherapy. The aim of the study was to examine the effects of heme oxygenase-1 induction on cell survival in a human colon cancer cell line, Caco-2. Serum deprivation induced apoptosis, reduced Akt and p38 phosphorylation, and increased p21(Cip/WAF1) levels. Heme oxygenase-1 induction by treatment with cobalt protoporphyrin IX resulted in resistance to apoptosis, activation of Akt, reduction in p21(Cip/WAF1) levels and modification of bcl2/bax ratio towards survival. Indomethacin reduced apoptosis but in contrast to heme oxygenase-1,…

Cyclin-Dependent Kinase Inhibitor p21BiliverdinCell SurvivalChemistryBilirubinp38 mitogen-activated protein kinasesProtoporphyrinsApoptosisCell BiologyBiochemistryCulture Media Serum-FreeCell biologyHeme oxygenasechemistry.chemical_compoundApoptosisEnzyme InductionHumansCaco-2 CellsProto-Oncogene Proteins c-aktHemeProtein kinase BHeme Oxygenase-1PI3K/AKT/mTOR pathwayThe International Journal of Biochemistry & Cell Biology
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Lovastatin causes sensitization of HeLa cells to ionizing radiation‐induced apoptosis by the abrogation of G2 blockage

2003

To investigate the effect of inhibition of Ras/Rho-regulated signalling by 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase inhibitors (statins) on radiation-induced cell killing and apoptosis.Different human cell lines were pretreated or not with lovastatin before exposure to gamma-rays. Afterwards, radiation-induced cell killing, formation and repair of double-strand breaks, activation of radiation-inducible signal mechanisms (i.e. p53, p21, extracellular-signal-related kinase (ERK), NF-kappaB), changes in cell cycle progression and apoptosis were analysed.As shown by a colony formation assay, lovastatin sensitized HeLa cells to gamma-radiation-induced cell killing. The lovastati…

Cyclin-Dependent Kinase Inhibitor p21G2 PhaseMAPK/ERK pathwayApoptosisBiologyHeLaCyclinspolycyclic compoundsmedicineHumansRadiology Nuclear Medicine and imagingLovastatinSensitizationRadiological and Ultrasound TechnologyKinaseNF-kappa Bnutritional and metabolic diseasesCell cyclebiology.organism_classificationCell biologyCell killingmedicine.anatomical_structureGamma RaysApoptosislipids (amino acids peptides and proteins)LovastatinHydroxymethylglutaryl-CoA Reductase InhibitorsMitogen-Activated Protein KinasesTumor Suppressor Protein p53DNA DamageHeLa Cellsmedicine.drugInternational Journal of Radiation Biology
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“Cysteinyl leukotriene-1 receptor activation in a human bronchial epithelial cell line leads to signal transducer and activator of transcription 1-me…

2008

Abstract We studied the effect of leukotriene D(4) (LTD(4)) on a human bronchial epithelial cell line (16HBE) overexpressing the cysteinyl leukotriene (CysLT) (1) receptor (HBECysLT(1)R), looking at the associated signal transduction mechanisms as well as at effects on inflammatory cell adhesion. The results obtained showed that LTD(4) increases the phosphorylation of extracellular signal-regulated protein kinase (ERK) 1/2 and of the signal transducer and activator of transcription 1 (STAT-1) in serine 727 (STAT-1Ser727), resulting in increased eosinophil adhesion to HBECysLT(1)R, associated with enhanced surface expression of intercellular adhesion molecule (ICAM) 1. Pretreatment with a Cy…

CyclopropanesMAPK/ERK pathwayIndolesBronchiAcetatesSulfidesBiologyCysteinyl leukotriene-1cysteinyl leukotrieneCell LineLeukotriene D4MaleimidesInterferon-gammaCell AdhesionHumansProtein kinase ACells CulturedProtein kinase CReceptors LeukotrienePharmacologyKinaseMEK inhibitorMembrane ProteinsEpithelial CellsIntercellular Adhesion Molecule-1Intercellular adhesion moleculeCell biologyEosinophilsSTAT1 Transcription FactorQuinolinesLeukotriene AntagonistsMolecular MedicinePhosphorylationMitogen-Activated Protein KinasesSignal transduction
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Activation and translocation of p38 mitogen-activated protein kinase after stimulation of monocytes with contact sensitizers.

2002

Recently we described the induction of tyrosine phosphorylation by contact sensitizers as an early molecular event during the activation of antigen- presenting cells. In this study, the role of the p38 mitogen-activated protein kinase for the activation of human monocytes after exposure to four structurally unrelated contact sensitizers was analyzed in comparison with the irritant benzalkonium chloride and an inductor of oxidative stress (H 2 O 2 ) using immunofluorescence, Western blotting, and enzyme-linked immunosorbent assay techniques. Bio chemical analysis revealed a translocation of p38 from the cytoplasm to the detergent-resistant cell fraction only upon stimulation with contact sen…

CytoplasmMAP Kinase Signaling SystemPyridinesp38 mitogen-activated protein kinasesDermatologyBiologyIn Vitro TechniquesBiochemistryp38 Mitogen-Activated Protein KinasesMonocyteschemistry.chemical_compoundProto-Oncogene ProteinsHumansEnzyme InhibitorsPhosphorylationProtein kinase ATranscription factorMolecular Biologyets-Domain Protein Elk-1KinaseImidazolesTyrosine phosphorylationBiological TransportCell BiologyMolecular biologyDNA-Binding ProteinsEnzyme ActivationIL-1β/irritantchemistryhaptenMitogen-activated protein kinasebiology.proteinIrritantsPhosphorylationSignal transductionMitogen-Activated Protein KinasesBenzalkonium CompoundsHaptenssignal transductionInterleukin-1Transcription FactorsThe Journal of investigative dermatology
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Interaction of Mitogen-activated Protein Kinases with the Kinase Interaction Motif of the Tyrosine Phosphatase PTP-SL Provides Substrate Specificity …

1999

ERK1 and ERK2 associate with the tyrosine phosphatase PTP-SL through a kinase interaction motif (KIM) located in the juxtamembrane region of PTP-SL. A glutathione S-transferase (GST)-PTP-SL fusion protein containing the KIM associated with ERK1 and ERK2 as well as with p38/HOG, but not with the related JNK1 kinase or with protein kinase A or C. Accordingly, ERK2 showed in vitro substrate specificity to phosphorylate GST-PTP-SL in comparison with GST-c-Jun. Furthermore, tyrosine dephosphorylation of ERK2 by the PTP-SLDeltaKIM mutant was impaired. The in vitro association of ERK1/2 with GST-PTP-SL was highly stable; however, low concentrations of nucleotides partially dissociated the ERK1/2.P…

Cytoplasmanimal structuresProtein Kinase C-alphaRecombinant Fusion ProteinsCèl·lulesNerve Tissue ProteinsProtein tyrosine phosphataseMitogen-activated protein kinase kinaseTransfectionenvironment and public healthBiochemistrySH3 domainReceptor tyrosine kinaseMAP2K7Substrate SpecificitySerineAnimalsc-RafAmino Acid SequenceMolecular BiologyProtein Kinase CSequence DeletionMitogen-Activated Protein Kinase 1Binding SitesMitogen-Activated Protein Kinase 3biologyCyclin-dependent kinase 2Intracellular Signaling Peptides and ProteinsJNK Mitogen-Activated Protein KinasesCell BiologyCyclic AMP-Dependent Protein KinasesIsoenzymesenzymes and coenzymes (carbohydrates)KineticsBiochemistryAmino Acid SubstitutionCOS CellsCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedCyclin-dependent kinase 9CattleMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesProteïnes
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A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase

1999

Protein tyrosine phosphatase PTP-SL retains mitogen-activated protein (MAP) kinases in the cytoplasm in an inactive form by association through a kinase interaction motif (KIM) and tyrosine dephosphorylation. The related tyrosine phosphatases PTP-SL and STEP were phosphorylated by the cAMP-dependent protein kinase A (PKA). The PKA phosphorylation site on PTP-SL was identified as the Ser231 residue, located within the KIM. Upon phosphorylation of Ser231, PTP-SL binding and tyrosine dephosphorylation of the MAP kinases extracellular signal–regulated kinase (ERK)1/2 and p38α were impaired. Furthermore, treatment of COS-7 cells with PKA activators, or overexpression of the Cα catalytic subunit …

Cytoplasmanimal structuresRecombinant Fusion ProteinsCèl·lulesAmino Acid MotifsNerve Tissue ProteinsProtein tyrosine phosphataseSH2 domainTransfectionenvironment and public healthModels Biologicalp38 Mitogen-Activated Protein KinasesReceptor tyrosine kinaseSH3 domainCell LinePhosphoserinetyrosine phosphatasesAnimalsHumansProtein phosphorylationPKAReceptor-Like Protein Tyrosine Phosphatases Class 7PhosphorylationPTP-SLCell NucleusMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3biologyBrief ReportIntracellular Signaling Peptides and ProteinsBiological TransportCell BiologyProtein Tyrosine Phosphatases Non-ReceptorCyclic AMP-Dependent Protein KinasesEnzyme Activationenzymes and coenzymes (carbohydrates)MAP kinasesBiochemistryMitogen-activated protein kinaseCOS CellsMutationbiology.proteinPhosphorylationMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesEnzimssignal transductionProto-oncogene tyrosine-protein kinase Src
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Late activation of stress kinases (SAPK/JNK) by genotoxins requires the DNA repair proteins DNA-PKcs and CSB.

2005

Although genotoxic agents are powerful inducers of stress kinases (SAPK/JNK), the contribution of DNA damage itself to this response is unknown. Therefore, SAPK/JNK activation of cells harboring specific defects in DNA damage-recognition mechanisms was studied. Dual phosphorylation of SAPK/JNK by the genotoxin methyl methanesulfonate (MMS) occurred in two waves. The early response (≤2 h after exposure) was similar in cells knockout for ATM, PARP, p53, and CSB or defective in DNA-PKcscompared with wild-type cells. The late response however (≥4 h), was drastically reduced in DNA-PKcsand Cockayne's syndrome B (CSB)-deficient cells. Similar results were obtained with human cells lacking DNA-PKc…

DNA ReplicationAlkylationDNA RepairDNA damageDNA repairPoly ADP ribose polymeraseDNA-Activated Protein KinaseBiologyModels Biologicalchemistry.chemical_compoundMiceAnimalsHumansPhosphorylationPoly-ADP-Ribose Binding ProteinsMolecular BiologyDNA-PKcsCells CulturedKinaseDNA HelicasesJNK Mitogen-Activated Protein KinasesNuclear ProteinsCell BiologyBase excision repairDNAArticlesMethyl MethanesulfonateMolecular biologyMethyl methanesulfonateDNA-Binding ProteinsEnzyme Activationenzymes and coenzymes (carbohydrates)DNA Repair EnzymeschemistryPhosphorylationProtein Processing Post-TranslationalDNA DamageMutagensSignal TransductionMolecular biology of the cell
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Ultraviolet light-induced apoptotic death is impaired by the HMG-CoA reductase inhibitor lovastatin.

2003

HMG-CoA reductase inhibitors (i.e., statins) attenuate C-terminal isoprenylation of Rho GTPases, thereby inhibiting UV-C-induced activation of c-Jun-N-terminal kinases/stress-activated protein kinases (JNKs/SAPKs). Inhibition of UV-C-triggered JNK/SAPK activation by lovastatin is due to inhibition of Rac-SEK1/MKK4-mediated phosphorylation of JNKs/SAPKs at Thr183/Tyr185. UV-C-stimulated phosphorylation of p38 kinase (Thr180/Tyr182) is also impaired by lovastatin. Cell killing provoked by UV-C irradiation was significantly inhibited by lovastatin. This was paralleled by a reduced frequency of chromosomal aberrations, accelerated recovery from UV-C-induced transient replication blockage, inhib…

DNA ReplicationUltraviolet Raysp38 mitogen-activated protein kinasesBiophysicsApoptosisCHO CellsBiochemistryp38 Mitogen-Activated Protein KinasesCricetinaemedicineUltraviolet lightAnimalsMitogen-Activated Protein Kinase 8LovastatinMolecular BiologyCaspasebiologyKinaseCell BiologyCell biologyrac GTP-Binding ProteinsEnzyme ActivationCell killingApoptosisCaspasesHMG-CoA reductasebiology.proteinLovastatinHydroxymethylglutaryl-CoA Reductase InhibitorsMitogen-Activated Protein Kinasesmedicine.drugBiochemical and biophysical research communications
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PED Mediates AKT-Dependent Chemoresistance in Human Breast Cancer Cells

2005

Abstract Killing of tumor cells by cytotoxic therapies, such as chemotherapy or gamma-irradiation, is predominantly mediated by the activation of apoptotic pathways. Refractoriness to anticancer therapy is often due to a failure in the apoptotic pathway. The mechanisms that control the balance between survival and cell death in cancer cells are still largely unknown. Tumor cells have been shown to evade death signals through an increase in the expression of antiapoptotic molecules or loss of proapoptotic factors. We aimed to study the involvement of PED, a molecule with a broad antiapoptotic action, in human breast cancer cell resistance to chemotherapeutic drugs–induced cell death. We show…

EXPRESSIONAdultCancer ResearchProgrammed cell deathmedicine.medical_treatmentINHIBITIONApoptosisBreast NeoplasmsProtein Serine-Threonine KinasesDNA AntisenseACTIVATIONBreast cancerTransduction GeneticCell Line TumorProto-Oncogene ProteinsComplementary DNAmedicineHumansCytotoxic T cellPROTEIN-KINASE-CProtein kinase BAgedNeoplasm StagingChemotherapybusiness.industryDEATHIntracellular Signaling Peptides and ProteinsJNK Mitogen-Activated Protein KinasesIN-VITROCHEMOTHERAPYMiddle AgedPhosphoproteinsmedicine.diseasePED/PEA-15Up-RegulationEnzyme ActivationOncologyDrug Resistance NeoplasmApoptosisCancer cellImmunologyCancer researchFemalePTEN GENEApoptosis Regulatory ProteinsbusinessProto-Oncogene Proteins c-aktCancer Research
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