Search results for "protein kinase C"

showing 10 items of 180 documents

Depletion of tumour glutathione in vivo by buthionine sulphoximine: modulation by the rate of cellular proliferation and inhibition of cancer growth.

1993

We have investigated in Ehrlich-ascites-tumour-bearing mice the effect of buthionine sulphoximine (BSO), a selective inhibitor of GSH synthesis, on the rate of GSH depletion of tumour versus normal tissues and its relation to tumour cell proliferation. In normal tissues, GSH and GSSG remain unchanged or close to normal values during tumour growth, even at the last stage of growth when the animal is close to death. After administration of a single dose of BSO (4 mmol/kg), the rates of GSH depletion and recovery in the tumour and in several normal tissues are very different. BSO depletes GSH in cancer cells to a level of 0.3-0.4 mumol/g. The fall in GSH levels is faster when tumour cells do n…

MaleAntimetabolites AntineoplasticIntracellular pHPharmacologyBiologyBiochemistrychemistry.chemical_compoundMiceIn vivoMethionine SulfoximineAnimalsButhionine sulfoximineCarcinoma Ehrlich TumorMolecular BiologyButhionine SulfoximineProtein kinase CDose-Response Relationship DrugCell growthCell BiologyGlutathioneGlutathioneDose–response relationshipchemistryBiochemistryCancer cellCell DivisionResearch Article
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Activation of L-arginine transport by protein kinase C in rabbit, rat and mouse alveolar macrophages

1998

1 The role of protein kinase C in controlling L-arginine transport in alveolar macrophages was investigated. 2 L-[3H]Arginine uptake in rabbit alveolar macrophages declined by 80 % after 20 h in culture. 4β-Phorbol 12-myristate 13-acetate (PMA), but not 4α-phorbol 12-myristate 13-acetate (α-PMA), present during 20 h culture, enhanced L-[3H]arginine uptake more than 10-fold. Staurosporine and chelerythrine opposed this effect. 3 L-[3H]Arginine uptake was saturable and blockable by L-lysine. After PMA treatment Vmax was increased more than 5-fold and Km was reduced from 0.65 to 0.32 mM. 4 Time course experiments showed that PMA increased L-[3H]arginine uptake almost maximally within 2 h. This…

MaleArgininePhysiologyMice Inbred StrainsStimulationCycloheximideArginineTritiumL-arginine transportRats Sprague-DawleyMicechemistry.chemical_compoundSpecies SpecificityLeucineMacrophages AlveolarmedicineAnimalsStaurosporineRNA MessengerEnzyme InhibitorsProtein Kinase CProtein kinase CbiologySodiumMembrane ProteinsBiological TransportRabbit ratOriginal Articlesbiology.organism_classificationMolecular biologyRatsKineticsChelerythrinechemistryEthylmaleimideCarcinogensAmino Acid Transport Systems BasicTetradecanoylphorbol AcetateFemaleRabbitsCarrier Proteinsmedicine.drugThe Journal of Physiology
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Vitamin E activates CRABP-II gene expression in cultured human fibroblasts, role of protein kinase C

2004

The treatment of human fibroblasts with different tocopherols in the presence of retinol caused an increase in cytoplasmic retinoic acid binding protein II (CRABP-II) mRNA and protein. The possibility of an involvement of protein kinase C (PKC) in the response to tocopherols was supported by the results obtained with the PKC-specific inhibitors, calphostin C and bisindolylmaleimide I. The effect of alpha-tocopherol was prevented by okadaic acid, suggesting that a protein phosphatase is responsible for PKC dephosphorylation produced by the presence of tocopherols. The results shown support the hypothesis that phosphorylation/dephosphorylation of RXRalpha via PKC may be involved in the regula…

MaleBisindolylmaleimideTranscription GeneticReceptors Retinoic AcidPhosphatasealpha-TocopherolBiophysicsBiochemistryDephosphorylationchemistry.chemical_compoundStructural BiologyProtein kinase COkadaic AcidGeneticsHumansVitamin ERNA MessengerRetinoic acid bindingPhosphorylationMolecular BiologyProtein kinase CCells CulturedDNA PrimersBase SequenceReverse Transcriptase Polymerase Chain ReactionInfant NewbornRetinoid X receptor αCell BiologyMolecular biologyRetinoic acid receptorCalphostin CchemistryGene Expression RegulationProtein phosphatasePhosphorylationFibroblastCytoplasmic retinoic acid binding protein IIFEBS Letters
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Midostaurin upregulates eNOS gene expression and preserves eNOS function in the microcirculation of the mouse

2005

Nitric oxide (NO) derived from endothelial NO synthase (eNOS) is a powerful vasodilator and possesses vasoprotective effects. Therefore, augmentation of eNOS expression and -activity by pharmacological means could provide protection against cardiovascular disease. However, this concept has been questioned recently, because in several disease models, eNOS upregulation was associated with a dysfunctional enzyme (referred to as eNOS uncoupling). In contrast, the present study demonstrates that an eNOS gene expression-enhancing compound with additional protein kinase C (PKC) inhibitory properties can upregulate eNOS while preserving its enzymatic function. Apolipoprotein E-knockout mice were tr…

MaleCancer ResearchNitric Oxide Synthase Type IIIPhysiologyClinical BiochemistryNitric Oxide Synthase Type IIBiologyPharmacologyBiochemistryNitric oxideMicechemistry.chemical_compoundApolipoproteins EEnosmedicineAnimalsStaurosporineRNA MessengerMidostaurinAortaNitritesProtein kinase CMice KnockoutNitratesMicrocirculationStaurosporinebiology.organism_classificationVasoprotectiveVasodilationNitric oxide synthaseBiochemistrychemistryEnzyme Inductionbiology.proteinNitric Oxide SynthaseReactive Oxygen SpeciesIntravital microscopymedicine.drugNitric Oxide
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Studies on protein kinases involved in regulation of nucleocytoplasmic mRNA transport

1988

The rate of energy-dependent nucleoside triphosphatase (NTPase)-mediated nucleocytoplasmic translocation of poly(A)-containing mRNA [poly(A)+mRNA] across the nuclear envelope is thought to be regulated by poly(A)-sensitive phosphorylation and dephosphorylation of nuclear-envelope protein. Studying the phosphorylation-related inhibition of the NTPase, we found that phosphorylation of one polypeptide of rat liver envelopes by endogenous NI- and NII-like protein kinase was particularly sensitive to poly(A). This polypeptide (106 kDa) was also phosphorylated by nuclear-envelope-bound Ca2+-activated and phospholipid-dependent protein kinase (protein kinase C). Activation of kinase C by tumour-pr…

MaleCytoplasmNuclear EnvelopeMitogen-activated protein kinase kinasePhosphatidylinositolsBiochemistryMAP2K7AnimalsRNA Messengerc-RafProtein kinase AMolecular BiologyProtein Kinase CProtein kinase CCell NucleusMembrane GlycoproteinsMAP kinase kinase kinasebiologyCyclin-dependent kinase 2Membrane ProteinsNuclear ProteinsBiological TransportRats Inbred StrainsCell BiologyMolecular biologyRatsNuclear Pore Complex ProteinsMicroscopy ElectronLiverBiochemistrybiology.proteinCyclin-dependent kinase 9PeptidesPoly AResearch ArticleBiochemical Journal
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Negative regulation of diacylglycerol kinase θ mediates adenosine-dependent hepatocyte preconditioning

2010

In liver ischemic preconditioning (IP), stimulation of adenosine A2a receptors (A2aR) prevents ischemia/reperfusion injury by promoting diacylglycerol-mediated activation of protein kinase C (PKC). By concerting diacylglycerol to phosphatidic acid, diacylglycerol kinases (DGKs) act as terminator of diacylglycerol signalling. This study investigates the role of DGK in the development of hepatocyte IP. DGK activity and cell viability were evaluated in isolated rat hepatocytes preconditioned by 10 min hypoxia followed by 10 min re-oxygenation or by the treatment with the A2aR agonist, CGS21680, and subsequently exposed to prolonged hypoxia. We observed that after IP or A2aR activation, a decre…

MaleDiacylglycerol Kinasemedicine.medical_specialtyAdenosineReceptor Adenosine A2Ap38 mitogen-activated protein kinasesBiologyQuinazolinonechemistry.chemical_compoundPiperidinecytoprotectionPiperidinesDownregulation and upregulationDiacylglycerol kinase thetaInternal medicinemedicineEnzyme Inhibitorhepatocytes adenosine RhoA hypoxia cytoprotectionAnimalsHepatocyteEnzyme InhibitorsRats WistarMolecular BiologyCells CulturedProtein kinase CQuinazolinonesDiacylglycerol kinaseCell DeathAnimalhypoxiaKinaseReceptors Purinergic P1RhoACell BiologyPhosphatidic acidAdenosineCell HypoxiaRatsCell biologyEndocrinologychemistryHepatocytesRatrhoA GTP-Binding Proteinmedicine.drugCell Death & Differentiation
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Phospholipase D in heart: basal activity and stimulation by phorbol esters and aluminum fluoride

1992

Evidence for a general role of phospholipase D in signal transduction is accumulating. In the present study, the activity of the enzyme was investigated in heart tissue under basal conditions and after addition of phorbol esters or aluminum fluoride (AlF inf4 sup− ; 10 mM NaF plus 10 μM AlCl3). Atria of rats and chickens were incubated with [3H]-myristic acid in order to label preferentially phosphatidylcholine. Under basal conditions, the tissues generated choline and phosphatidic acid (PtdOH), the primary catalytic products of phospholipase D. When 0.5 or 2.0% ethanol was present, [3H]-phosphatidyl-ethanol (PETH) was rapidly formed at the expense of [3H]-PtdOH. This transphosphatidylation…

MaleG proteinPhospholipaseBiologyCholineFluorideschemistry.chemical_compoundGTP-Binding ProteinsPhosphatidylcholinePhorbol EstersPhospholipase DAnimalsPhospholipase D activityRats WistarAluminum CompoundsProtein kinase AChromatography High Pressure LiquidProtein Kinase CProtein kinase CPharmacologyEthanolPhospholipase DMyocardiumHeartGeneral MedicinePhosphatidic acidMolecular biologyRatsBiochemistrychemistryChickensAluminumSignal TransductionNaunyn-Schmiedeberg's Archives of Pharmacology
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Phospholipase D in rat myocardium: formation of lipid messengers and synergistic activation by G-protein and protein kinase C.

1998

Activation of phospholipase D (PLD) and phosphoinositide-specific phospholipase C (PI-PLC) by fluoride, to stimulate heterotrimeric G-proteins, and by phorbol esters, to stimulate protein kinase C (PKC), was studied in rat atria. Fluoride and 4beta-phorbol-12beta,13alpha-dibutyrate (PDB), in contrast to 4beta-phorbol-13alpha-acetate (PAc), activated PLD, catalyzing the formation of [3H]-phosphatidylethanol ([3H]-PETH), [3H]-phosphatidic acid ([3H]-PA), choline and sn-1,2-diacylglycerol (DAG). Basal PLD activity was resistant to drastic changes in Ca2+ and to Ro 31-8220, a PKC inhibitor, but was decreased by genistein, an inhibitor of tyrosine kinase, and increased by vanadate, a tyrosine ph…

MaleG proteinProtein tyrosine phosphataseBiologyBiochemistrySecond Messenger Systemschemistry.chemical_compoundPhosphoinositide Phospholipase CGTP-Binding ProteinsPhorbol EstersPhospholipase DAnimalsRats WistarProtein kinase CPhorbol 1213-DibutyrateProtein Kinase CDiacylglycerol kinasePharmacologyPhospholipase CPhospholipase DMyocardiumPhosphatidylinositol Diacylglycerol-LyaseTyrosine phosphorylationDrug SynergismLipid MetabolismLipidsRatsEnzyme ActivationBiochemistrychemistryType C PhospholipasesSecond messenger systemlipids (amino acids peptides and proteins)Biochemical pharmacology
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Anti-B-50 (GAP-43) antibodies decrease exocytosis of glutamate in permeated synaptosomes.

1999

Abstract The involvement of the protein kinase C substrate, B-50 (GAP-43), in the release of glutamate from small clear-cored vesicles in streptolysin-O-permeated synaptosomes was studied by using anti-B-50 antibodies. Glutamate release was induced from endogenous as well as 3 H -labelled pools in a [Ca2+]-dependent manner. This Ca2+-induced release was partially ATP dependent and blocked by the light-chain fragment of tetanus toxin, demonstrating its vesicular nature. Comparison of the effects of anti-B-50 antibodies on glutamate and noradrenaline release from permeated synaptosomes revealed two major differences. Firstly, Ca2+-induced glutamate release was decreased only partially by anti…

MaleGlutamic AcidBiologyIn Vitro TechniquesSynaptic vesicleExocytosisExocytosischemistry.chemical_compoundNorepinephrineAdenosine TriphosphateGAP-43 ProteinAnimalsEnzyme InhibitorsRats WistarNeurotransmitterProtein kinase CProtein Kinase CPharmacologySynaptosomeVesicleGlutamate receptorAntibodies MonoclonalIntracellular MembranesRatschemistryBiochemistryStreptolysinsBiophysicsLiberationCalciumSynaptosomesEuropean journal of pharmacology
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Phosphorylation of extracellular signal-related protein kinase is required for rapid facilitation of heat-induced currents in rat dorsal root ganglio…

2005

A subgroup of dorsal root ganglion (DRG) neurons responds to noxious heat with an influx of cations carried by specific ion channels such as the transient receptor potential channel of the vanilloid receptor type, subtype 1 (TRPV1). Application of capsaicin induces a reversible facilitation of these currents. This facilitation could be an interaction of two agonists at their common receptor or be caused by an influx of calcium ions into the cell. Calcium influx into the cell can activate protein kinases such as the extracellular signal-related protein kinase (ERK) pathway. This study explored the kinetics, calcium-dependency and intracellular signals following application of capsaicin and l…

MaleMAPK/ERK pathwayHot TemperaturePatch-Clamp TechniquesStatistics as TopicTRPV1BiologyMembrane PotentialsRats Sprague-Dawleychemistry.chemical_compoundBAPTAGanglia SpinalNitrilesButadienesAnimalsDrug InteractionsEnzyme InhibitorsPhosphorylationExtracellular Signal-Regulated MAP KinasesProtein kinase AProtein kinase CNeuronsAnalysis of VarianceDose-Response Relationship DrugGeneral NeuroscienceMEK inhibitorRatsCell biologychemistryBiochemistryCapsaicinMitogen-activated protein kinasebiology.proteinCalciumFemaleCapsaicinNeuroscience
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