Search results for "Mitogen-Activated Protein Kinase Kinase"

showing 10 items of 43 documents

Involvement of protein kinases in the induction of NO synthase II in human DLD-1 cells

1998

Protein phosphorylation is involved in the induction of nitric oxide synthase II (NOS II, iNOS) in several types of animal cells. Here we have investigated the possible involvement of major protein kinases in the induction of NOS II expression in human DLD-1 cells. In DLD-1 cells, interferon-γ alone induced a submaximal NOS II expression; a cytokine mixture consisting of interferon-γ, tumour necrosis factor-α and interleukin-1β produced maximal NOS II induction. Activators of protein kinase A (forskolin, 8-dibutyryl-cyclic AMP), of protein kinase C (tetradecanoylphorbol-13-acetate), and of protein kinase G (8-bromo cyclic GMP) did not induce NOS II mRNA by themselves, nor did they alter NOS…

PharmacologybiologyMAP kinase kinase kinaseCyclin-dependent kinase 4Cyclin-dependent kinase 2biology.proteinCyclin-dependent kinase 9ASK1c-RafMitogen-activated protein kinase kinaseMolecular biologyMAP2K7British Journal of Pharmacology
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Systematic review of BRAF/MEK inhibitors‐induced Severe Cutaneous Adverse Reactions (SCARs)

2020

Severe cutaneous adverse reactions (SCARs) [Stevens-Johnson syndrome (SJS), toxic epidermal necrolysis (TEN), drug rash with eosinophilia and systemic syndrome (DRESS), acute generalized exanthematous pustulosis (AGEP), and generalized bullous fixed eruption (GBFE)] are severe drug reactions that often require hospitalization and could be fatal. BRAF and MEK inhibitors (BRAF/MEKi) are a standard of care in patients with BRAF-mutated metastatic melanomas. These agents are administered until disease progression or unacceptable toxicity occurs. This review has focus on BRAF/MEKi-induced SCARs. A systematic search of the following terms: 'vemurafenib', 'cobimetinib', 'dabrafenib', 'trametinib',…

Proto-Oncogene Proteins B-rafmedicine.medical_specialtyDermatologyCicatrix030207 dermatology & venereal diseases03 medical and health scienceschemistry.chemical_compound0302 clinical medicinemedicineHumansVemurafenibRetrospective StudiesMitogen-Activated Protein Kinase KinasesTrametinibCobimetinibbusiness.industryBinimetinibDabrafenibAcute generalized exanthematous pustulosismedicine.diseaseDermatologyToxic epidermal necrolysisInfectious DiseasesAcute Generalized Exanthematous PustulosischemistryDrug Hypersensitivity SyndromeStevens-Johnson Syndrome030220 oncology & carcinogenesisbusinessmedicine.drugJournal of the European Academy of Dermatology and Venereology
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Activation of mitogen-activated protein kinase by the bradykinin B2receptor is independent of receptor phosphorylation and phosphorylation-triggered …

1999

Recent evidence suggests that serine/threonine phosphorylation and internalization of beta2-adrenergic receptors play critical roles in signalling to the mitogen-activated protein kinase cascade. To investigate whether this represents a general mechanism employed by G protein-coupled receptors, we studied the requirement of these processes in the activation of mitogen-activated protein kinase by G alpha(q)-coupled bradykinin B2 receptors. Mutant B2 receptors impaired in receptor phosphorylation and internalization are fully capable to activate mitogen-activated protein kinase. Bradykinin-induced long-term effects on mitogenic signalling monitored by measuring the transcriptional activity of…

Receptor Bradykinin B2Bradykinin B2 receptorBiophysicsMitogen-activated protein kinase kinaseBradykininBiochemistryCell LineMAP2K7Structural BiologyMitogenic signallingGeneticsHumansPhosphorylationBradykinin receptorProtein kinase AMolecular BiologyProtein kinase CG protein-coupled receptorG protein-coupled receptor kinaseMAP kinase kinase kinaseChemistryReceptors BradykininCell BiologyMitogen-activated protein kinaseEnzyme ActivationBiochemistryCalcium-Calmodulin-Dependent Protein KinasesInternalizationSignal TransductionFEBS Letters
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Convergence of the target of rapamycin and the Snf1 protein kinase pathways in the regulation of the subcellular localization of Msn2, a transcriptio…

2002

The subcellular localization of Msn2, a transcriptional activator of STRE (stress response element)-regulated genes, is modulated by carbon source availability. In cells growing in glucose, Msn2 is located mainly in the cytosol, whereas in carbon source-starved cells, Msn2 is located largely inside the nucleus. However, in cells lacking Reg1 (the regulatory subunit of the Reg1/Glc7 protein phosphatase complex), the regulation of subcellular distribution is absent, Msn2 being constitutively present in the cytosol. The localization defect in these mutants is specific for carbon starvation stress, and it is because of the presence of an abnormally active Snf1 protein kinase that inhibits the n…

Saccharomyces cerevisiae ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeMitogen-activated protein kinase kinaseBiologyProtein Serine-Threonine KinasesBiochemistryASK1Molecular BiologyDNA PrimersSirolimusMAP kinase kinase kinaseBase SequenceKinaseCell BiologySubcellular localizationCarbonCell biologyCulture MediaDNA-Binding ProteinsCytosolBiochemistryTrans-ActivatorsCyclin-dependent kinase 9Nuclear localization sequenceSubcellular FractionsTranscription FactorsThe Journal of biological chemistry
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The development of benzimidazoles as selective rho kinase inhibitors

2010

Rho Kinase (ROCK) is a serine/threonine kinase whose inhibition could prove beneficial in numerous therapeutic areas. We have developed a promising class of ATP-competitive inhibitors based upon a benzimidazole scaffold, which show excellent potency toward ROCK (IC(50)<10nM). This report details the optimization of selectivity for ROCK over other related kinases such as Protein kinase A (PKA).

Serine/threonine-specific protein kinaserho-Associated KinasesMAP kinase kinase kinaseChemistryKinaseOrganic ChemistryClinical BiochemistryPharmaceutical ScienceGlaucomaChromanMitogen-activated protein kinase kinaseBiochemistryBenzimidazoleBiochemistryDrug DiscoveryROCKMolecular MedicineBenzimidazolesCyclin-dependent kinase 9Protein kinase ARho KinaseProtein Kinase InhibitorsMolecular BiologyRho-associated protein kinaseProtein kinase CBioorganic & Medicinal Chemistry Letters : a tetrahedron publication for the rapid dissemination of preliminary communication and all aspects of bioorganic chemistry, medicinal chemistry and related disciplines
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Alteration of DNA topoisomerase II activity during infection of H9 cells by human immunodeficiency virus type 1 in vitro: a target for potential ther…

1990

Infection of H9 cells with human immunodeficiency virus type 1 (HIV-1) was found to decrease the phosphorylation of DNA topoisomerase II during the initial phase of infection. Simultaneously, with a later overshoot of phosphorylation and the subsequent activation of DNA topoisomerase II, the production of HIV-1 started. Applying three new protein kinase C inhibitors from the class of O-alkylglycerophospholipids we demonstrated that inhibition of protein kinase C-mediated phosphorylation of DNA topoisomerase II resulted in an inhibition of HIV-1 production. Based on the differential effect of the two protein kinase C activators, phorbol ester and bryostatin, we conclude that phosphorylation …

T-LymphocytesMitogen-activated protein kinase kinaseIn Vitro TechniquesMAP2K7Cell LineLactonesVirologyAnimalsPhosphorylationProtein kinase AProtein kinase CProtein Kinase CPharmacologybiologyCyclin-dependent kinase 2LysophosphatidylcholinesRats Inbred StrainsDNA topoisomerase II activityBryostatinsProtein kinase RMolecular biologyRatsDNA Topoisomerases Type Ibiology.proteinHIV-1Tetradecanoylphorbol AcetateCyclin-dependent kinase 9Electrophoresis Polyacrylamide GelMacrolidesAntiviral research
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JNK phosphorylation relieves HDAC3-dependent suppression of the transcriptional activity of c-Jun

2003

The AP-1 transcription factor c-Jun is a prototypical nuclear effector of the JNK signal transduction pathway. The integrity of JNK phosphorylation sites at serines 63/73 and at threonines 91/93 in c-Jun is essential for signal-dependent target gene activation. We show that c-Jun phosphorylation mediates dissociation of an inhibitory complex, which is associated with histone deacetylase 3 (HDAC3). The subsequent events that ultimately cause increased mRNA synthesis are independent of c-Jun phosphorylation and its interaction with JNK. These findings provide an 'activation by de-repression' model as an explanation for the stimulatory function of JNK on c-Jun.

ThreonineTranscriptional ActivationTranscription GeneticMAP Kinase Kinase 4Proto-Oncogene Proteins c-junRecombinant Fusion ProteinsMitogen-activated protein kinase kinaseHistone DeacetylasesGeneral Biochemistry Genetics and Molecular BiologyCell LinePhosphorylation cascadeMiceSuppression GeneticGenes ReporterSerineAnimalsHumansRNA MessengerPhosphorylationMolecular BiologyTranscription factorSequence DeletionMitogen-Activated Protein Kinase KinasesGeneral Immunology and MicrobiologybiologyGeneral Neurosciencec-junJNK Mitogen-Activated Protein KinasesArticles3T3 CellsHDAC3Molecular biologyProtein Structure TertiaryMitogen-activated protein kinaseMutationMutagenesis Site-Directedbiology.proteinPhosphorylationSignal transductionProtein BindingThe EMBO Journal
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Urokinase activates macrophage PON2 gene transcription via the PI3K/ROS/MEK/SREBP-2 signalling cascade mediated by the PDGFR-β

2009

Aims We have recently shown that urokinase plasminogen activator (uPA) increases oxidative stress (OS), cholesterol biosynthesis, and paraoxonase 2 (PON2) expression in macrophages via binding to its receptor, the uPAR. Since PON2 is regulated by both OS and cholesterol content, we hypothesized that uPA elicits a cascade of signal transduction events shared by NADPH oxidase and cholesterol biosynthesis that culminates in PON2 gene expression. Here, we investigated the signalling pathway that leads to the expression of PON2 in macrophages in response to uPA. Methods and results The increase in macrophage PON2 mRNA levels in response to uPA was shown to depend on PON2 gene promoter activation…

Transcription GeneticPhysiologyReceptor Platelet-Derived Growth Factor betaPhosphatidylinositol 3-KinasesPhysiology (medical)Gene expressionHumansExtracellular Signal-Regulated MAP KinasesTranscription factorCells CulturedMitogen-Activated Protein Kinase KinasesRegulation of gene expressionNADPH oxidasebiologyAryldialkylphosphataseKinaseMacrophagesNADPH OxidasesUrokinase-Type Plasminogen ActivatorCell biologySterol regulatory element-binding proteinUrokinase receptorGene Expression RegulationBiochemistryTissue Plasminogen Activatorbiology.proteinSignal transductionReactive Oxygen SpeciesCardiology and Cardiovascular MedicineSignal TransductionSterol Regulatory Element Binding Protein 2Cardiovascular Research
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Mutant HRAS as novel target for MEK and mTOR inhibitors.

2015

HRAS is a frequently mutated oncogene in cancer. However, mutant HRAS as drug target has not been investigated so far. Here, we show that mutant HRAS hyperactivates the RAS and the mTOR pathway in various cancer cell lines including lung, bladder and esophageal cancer. HRAS mutation sensitized toward growth inhibition by the MEK inhibitors AZD6244, MEK162 and PD0325901. Further, we found that MEK inhibitors induce apoptosis in mutant HRAS cell lines but not in cell lines lacking RAS mutations. In addition, knockdown of HRAS by siRNA blocked cell growth in mutant HRAS cell lines. Inhibition of the PI3K pathway alone or in combination with MEK inhibitors did not alter signaling nor had an imp…

mTOR inhibitorMutantBlotting Western610 Medicine & healthApoptosisMice SCIDCell LineProto-Oncogene Proteins p21(ras)chemistry.chemical_compoundCell Line TumorNeoplasmsMedicineAnimalsHumansHRASHRAS mutationsProtein Kinase InhibitorsPI3K/AKT/mTOR pathwayCell ProliferationGeneticsMitogen-Activated Protein Kinase KinasesMEK inhibitorOncogeneCell growthbusiness.industryMEK inhibitorTOR Serine-Threonine KinasesDiphenylamineXenograft Model Antitumor AssaysTumor Burdenlung cancer10219 Clinic for Gastroenterology and HepatologyCell Transformation NeoplasticOncologychemistry10032 Clinic for Oncology and HematologyBenzamidesMutationCancer researchbladder cancer2730 OncologyBenzimidazolesRNA InterferenceSignal transductionGrowth inhibitionbusinessSignal TransductionResearch PaperOncotarget
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The role of the renin-angiotensin system in atrial fibrillation and the therapeutic effects of ACE-Is and ARBS

2008

Atrial fibrillation (AF) is the most common rhythm disturbance in medical practice and represents a very expensive health problem. AF can be managed with the prevention of thromboembolism and either a rate control of rhythm strategy. As both strategies have important limitations, probably a preventative strategy in patients at risk of developing arrhythmia can be a more attractive option. The renin-angiotensin system (RAS) seems to be involved in the genesis of arrhythmia by the following two mechanisms: 1. the induction of atrial fibrosis and structural remodelling by mitogen-activated protein kinase (MAPK) expression and reduction of collagenase activity; 2. the induction of electrical re…

medicine.medical_specialtyHeart diseaseGenotypeElectric CountershockAngiotensin-Converting Enzyme InhibitorsReview ArticleRenin-Angiotensin Systemrenin-angiotensin system atrial fibrillation ACE-I ARBDiabetes mellitusInternal medicineRenin–angiotensin systemAtrial FibrillationmedicineHumansPharmacology (medical)PharmacologyMitogen-Activated Protein Kinase KinasesEvidence-Based Medicinebiologybusiness.industryAngiotensin IIfungifood and beveragesAtrial fibrillationAngiotensin-converting enzymemedicine.diseaseAngiotensin IIEndocrinologyHeart failureACE inhibitorCardiologybiology.proteinbusinessAnti-Arrhythmia Agentsmedicine.drug
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