Search results for "PROTEIN KINASE"

showing 10 items of 1188 documents

Inhibition of Mitochondrial Function by Efavirenz Increases Lipid Content in Hepatic Cells

2010

Efavirenz (EFV) is a non-nucleoside reverse transcriptase inhibitor (NNRTI) widely used in human immunodeficiency virus (HIV) infection therapy. It has been associated with hepatotoxic effects and alterations in lipid and body fat composition. Given the importance of the liver in lipid regulation, we have evaluated the effects of clinically used concentrations of EFV on the mitochondria and lipid metabolism of human hepatic cells in vitro. Mitochondrial function was rapidly undermined by EFV to an extent that varied with the concentration employed; in particular, respiration and intracellular adenosine triphosphate (ATP) levels were reduced whereas reactive oxygen species (ROS) production i…

CyclopropanesMaleEfavirenzAnti-HIV AgentsRespiratory chainMitochondria LiverPharmacologyBiologyMitochondrionNucleoside Reverse Transcriptase InhibitorRats Sprague-Dawleychemistry.chemical_compoundOxygen ConsumptionAMP-Activated Protein Kinase KinasesmedicineAnimalsHumansHepatologyAMPKLipid metabolismLipid MetabolismAdenosineLipidsBenzoxazinesRatschemistryBiochemistryAlkynesHepatocytesAdenosine triphosphateProtein Kinasesmedicine.drug
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Isoenzyme-specific phosphorylation of cytochromes P-450 and other drug metabolizing enzymes.

1987

Abstract A series of fourteen cytochrome P-450 isoenzymes was treated with three different protein kinases and found to devide into isoenzymes phosphorylated (i) by both the cyclic AMP-dependent kinase and the calcium-phospholipid-dependent kinase (P-450 PB 3a and PB 2e), (ii) by none of these kinases (P-450 PB 1b, MC 1b, UT 1, and thromboxane synthase), and (iii) by either the cyclic AMP-dependent kinase (P-450 LM 2, PB 2d, and PB 3b) or the calcium-phospholipid-dependent kinase (P-450 PB 1a, PB 2a, MC 1a, LM 3c, and LM 4). Other components of the monooxygenase system, cytochrome P-450 reductase, cytochrome b5, cytochrome b5 reductase as well as microsomal epoxide hydrolase, were poor subs…

CytochromeBiophysicsReductaseBiochemistrySubstrate SpecificityCytochrome P-450 Enzyme SystemCytochrome b5Cyclic AMPAnimalsPhosphorylationMolecular BiologyCytochrome b5 reductaseProtein Kinase CGlutathione TransferasebiologyChemistryKinaseCell BiologyMonooxygenaseMolecular biologyRatsIsoenzymesBiochemistryPharmaceutical PreparationsMicrosomal epoxide hydrolasebiology.proteinThromboxane-A synthaseRabbitsCasein KinasesProtein KinasesBiochemical and biophysical research communications
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Phosphorylation of rabbit liver cytochrome P-450 LM2 and its effect on monooxygenase activity

1984

The phosphorylation of rabbit liver microsomal cytochrome P-450 LM2 by catalytic subunit of cyclic AMP-dependent protein kinase (W. Pyerin et al. (1983) Carcinogenesis 4, 573) has now been studied in detail with purified soluble form of cytochrome P-450 as well as with the purified protein incorporated into model membranes. The apparent Km values for P-450 of the phosphorylation reaction in all experimental systems were in a range of 2-8 microM, while the Vmax values were dependent on the state of P-450. Upon phosphorylation, the reconstituted enzyme activities with benzphetamine (N-demethylation) and 7-ethoxycoumarin (O-deethylation) as substrates were reduced to 30-40% of control.

CytochromeProtein subunitBiophysicsBiochemistryMixed Function OxygenasesCytochrome P-450 Enzyme SystemmedicineAnimalsPhosphorylationProtein kinase AMolecular Biologychemistry.chemical_classificationbiologyKinaseCell BiologyMolecular biologyKineticsEnzymechemistryBiochemistryPhenobarbitalMicrosomes Liverbiology.proteinMicrosomePhosphorylationRabbitsBenzphetamineProtein Kinasesmedicine.drugBiochemical and Biophysical Research Communications
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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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Molecular basis of the functional distinction between Cln1 and Cln2 cyclins

2012

Cln1 and Cln2 are very similar but not identical cyclins. In this work, we tried to describe the molecular basis of the functional distinction between Cln1 and Cln2. We constructed chimeric cyclins containing different fragments of Cln1 and Cln2 and performed several functional analysis that make it possible to distinguish between Cln1 or Cln2. We identified that region between amino acids 225 and 299 of Cln2 is not only necessary but also sufficient to confer Cln2 specific functionality compared with Cln1. We also studied Cln1 and Cln2 subcellular localization identifying additional differences between them. Both cyclins are distributed between the nucleus and the cytoplasm, but Cln1 shows…

CytoplasmSaccharomyces cerevisiae ProteinsTranscription GeneticBlotting WesternGenes FungalGenetic VectorsGreen Fluorescent ProteinsActive Transport Cell NucleusSaccharomyces cerevisiaeKaryopherinsBiologyReportCyclinsGene Expression Regulation FungalmedicineAmino Acid SequenceNuclear export signalMolecular BiologyPeptide sequenceCyclinKaryopherinCell Nucleuschemistry.chemical_classificationCell Cycle CheckpointsCell BiologySubcellular localizationCell nucleusmedicine.anatomical_structureBiochemistrychemistryCytoplasmNuclear transportCDC28 Protein Kinase S cerevisiaePlasmidsDevelopmental BiologyCell Cycle
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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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Combining dasatinib with dexamethasone long-term leads to maintenance of antiviral and antileukemia specific cytotoxic T cell responses in vitro

2012

Maintaining graft versus leukemia (GvL) and antivirus responses of cytotoxic T cells (CTLs) while suppressing graft-versus-host disease (GvHD) remains a challenge after allogeneic bone marrow transplantation. Clinical observations indicate that combining glucocorticoids with multi-tyrosine-kinase inhibitors could be a successful therapeutic approach. We and others have shown that the BCR-ABL/SRC kinase inhibitor dasatinib may enhance or suppress T cells in vitro. In this report, we evaluated combination effects of dasatinib and dexamethasone on CD3 + and virus-specific CD8 + T cells directly ex vivo and on antigen-specific leukemia-reactive and alloreactive CD8 + T cell clones. Functional o…

Cytotoxicity ImmunologicHerpesvirus 4 HumanCancer ResearchNaive T cellT cellDasatinibDrug Evaluation PreclinicalReceptors Antigen T-CellCytomegalovirusApoptosisT-Cell Antigen Receptor SpecificityBiologyLymphocyte ActivationCell DegranulationDexamethasoneAntigenHLA AntigensT-Lymphocyte SubsetsGeneticsmedicineHumansCytotoxic T cellAntigens ViralProtein Kinase InhibitorsMolecular BiologyCells CulturedDegranulationDrug SynergismT-Lymphocytes Helper-InducerCell BiologyHematologyDasatinibThiazolesPyrimidinesmedicine.anatomical_structureImmunologyCancer researchCytokinesK562 CellsMemory T cellCell DivisionCD8Signal TransductionT-Lymphocytes Cytotoxicmedicine.drugExperimental Hematology
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Effect of the protein kinase inhibitors, 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine H-7 and N-(2-[methylamino]ethyl)-5-isoquinoline-sulfonamide H…

1998

The effects of 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine H-7 (a cAMP-dependent protein kinase and protein kinase C inhibitor), n-(2-[methylamino]ethyl)-5-isoquinoline-sulfonamide H-8 (a cAMP- and cGMP-dependent protein kinase inhibitor) and indomethacin (IND, a cyclooxygenase inhibitor) on both the spontaneous metastatic ability of 3LL (Lewis lung carcinoma) tumor cells and anti-tumor host response were studied. The study of tumor progression showed that H-7 and H-8 (2 mg kg(-1) day(-1) , i.p., for 8 days) significantly reduced the mean number of metastases (0.8 +/- 0.2 and 1.0 +/- 0.7, respectively, P0.05) with respect to the number of lung metastases (4.2 +/- 2.1) observed in the con…

Cytotoxicity ImmunologicMalemedicine.medical_specialtymedicine.drug_classIndomethacinCarcinoma Lewis LungMiceInternal medicine1-(5-Isoquinolinesulfonyl)-2-MethylpiperazinemedicineAnimalsCyclooxygenase InhibitorsLymphocytesEnzyme InhibitorsNeoplasm MetastasisCytotoxicityProtein kinase AProtein kinase CPharmacologybiologyLewis lung carcinomaProtein kinase inhibitorIsoquinolinesMice Inbred C57BLEndocrinologyEnzyme inhibitorTumor progressionbiology.proteinCancer researchDisease ProgressionLeukocytes MononuclearCyclooxygenaseCell DivisionNeoplasm TransplantationSpleenEuropean journal of pharmacology
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A loop involving NRF2, miR‐29b‐1‐5p and AKT, regulates cell fate of MDA‐MB‐231 triple‐negative breast cancer cells

2019

The present study shows that nuclear factor erythroid 2-related factor 2 (NRF2) and miR-29b-1-5p are two opposite forces which could regulate the fate of MDA-MB-231 cells, the most studied triple-negative breast cancer (TNBC) cell line. We show that NRF2 activation stimulates cell growth and markedly reduces reactive oxygen species (ROS) generation, whereas miR-29b-1-5p overexpression increases ROS generation and reduces cell proliferation. Moreover, NRF2 downregulates miR-29b-1-5p expression, whereas miR-29b-1-5p overexpression decreases p-AKT and p-NRF2. Furthermore, miR-29b-1-5p overexpression induces both inhibition of DNA N-methyltransferases (DNMT1, DNMT3A, and DNMT3B) expression and …

DNA (Cytosine-5-)-Methyltransferase 10301 basic medicineNF-E2-Related Factor 2PhysiologyClinical BiochemistryTriple Negative Breast NeoplasmsAKT DNMTs miR‐29b‐1‐5p NRF2 parthenolide tumor suppressor genesCell fate determinationenvironment and public healthDNA Methyltransferase 3A03 medical and health scienceschemistry.chemical_compound0302 clinical medicineSettore BIO/10 - BiochimicaCell Line TumorCyclin D2HumansParthenolideDNA (Cytosine-5-)-MethyltransferasesProtein kinase BTriple-negative breast cancerCell Proliferationchemistry.chemical_classificationReactive oxygen speciesCell growthTumor Suppressor ProteinsCell BiologyDNA Methylationrespiratory systemCell biologyGene Expression Regulation NeoplasticMicroRNAs030104 developmental biologychemistryCell culture030220 oncology & carcinogenesisDNMT1FemaleReactive Oxygen SpeciesProto-Oncogene Proteins c-aktSesquiterpenesSignal TransductionJournal of Cellular Physiology
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