Search results for "protein kinase A"

showing 10 items of 231 documents

DNA replication arrest in response to genotoxic stress provokes early activation of stress-activated protein kinases (SAPK/JNK).

2009

Abstract The impact of DNA damage-induced replication blockage for early activation of stress kinases [stress-activated protein kinase (SAPK)/c-Jun N-terminal kinase (JNK)] is largely unknown. Here, we show that induction of dual phosphorylation of SAPK/JNK by the DNA polymerase inhibitor aphidicolin was not ameliorated by additional exposure to ultraviolet (UV) light, indicating that overlapping mechanisms participate in signaling to SAPK/JNK triggered by both agents. UV-induced DNA replication blockage, cyclobutane pyrimidine dimer formation and DNA strand break induction coincided with SAPK/JNK phosphorylation at early (≤ 30 min) but not late (≥ 2 h) time points after exposure. Genotoxin…

AphidicolinDNA ReplicationDNA damageUltraviolet RaysPoly ADP ribose polymeraseCell Linechemistry.chemical_compoundMiceAphidicolinStructural BiologyCricetinaeAnimalsHumansLymphocytesPhosphorylationProtein kinase AMolecular BiologyNucleic Acid Synthesis InhibitorsBRCA2 ProteinMice KnockoutbiologyKinaseCell CycleDNA replicationJNK Mitogen-Activated Protein KinasesFibroblastsMolecular biologyProliferating cell nuclear antigenDNA-Binding ProteinsEnzyme ActivationchemistryPyrimidine Dimersbiology.proteinPhosphorylationApoptosis Regulatory ProteinsDNA DamageJournal of molecular biology
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4-(4-Fluorophenyl)-2-methyl-3-(1-oxy-4-pyridyl)isoxazol-5(2H)-one

2008

The crystal structure of the title compound, C15H11FN2O3, was determined as part of a study on the biological activity of isoxazolone derivatives as p38 mitogen-activated protein kinase (MAPK) inhibitors. The dihedral angles between rings are isoxazole/benzene = 55.0 (3)°, isoxazole/pyridine = 33.8 (2)° and benzene/pyridine = 58.1 (2)°.

Biological activityGeneral ChemistryCrystal structureDihedral angleCondensed Matter PhysicsBioinformaticsOrganic PapersMedicinal chemistrylcsh:Chemistrychemistry.chemical_compoundlcsh:QD1-999chemistryPyridineGeneral Materials ScienceIsoxazoleBenzeneProtein kinase AActa Crystallographica Section E Structure Reports Online
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Mechanisms of cell activation by heavy metal ions

1998

Heavy metal ions can be released by corroding metallic implants into the surrounding tissue. When they enter blood vessels some of them are carried by proteins like albumin and can be taken up by endothelial cells lining the vessels. To study their involvement in the inflammatory response we investigated heavy metal ion induced effects in cultured human vascular endothelial cells (HUVECs). NiCl2 and CoCl2 upregulate, especially in concentrations of 1 mM, the expression of adhesion molecules (e.g., E-selectin and intercellular adhesion molecule-1), as well as the cytokines IL-6 and IL-8, as shown by enzyme immunoassay and Northern blot analysis. In addition, possible signal transduction mech…

BiomaterialsEndothelial stem cellBiochemistryChemistryKinaseCell adhesion moleculeIntercellular Adhesion Molecule-1Biomedical EngineeringSignal transductionCell activationProtein kinase ACell biologyProinflammatory cytokineJournal of Biomedical Materials Research
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Phosphorylation of cytochromes P450: First discovery of a posttranslational modification of a drug-metabolizing enzyme

2005

Cytochromes P450 (CYP) are important components of xenobiotic-metabolizing monooxygenases (CYP-dependent monooxygenases). Their regulation by induction, most commonly by transcriptional activation, mediated by xenobiotics, normally substrates of the corresponding CYP, is well known and has been widely studied. Our team has discovered an additional important regulation of xenobiotic-metabolizing CYPs pertaining to posttranslational modification by phosphorylation. Individual CYPs are phosphorylated by different protein kinases, leading to CYP isoenzyme-selective changes in the metabolism of individual substrates and consequent drastic changes in the control of genotoxic metabolites. Best stu…

Biophysicsurologic and male genital diseasesBiochemistryCytochrome P-450 Enzyme SystemAnimalsHumansheterocyclic compoundsPhosphorylationEnzyme inducerProtein kinase AMolecular BiologyTranscription factorRegulation of gene expressionbiologyKinaseorganic chemicalsCell Biologyrespiratory systemMonooxygenaseenzymes and coenzymes (carbohydrates)LiverBiochemistrybiology.proteinPhosphorylationProtein Processing Post-TranslationalNuclear localization sequenceMutagensBiochemical and Biophysical Research Communications
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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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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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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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