Search results for " Protein kinases"

showing 10 items of 342 documents

N-acetyl-L-cysteine (NAC) inhibit mucin synthesis and pro-inflammatory mediators in alveolar type II epithelial cells infected with influenza virus A…

2011

64% of chronic obstructive pulmonary disease (COPD) exacerbations are caused by respiratory infections including influenza (strains A and B) and respiratory syncytial virus (RSV). They affect the airway epithelium increasing inflammatory and apoptosis events through mechanisms involving ROS generation, and induce the release of mucins from epithelial cells that are involved in the deterioration of the patient's health during the course of the disease. The antioxidant NAC has proved useful in the management of COPD reducing symptoms, exacerbations and accelerated lung function decline. It has been shown to inhibit influenza virus replication and to diminish the release of inflammatory and ap…

BiologyMucin 5ACmedicine.disease_causeVirus ReplicationBiochemistryp38 Mitogen-Activated Protein KinasesVirusCell LinePulmonary Disease Chronic ObstructivemedicineHumansInterleukin 8PhosphorylationPharmacologyA549 cellMucinNF-kappa BAcetylcysteineRespiratory Syncytial VirusesPulmonary AlveoliInfluenza B virusRespiratory syncytial virus (RSV)Viral replicationApoptosisInfluenza A virusImmunologyRespiratory epitheliumInflammation MediatorsBiochemical pharmacology
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TORC1 controls G1–S cell cycle transition in yeast via Mpk1 and the greatwall kinase pathway

2015

The target of rapamycin complex 1 (TORC1) pathway couples nutrient, energy and hormonal signals with eukaryotic cell growth and division. In yeast, TORC1 coordinates growth with G1–S cell cycle progression, also coined as START, by favouring the expression of G1 cyclins that activate cyclin-dependent protein kinases (CDKs) and by destabilizing the CDK inhibitor Sic1. Following TORC1 downregulation by rapamycin treatment or nutrient limitation, clearance of G1 cyclins and C-terminal phosphorylation of Sic1 by unknown protein kinases are both required for Sic1 to escape ubiquitin-dependent proteolysis prompted by its flagging via the SCFCdc4 (Skp1/Cul1/F-box protein) ubiquitin ligase complex.…

BioquímicaBiologiaSaccharomyces cerevisiae ProteinsImmunoblottingGeneral Physics and AstronomyCell Cycle ProteinsSaccharomyces cerevisiaeMechanistic Target of Rapamycin Complex 1ArticleGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciences0302 clinical medicineCyclin-dependent kinaseCyclinsImmunoprecipitationProtein Phosphatase 2Cell division control protein 4PhosphorylationProtein kinase ACyclin-Dependent Kinase Inhibitor Proteins030304 developmental biology0303 health sciencesMultidisciplinarybiologyTOR Serine-Threonine KinasesUbiquitin-Protein Ligase ComplexesGeneral ChemistryBlotting NorthernFlow CytometryG1 Phase Cell Cycle CheckpointsSic1Cyclin-Dependent KinasesCell biologyBiochemistryMultiprotein Complexes030220 oncology & carcinogenesisUbiquitin ligase complexbiology.proteinIntercellular Signaling Peptides and ProteinsPhosphorylationTOR Serine-Threonine KinasesMitogen-Activated Protein KinasesPeptidesProtein KinasesCyclin-dependent kinase inhibitor proteinNature Communications
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Specific and global regulation of mRNA stability during osmotic stress in Saccharomyces cerevisiae.

2009

Hyperosmotic stress yields reprogramming of gene expression in Saccharomyces cerevisiae cells. Most of this response is orchestrated by Hog1, a stress-activated, mitogen-activated protein kinase (MAPK) homologous to human p38. We investigated, on a genomic scale, the contribution of changes in transcription rates and mRNA stabilities to the modulation of mRNA amounts during the response to osmotic stress in wild-type and hog1 mutant cells. Mild osmotic shock induces a broad mRNA destabilization; however, osmo-mRNAs are up-regulated by increasing both transcription rates and mRNA half-lives. In contrast, mild or severe osmotic stress in hog1 mutants, or severe osmotic stress in wild-type cel…

BioquímicaMessenger RNASaccharomyces cerevisiae ProteinsTranscription GeneticOsmotic shockMRNA destabilizationRNA Stabilityp38 mitogen-activated protein kinasesSaccharomyces cerevisiaeMRNA stabilizationSaccharomyces cerevisiaeBiologybiology.organism_classificationMolecular biologyArticleGenètica molecularCell biologyOsmotic PressureGene Expression Regulation FungalGene expressionOsmotic pressureRNA MessengerMitogen-Activated Protein KinasesMolecular Biology
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Structure-activity relationship of staurosporine analogs in regulating expression of endothelial nitric-oxide synthase gene.

2000

In human umbilical vein endothelial cells and in human umbilical vein endothelial cell-derived EA.hy 926 cells, staurosporine (Stsp) and its glycosidic indolocarbazole analogs 7-hydroxystaurosporine (UCN-01) and 4'-N-benzoyl staurosporine (CGP 41251) enhanced nitric-oxide synthase (NOS) III mRNA expression (analyzed by RNase protection assay), protein expression (determined by Western blot), and activity [measured by rat fetal lung fibroblast (RFL-6) reporter cell assay] in a concentration- and time-dependent manner. In contrast, the bisindolylmaleimide analogs GF 109203X, Ro 31-8220 and Go 6983 had no effect on NOS III expression, and Go 6976, a methyl- and cyanoalkyl-substituted nonglycos…

BisindolylmaleimideNitric Oxide Synthase Type IIIBiologyEndothelial NOSNitric OxideGene Expression Regulation Enzymologicchemistry.chemical_compoundStructure-Activity RelationshipAlkaloidsmedicineCyclic GMP-Dependent Protein KinasesStaurosporineAnimalsHumansDrug InteractionsRNA MessengerEnzyme InhibitorsProtein kinase APromoter Regions GeneticProtein Kinase InhibitorsProtein kinase CCells CulturedProtein Kinase CPharmacologyKinaseTumor Necrosis Factor-alphaNitric Oxide Synthase Type IIIProtein-Tyrosine KinasesStaurosporineMolecular biologyCyclic AMP-Dependent Protein KinasesRatschemistryMolecular MedicineEndothelium VascularNitric Oxide SynthaseTyrosine kinaseProtein Kinasesmedicine.drugMolecular pharmacology
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Exercise and Metformin Intervention Prevents Lipotoxicity-Induced Hepatocyte Apoptosis by Alleviating Oxidative and ER Stress and Activating the AMPK…

2022

Objective. Nonalcoholic fatty liver disease (NAFLD) and type 2 diabetes (T2DM) commonly coexist and act synergistically to drive adverse clinical outcomes. This study is aimed at investigating the effects of exercise intervention and oral hypoglycaemic drug of metformin (MET) alone or combined on hepatic lipid accumulation. To investigate if oxidative stress and endoplasmic reticulum stress (ERS) are involved in lipotoxicity-induced hepatocyte apoptosis in diabetic mice and whether exercise and/or MET alleviated oxidative stress or ERS-apoptosis by AMPK-Nrf2-HO-1 signaling pathway. Methods. Forty db/db mice with diabetes ( random   blood   glucose ≥ 250   mg / dL ) were randomly allocated i…

Blood GlucoseAgingArticle SubjectNF-E2-Related Factor 2metformiiniApoptosisAMP-Activated Protein KinasesBiochemistryAntioxidantsDiabetes Mellitus ExperimentalMiceohjelmoitunut solukuolemaSuperoxide Dismutase-1aineenvaihduntahäiriötAnimalsHypoglycemic AgentsHematoxylinoksidatiivinen stressibcl-2-Associated X ProteinCaspase 3Cell BiologyGeneral MedicineEndoplasmic Reticulum StressLipidsMetforminOxidative StressDiabetes Mellitus Type 2ei-alkoholiperäinen rasvamaksasairausHepatocyteslääkehoitoEosine Yellowish-(YS)koe-eläinmallitaikuistyypin diabetesSignal TransductionliikuntahoitoOxidative Medicine and Cellular Longevity
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Dual role of the p38 MAPK/cPLA2 pathway in the regulation of platelet apoptosis induced by ABT-737 and strong platelet agonists.

2013

p38 Mitogen-activated protein (MAP) kinase is involved in the apoptosis of nucleated cells. Although platelets are anucleated cells, apoptotic proteins have been shown to regulate platelet lifespan. However, the involvement of p38 MAP kinase in platelet apoptosis is not yet clearly defined. Therefore, we investigated the role of p38 MAP kinase in apoptosis induced by a mimetic of BH3-only proteins, ABT-737, and in apoptosis-like events induced by such strong platelet agonists as thrombin in combination with convulxin (Thr/Cvx), both of which result in p38 MAP kinase phosphorylation and activation. A p38 inhibitor (SB202190) inhibited the apoptotic events induced by ABT-737 but did not influ…

Blood PlateletsCancer ResearchcPLA2p38 mitogen-activated protein kinasesImmunologyBlotting Westernp38 Mitogen-Activated Protein KinasesPiperazinesNitrophenolsCellular and Molecular NeurosciencePhospholipase A2Crotalid VenomsHumansLectins C-Typeddc:610Cells CulturedMembrane Potential MitochondrialplateletSulfonamidesbiologyKinaseGroup IV Phospholipases A2Biphenyl CompoundsapoptosisConvulxinCell BiologyFlow Cytometryp38 MAP kinaseCell biologyApoptosisMitogen-activated protein kinasebiology.proteinPhosphorylationOriginal ArticleSignal transductionReactive Oxygen SpeciesSignal TransductionCell deathdisease
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Differential roles of cAMP and cGMP in megakaryocyte maturation and platelet biogenesis

2012

The cyclic nucleotides cyclic adenosine monophosphate (cAMP) and cyclic guanosine monophosphate (cGMP) regulate the activity of protein kinase A (PKA) and protein kinase G (PKG), respectively. This process helps maintain circulating platelets in a resting state. Here we studied the role of cAMP and cGMP in the regulation of megakaryocyte (MK) differentiation and platelet formation. Cultured, platelet-producing MKs were differentiated from fetal livers harvested from 13.5 days postcoital mouse embryos. MK development was accompanied by a dramatic increase in cAMP production and expression of soluble guanylate cyclase, PKG, and PKA as well as their downstream targets vasodilator-stimulated ph…

Blood PlateletsCancer Researchmegakaryocytes; cAMP; cGMP; plateletsPhosphodiesterase 3BiologyArticleAdenylyl cyclaseMicechemistry.chemical_compoundPregnancyCyclic AMPGeneticsAnimalsCyclic adenosine monophosphatePhosphorylationProtein kinase ACyclic GMPMolecular BiologyCyclic guanosine monophosphateMicrofilament ProteinsCell DifferentiationCell BiologyHematologyPhosphoproteinsCyclic AMP-Dependent Protein KinasesCell biologyMice Inbred C57BLCytoskeletal ProteinsThrombopoietinchemistrycAMP-dependent pathwayFemalePDE10ASignal transductionCell Adhesion MoleculesMegakaryocytesExperimental Hematology
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Time-resolved characterization of cAMP/PKA-dependent signaling reveals that platelet inhibition is a concerted process involving multiple signaling p…

2014

One of the most important physiological platelet inhibitors is endothelium-derived prostacyclin which stimulates the platelet cyclic adenosine monophosphate/protein kinase A (cAMP/PKA)-signaling cascade and inhibits virtually all platelet-activating key mechanisms. Using quantitative mass spectrometry, we analyzed time-resolved phosphorylation patterns in human platelets after treatment with iloprost, a stable prostacyclin analog, for 0, 10, 30, and 60 seconds to characterize key mediators of platelet inhibition and activation in 3 independent biological replicates. We quantified over 2700 different phosphorylated peptides of which 360 were significantly regulated upon stimulation. This com…

Blood PlateletsImmunologyProstacyclinBiologyBiochemistrychemistry.chemical_compoundCyclic AMPmedicineHumansCyclic adenosine monophosphateIloprostProtein Interaction MapsPlatelet activationPhosphorylationProtein kinase AKinaseCell BiologyHematologyPlatelet ActivationCyclic AMP-Dependent Protein KinaseschemistryBiochemistryPlatelet aggregation inhibitorPhosphorylationSignal transductionPlatelet Aggregation InhibitorsSignal Transductionmedicine.drugBlood
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Potential and limitations of PKA/ PKG inhibitors for platelet studies

2021

Cyclic nucleotides (cAMP and cGMP) and corresponding protein kinases, protein kinase A (PKA) and protein kinase G (PKG), are the main intracellular mediators of endothelium-derived platelet inhibitors. Pharmacological PKA/PKG inhibitors are often used to discriminate between these two kinase activities and to analyze their underlying mechanisms. Previously we showed that all widely used PKG inhibitors (KT5823, DT3, RP isomers) either did not inhibit PKG or inhibited and even activated platelets independently from PKG. In this study, we examined several PKA inhibitors as well as inhibitors of adenylate and guanylate cyclases to reveal their effects on platelets and establish whether they are…

Blood PlateletsKinaseIntracellular Signaling Peptides and ProteinsAdenylate kinaseHematologyGeneral MedicineKT5720Cyclic AMP-Dependent Protein Kinaseschemistry.chemical_compoundchemistryBiochemistryCyclic AMPCyclic GMP-Dependent Protein Kinasescardiovascular systemHumansPlateletPlatelet activationProtein kinase ACyclic GMPcGMP-dependent protein kinaseIntracellularPlatelets
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Activation of cGMP-dependent Protein Kinase Iβ Inhibits Interleukin 2 Release and Proliferation of T Cell Receptor-stimulated Human Peripheral T Cells

2000

Several major functions of type I cGMP-dependent protein kinase (cGK I) have been established in smooth muscle cells, platelets, endothelial cells, and cardiac myocytes. Here we demonstrate that cGK Ibeta is endogenously expressed in freshly purified human peripheral blood T lymphocytes and inhibits their proliferation and interleukin 2 release. Incubation of human T cells with the NO donor, sodium nitroprusside, or the membrane-permeant cGMP analogs PET-cGMP and 8-pCPT-cGMP, activated cGK I and produced (i) a distinct pattern of phosphorylation of vasodilator-stimulated phosphoprotein, (ii) stimulation of the mitogen-activated protein kinases ERK1/2 and p38 kinase, and, upon anti-CD3 stimu…

Blood PlateletsNitroprussideInterleukin 2Cell Membrane PermeabilityCD3 ComplexT-Lymphocytesp38 mitogen-activated protein kinasesT cellReceptors Antigen T-CellCell SeparationBiologyLymphocyte ActivationBiochemistryJurkat cellsJurkat CellsCyclic AMPCyclic GMP-Dependent Protein KinasesmedicineHumansProtein kinase ACyclic GMPMolecular BiologyCyclic GMP-Dependent Protein Kinase Type IKinaseCell growthMicrofilament ProteinsCell BiologyPhosphoproteinsMolecular biologyCell biologyEnzyme ActivationAlternative Splicingmedicine.anatomical_structureInterleukin-2Mitogen-Activated Protein KinasesCell Adhesion MoleculescGMP-dependent protein kinasemedicine.drugJournal of Biological Chemistry
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