Search results for "Mitogen-Activated Protein Kinase"

showing 10 items of 353 documents

Tristetraprolin Regulates the Expression of the Human Inducible Nitric-Oxide Synthase Gene

2005

The expression of human inducible NO synthase (iNOS) is regulated both by transcriptional and post-transcriptional mechanisms. Stabilization of mRNAs often depends on activation of p38 mitogen-activated protein kinase (p38 MAPK). In human DLD-1 cells, inhibition of p38 MAPK by the compound 4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)1H-imidazole (SB203580) or by overexpression of a dominant-negative p38 MAPKalpha protein resulted in a reduction of human iNOS mRNA and protein expression, whereas human iNOS promoter activity was not affected. An important RNA binding protein regulated by the p38 MAPK pathway and involved in the regulation of the stability of several mRNAs is tr…

ImmunoprecipitationRNA Stabilityp38 mitogen-activated protein kinasesTristetraprolinNitric Oxide Synthase Type IIRNA-binding proteinGene Expression Regulation EnzymologicCell LineImmediate-Early ProteinsTristetraprolinEnzyme StabilityHumansRNA MessengerProtein kinase APharmacologyRegulation of gene expressionbiologyChemistryZinc FingersTransfectionMolecular biologyDNA-Binding ProteinsNitric oxide synthasebiology.proteinMolecular MedicineNitric Oxide SynthaseMolecular Pharmacology
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Protein Kinase C μ Is Regulated by the Multifunctional Chaperon Protein p32

2000

We identified the multifunctional chaperon protein p32 as a protein kinase C (PKC)-binding protein interacting with PKCalpha, PKCzeta, PKCdelta, and PKC mu. We have analyzed the interaction of PKC mu with p32 in detail, and we show here in vivo association of PKC mu, as revealed from yeast two-hybrid analysis, precipitation assays using glutathione S-transferase fusion proteins, and reciprocal coimmunoprecipitation. In SKW 6.4 cells, PKC mu is constitutively associated with p32 at mitochondrial membranes, evident from colocalization with cytochrome c. p32 interacts with PKC mu in a compartment-specific manner, as it can be coimmunoprecipitated mainly from the particulate and not from the so…

ImmunoprecipitationRecombinant Fusion ProteinsGolgi ApparatusSaccharomyces cerevisiaeSpodopteraMitogen-activated protein kinase kinaseBiologyTransfectionBiochemistryCell LineMitochondrial ProteinsAnimalsHumansCloning MolecularKinase activityMolecular BiologyProtein Kinase CProtein kinase CGlutathione TransferaseB-LymphocytesBinding SitesMembrane GlycoproteinsKinaseAutophosphorylationJNK Mitogen-Activated Protein KinasesCell BiologyFusion proteinMitochondriaReceptors ComplementCell biologybody regionsHyaluronan ReceptorsProtein kinase domainBiochemistryMitogen-Activated Protein KinasesCarrier ProteinsMolecular ChaperonesProtein BindingJournal of Biological Chemistry
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Design and synthesis of 1-aryl-5-anilinoindazoles as c-Jun N-terminal kinase inhibitors.

2012

Starting from pyrazole HTS hit (1), a series of 1-aryl-1H-indazoles have been synthesized as JNK3 inhibitors with moderate selectivity against JNK1. SAR studies led to the synthesis of 5r as double digital nanomolar JNK3 inhibitor with good in vivo exposure.

IndazolesStereochemistryClinical BiochemistryPharmaceutical SciencePlasma protein bindingPyrazoleBiochemistrychemistry.chemical_compoundStructure-Activity RelationshipIn vivoMitogen-Activated Protein Kinase 10Drug DiscoveryStructure–activity relationshipAnimalsMitogen-Activated Protein Kinase 8Molecular BiologyProtein Kinase InhibitorsAniline CompoundsChemistryKinaseArylOrganic Chemistryc-junJNK Mitogen-Activated Protein KinasesBrainCombinatorial chemistryRatsDrug DesignMolecular MedicineSelectivityHalf-LifeProtein BindingBioorganicmedicinal chemistry letters
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Diacylglycerols containing Omega 3 and Omega 6 fatty acids bind to RasGRP and modulate MAP kinase activation.

2003

We elucidated the effects of different diacylglycerols (DAGs), i.e. 1-stearoyl-2-arachidonoyl-sn-glycerol (SAG), 1-stearoyl-2-docosahexaenoyl-sn-glycerol (SDG), and 1-stearoyl-2-eicosapentaenoyl-sn-glycerol (SEG), on [3H]PDBu binding to RasGRP. The competition studies with these DAGs on [3H]PDBu binding to RasGRP revealed different Ki values for these DAG molecular species. Furthermore, we transfected human Jurkat T cells by a plasmid containing RasGRP and assessed the implication of endogenous DAGs on activation of MAP kinases ERK1/ERK2, induced by phorbol-12-myristate-13-acetate (PMA). In control cells, GF109203X, a protein kinase C inhibitor, inhibited ERK1/ERK2 activation. However, this…

IndolesTime FactorsBiochemistryJurkat cellsMaleimideschemistry.chemical_compoundJurkat CellsGuanine Nucleotide Exchange FactorsEnzyme InhibitorsMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3KinaseFatty AcidsBrainTransfectionCell biologyDNA-Binding ProteinsBiochemistryEicosapentaenoic AcidDocosahexaenoic acidMitogen-activated protein kinasePhosphorylationTetradecanoylphorbol Acetatelipids (amino acids peptides and proteins)Arachidonic acidMitogen-Activated Protein KinasesPlasmidsProtein BindingDNA ComplementaryDocosahexaenoic AcidsMAP Kinase Signaling SystemImmunoblottingBiologyTransfectionBinding CompetitiveDiglyceridesInhibitory Concentration 50Fatty Acids Omega-6Fatty Acids Omega-3Escherichia coliAnimalsHumansCalphostinMolecular BiologyDose-Response Relationship Drugurogenital systemCell BiologyRatsEnzyme ActivationKineticschemistrybiology.proteinThe Journal of biological chemistry
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Cross-talk between oxidative stress and pro-inflammatory cytokines in acute pancreatitis: a key role for protein phosphatases.

2009

Acute pancreatitis is an acute inflammatory process localized in the pancreatic gland that frequently involves peripancreatic tissues. It is still under investigation why an episode of acute pancreatitis remains mild affecting only the pancreas or progresses to a severe form leading to multiple organ failure and death. Proinflammatory cytokines and oxidative stress play a pivotal role in the early pathophysiological events of the disease. Cytokines such as interleukin 1beta and tumor necrosis factor alpha initiate and propagate almost all consequences of the systemic inflammatory response syndrome. On the other hand, depletion of pancreatic glutathione is an early hallmark of acute pancreat…

Inflammationmedicine.disease_causeProinflammatory cytokineDrug DiscoveryPhosphoprotein PhosphatasesMedicineAnimalsHumansPharmacologyInflammationbiologybusiness.industrymedicine.diseaseSystemic inflammatory response syndromeOxidative StressPancreatitisMitogen-activated protein kinaseImmunologyAcute Diseasebiology.proteinAcute pancreatitisPancreatitisCytokinesTumor necrosis factor alphamedicine.symptomMitogen-Activated Protein KinasesbusinessOxidation-ReductionOxidative stressSignal TransductionCurrent pharmaceutical design
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The collagen receptor integrins have distinct ligand recognition and signaling functions

2000

Distinct collagen subtypes are recognized by specific cell surface receptors. Two of the best known collagen receptors are members of the integrin family and are named alpha1beta1 and alpha2beta1. Integrin alpha1beta1 is abundant on smooth muscle cells, whereas the alpha2beta1 integrin is the major collagen receptor on epithelial cells and platelets. Many cell types, such as fibroblasts, osteoblasts, chondrocytes, endothelial cells, and lymphocytes may concomitantly express both of the receptors. We have studied the cell biology of these integrins at two levels. First, we have analyzed their ligand binding mechanism and specificity. Second, we have studied their signaling function inside th…

IntegrinsCell typeReceptors CollagenbiologyCell adhesion moleculeIntegrinLigandsLigand (biochemistry)p38 Mitogen-Activated Protein KinasesMolecular biologyIntegrin alpha1beta1Collagen receptorCell biologybiology.proteinAnimalsHumansPlateletMitogen-Activated Protein KinasesSignal transductionReceptorMolecular BiologySignal TransductionMatrix Biology
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Integrin alpha 2 beta 1 promotes activation of protein phosphatase 2A and dephosphorylation of Akt and glycogen synthase kinase 3 beta.

2002

The integrins are a large family of heterodimeric transmembrane receptors composed of α and β subunits (22). In addition to mediating cell-matrix interactions, integrins have been shown to activate intracellular signaling pathways which, in collaboration with growth factor-induced signals, regulate cellular functions (46). Some integrin signaling cascades are activated via the β subunit cytoplasmic domain, and they are therefore triggered by several integrin heterodimers. These signals include the activation of protein tyrosine kinases of the Src and focal adhesion kinase (FAK) families (9, 47). More-recent studies have revealed signaling events that are activated specifically by an α subun…

IntegrinsReceptors CollagenIntegrinProtein Serine-Threonine KinasesCD49cp38 Mitogen-Activated Protein KinasesCollagen receptorGlycogen Synthase Kinase 3Proto-Oncogene ProteinsCell AdhesionPhosphoprotein PhosphatasesHumansIntegrin-linked kinaseProtein Phosphatase 2cdc42 GTP-Binding ProteinMolecular BiologyCell Growth and DevelopmentCells CulturedbiologyAkt/PKB signaling pathwayCell adhesion moleculeGlycogen Synthase KinasesCell BiologyCell biologyEnzyme ActivationBiochemistryIntegrin alpha MCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinIntegrin beta 6CollagenMitogen-Activated Protein KinasesProto-Oncogene Proteins c-aktProtein BindingSignal TransductionMolecular and cellular biology
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mGluR2/3 agonist LY379268, by enhancing the production of GDNF, induces a time-related phosphorylation of RET receptor and intracellular signaling Er…

2011

In the present study we aimed to verify if the enhancement of glial cell line-derived neurotrophic factor (GDNF) production in mouse striatum following treatment with LY379268 may also induce in the nigrostriatal system a time-related activation of RET receptor and its specific intracellular signaling. For this purpose, we have investigated the effects of LY379268 treatment on RET phosphorylation at the Tyr1062 and on downstream signaling Erk1/2, Akt and PLCγ1 pathway activation. The results showed that treatment with LY379268 (3 mg/kg) induces a significant increase of GDNF levels and time-related RET and Erk1/2 phosphorylation in the striatum. These increases were detected at 24 h and 48 …

Intracellular FluidMalemedicine.medical_specialtyTime FactorsMAP Kinase Signaling SystemSubstantia nigraStriatumReceptors Metabotropic GlutamateSettore BIO/09 - FisiologiaCellular and Molecular NeuroscienceMiceErk1/2Neurotrophic factorsInternal medicinemedicineGlial cell line-derived neurotrophic factorAnimalsGlial Cell Line-Derived Neurotrophic FactorAmino AcidsPhosphorylationReceptormGluR2/3Protein kinase BPharmacologyMitogen-Activated Protein Kinase 3biologyChemistryProto-Oncogene Proteins c-retLY379268Bridged Bicyclo Compounds HeterocyclicGDNFCorpus StriatumUp-RegulationMice Inbred C57BLEndocrinologynervous systembiology.proteinPhosphorylationTrK phosphorylationRETGDNF family of ligandsNeuropharmacology
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The Friedreich's Ataxia protein frataxin modulates DNA base excision repair in prokaryotes and mammals

2010

DNA-repair mechanisms enable cells to maintain their genetic information by protecting it from mutations that may cause malignant growth. Recent evidence suggests that specific DNA-repair enzymes contain ISCs (iron–sulfur clusters). The nuclearencoded protein frataxin is essential for the mitochondrial biosynthesis of ISCs. Frataxin deficiency causes a neurodegenerative disorder named Friedreich's ataxia in humans. Various types of cancer occurring at young age are associated with this disease, and hence with frataxin deficiency. Mice carrying a hepatocyte-specific disruption of the frataxin gene develop multiple liver tumours for unresolved reasons. In the present study, we show that frata…

Iron-Sulfur ProteinsDNA Repairmedicine.disease_causeBiochemistryDNA Glycosylases8-oxoG 78-dihydro-8-oxoguanineMice0302 clinical medicineIron-Binding Proteinsoxidative stressBER base excision repairCells CulturedMammalsMice Knockout0303 health sciencesfrataxinDMEM Dulbecco's modified Eagle's mediumbiologyLiver NeoplasmsSalmonella entericairon–sulfur clusterLife SciencesIron-binding proteinsTransfection3. Good healthLB Luria–BertaniOGG1 8-oxoguanine DNA glycosylase 1ISC iron–sulfur clusterFpg formamido-pyrimidine DNA glycosylaseHPRT hypoxanthine phosphoribosyltransferaseResearch ArticleDNA damageDNA repairSSB DNA single-strand breakTransfectionCell Line03 medical and health sciencesFRDA Friedreich's ataxiaROS reactive oxygen speciesmedicineAnimalsHumansMUTYH human mutY homologue (Escherichia coli)Molecular BiologyGene030304 developmental biologyFriedreich's ataxiaCell BiologyFibroblastsMolecular biologytumorigenesisProkaryotic CellsFriedreich AtaxiaDNA base excision repairDNA glycosylaseMutationHepatocytesFrataxinbiology.proteinInstitut für ErnährungswissenschaftCarcinogenesisMAPK mitogen-activated protein kinase030217 neurology & neurosurgeryDNA Damage
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Differential role of p38 mitogen activated protein kinase for cellular recovery from attack by pore-forming S. aureus alpha-toxin or streptolysin O.

2006

Following the observation that cells are able to recover from membrane lesions incurred by Staphylococcus aureus alpha-toxin and streptolysin O (SLO), we investigated the role of p38 in this process. p38 phosphorylation occurred in response to attack by both toxins, commencing within minutes after toxin treatment and waning after several hours. While SLO reportedly activates p38 via ASK1 and ROS, we show that this pathway does not play a major role for p38 induction in alpha-toxin-treated cells. Strikingly divergent effects of p38 blockade were noted depending on the toxin employed. In the case of alpha-toxin, inhibition of p38 within the time frame of its activation led to disruption of th…

KeratinocytesProgrammed cell deathStaphylococcus aureusCell Membrane Permeabilityp38 mitogen-activated protein kinasesBacterial ToxinsBiophysicsBiologymedicine.disease_causeMAP Kinase Kinase Kinase 5Biochemistryp38 Mitogen-Activated Protein KinasesMicrobiologyHemolysin ProteinsAdenosine TriphosphateBacterial ProteinsProto-Oncogene ProteinsmedicineHumansASK1PhosphorylationMolecular BiologyCells CulturedPore-forming toxinToxinCell MembraneCell BiologyProtein-Tyrosine KinasesBlockadeCell biologyEnzyme ActivationStreptolysinsPhosphorylationStreptolysinBiochemical and biophysical research communications
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