Search results for "cyclic AMP"

showing 10 items of 177 documents

Regulation of cyclooxygenase-2 expression by cyclic AMP.

2007

Abstract Prostaglandins (PG) regulate many biological processes, among others inflammatory reactions. Cyclooxygenases-1 and -2 (COX-1 and COX-2) catalyse PG synthesis. Since this step is rate limiting, the regulation of COX expression is of critical importance to PG biology. Contrary to COX-1, which is constitutively expressed, COX-2 expression is subject to regulation. For example, COX-2 levels are increased in inflammatory reactions. Many signalling pathways can regulate COX-2 expression, not least those involving receptors for COX products themselves. Analysis of the intracellular signal transducers involved reveals a crucial role for cAMP, albeit as a modulator rather than direct induce…

Cell typeMessenger RNAProstaglandinPhosphodiesteraseCell BiologyBiologyCREBGene Expression Regulation EnzymologiccGMPBiochemistryCyclooxygenase 2cAMPbiology.proteincAMP-responsive elementCyclic AMPAdenylate cyclaseAnimalsHumansPhosphodiesteraseCyclooxygenaseReceptorMolecular BiologyGeneIntracellularSignal TransductionBiochimica et biophysica acta
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Multiple signal transduction pathways regulate clusterin (gp 80) gene expression in MDCK cells

1996

ABSTRACT Clusterin (gp 80, apolipoprotein J, TRPM-2) is a widely expressed multifunctional glycoprotein. Its demonstrated and proposed functions include the transport of lipids and membrane fragments, the inhibition of the cytolytic action of the terminal complement complex and the modulation of cell—cell interactions. The expression of the gene is enhanced during tissue injury and remodelling and by hormone-withdrawal-induced apoptosis of prostate and mammary cells. We show here that, in the kidney-derived epithelial cell line MDCK, clusterin mRNA is repressed by glucocorticoids and by progesterone. Treatment with epidermal growth factor also represses clusterin gene expression in MDCK cel…

Cell typeTranscription GeneticKidneyDexamethasoneEpitheliumCell LineAlkaloidsDogsEndocrinologyEpidermal growth factor1-Methyl-3-isobutylxanthineGene expressionCyclic AMPAnimalsRNA MessengerEnzyme InhibitorsAldosteroneMolecular BiologyProgesteroneProtein Kinase CProtein kinase CGlycoproteinsBenzophenanthridinesMessenger RNAEpidermal Growth FactorClusterinbiologyChemistryMolecular biologyeye diseasesPhenanthridinesCell biologyKineticsClusterinCell culturebiology.proteinTetradecanoylphorbol Acetatesense organsSignal transductionMolecular ChaperonesSignal TransductionJournal of Molecular Endocrinology
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Role of cAMP in mediating AHR signaling.

2009

Regulation of the nuclear import of many transcription factors represents a step in gene regulation which is crucial for a number of cellular processes. The aryl hydrocarbon receptor (AHR), a basic helix-loop-helix protein of the PAS (PER-ARNT-SIM) family of transcriptional regulators is a cytosol-associated and ligand-activated receptor. The environmental toxin dioxin binds with high affinity to AHR rendering it nuclear and leading to the activation of AHR sensitive genes. However, the fact, that the AHR mediates a large variety of physiological events without the involvement of any known exogenous ligand, including liver and vascular system development, maturation of the immune system, re…

Cellular differentiationNuclear translocationSignal transductionDioxinsLigandsBiochemistryCell LineProtein kinase ACyclic AMPCytochrome P-450 CYP1A1AnimalsHumansPhosphorylationReceptorProtein kinase ATranscription factorAryl hydrocarbon receptorPharmacologyRegulation of gene expressionbiologyAryl hydrocarbon receptorCyclic AMP-Dependent Protein KinasesProtein TransportBiochemistryReceptors Aryl HydrocarbonSecond messenger systembiology.proteinEnvironmental PollutantsSignal transductionDioxin toxicitySignal TransductionBiochemical pharmacology
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Caveolin and GLT-1 gene expression is reciprocally regulated in primary astrocytes: Association of GLT-1 with non-caveolar lipid rafts

2004

Caveolae represent membrane microdomains acting as integrators of cellular signaling and functional processes. Caveolins are involved in the biogenesis of caveolae and regulate the activity of caveolae-associated proteins. Although caveolin proteins are found in the CNS, the regulation of caveolins in neural cells is poorly described. In the present study, we investigated different modes and mechanisms of caveolin gene regulation in primary rat astrocytes. We demonstrated that activation of cAMP-dependent signaling pathways led to a marked reduction in protein levels of caveolin-1/-2 in cortical astrocytes. Application of transforming growth factor-alpha (TGF-alpha) also resulted in a decre…

Central Nervous SystemCaveolin 2Caveolin 1Down-RegulationGlutamic AcidBiologyCaveolinsHistone DeacetylasesChromatin remodelingRats Sprague-DawleyPhosphatidylinositol 3-KinasesCellular and Molecular NeuroscienceAstrocyte differentiationMembrane MicrodomainsCaveolaeCaveolinCyclic AMPAnimalsRNA MessengerLipid raftCerebral CortexRegulation of gene expressionTransforming Growth Factor alphaRatsCell biologyCaveolin 2Animals NewbornExcitatory Amino Acid Transporter 2Gene Expression RegulationNeurologyAstrocytesCaveolin 1Signal TransductionGlia
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Pharmacological Suppression of CNS Scarring by Deferoxamine Reduces Lesion Volume and Increases Regeneration in an In Vitro Model for Astroglial-Fibr…

2015

Lesion-induced scarring is a major impediment for regeneration of injured axons in the central nervous system (CNS). The collagen-rich glial-fibrous scar contains numerous axon growth inhibitory factors forming a regeneration-barrier for axons. We demonstrated previously that the combination of the iron chelator 2,2'-bipyridine-5,5'-decarboxylic acid (BPY-DCA) and 8-Br-cyclic AMP (cAMP) inhibits scar formation and collagen deposition, leading to enhanced axon regeneration and partial functional recovery after spinal cord injury. While BPY-DCA is not a clinical drug, the clinically approved iron chelator deferoxamine mesylate (DFO) may be a suitable alternative for anti-scarring treatment (A…

Central Nervous SystemCollagen Type IVmedicine.medical_specialtyNeuriteCentral nervous systemlcsh:MedicineBiologyPharmacologyDeferoxamineIn Vitro TechniquesIron Chelating AgentsCicatrixIn vivoTransforming Growth Factor betamedicineCyclic AMPNeuritesAnimalsHumansRNA MessengerAxonRats Wistarlcsh:ScienceSpinal cord injurySpinal Cord InjuriesMultidisciplinaryDeferoxamine mesylatelcsh:RFibroblastsSpinal cordmedicine.diseaseAxonsSurgeryNerve RegenerationRatsDeferoxamineDisease Models Animalmedicine.anatomical_structureAstrocyteslcsh:QFemalemedicine.drugResearch ArticlePloS one
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Neurosteroidogenesis in Rat Retinas

2002

Neurosteroids (steroids synthesized in the CNS) function by modulating neurotransmission. To establish an experimental model for investigation of neurosteroid synthesis and regulation, independent of blood-borne steroids, we examined the steroidogenic activity of isolated rat retinas. We identified progesterone, pregnenolone, dehydroepiandrosterone, desoxycorticosterone, 3 alpha,5 alpha-tetrahydrodesoxycorticosterone, 3 alpha-hydroxy-5 alpha-dihydroprogesterone, 17-hydroxyprogesterone, and 17-hydroxypregnenolone together with their esterified forms. As pregnenolone is the precursor of all steroids, its formation was studied in detail as an index of a steroid-synthesizing tissue. Pregnenolon…

Central Nervous SystemMaleTime FactorsNeuroactive steroidDehydroepiandrosteroneBiochemistryGas Chromatography-Mass SpectrometryRetinaCellular and Molecular NeuroscienceCyclic AMPmedicineAnimalsCholesterol Side-Chain Cleavage EnzymeLovastatinRats WistarChromatography High Pressure LiquidProgesteroneNeurotransmitter AgentsDose-Response Relationship DrugbiologyCholesterol side-chain cleavage enzymeCytochrome P450DehydroepiandrosteroneAminoglutethimideImmunohistochemistryRatsmedicine.anatomical_structureBiochemistryPregnenoloneInner nuclear layerPregnenolonebiology.proteinSteroidsLovastatinAminoglutethimidemedicine.drugJournal of Neurochemistry
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Central Modulatory Neurons Control Fuel Selection in Flight Muscle of Migratory Locust

2003

Insect flight is one of the most intense and energy-demanding physiological activities. High carbohydrate oxidation rates are necessary for take-off, but, to spare the limited carbohydrate reserves, long-distance flyers, such as locusts, soon switch to lipid as the main fuel. We demonstrate that before a flight, locust muscles are metabolically poised for take-off by the release of octopamine from central modulatory dorsal unpaired median (DUM) neurons, which increases the levels of the potent glycolytic activator fructose 2,6-bisphosphate in flight muscle. Because DUM neurons innervating the flight muscles are active during rest but selectively inhibited during flight, they stimulate carbo…

Central Nervous SystemMalemedicine.medical_specialtyGrasshoppersBrief CommunicationInsect flightCarbohydrate catabolismInternal medicinemedicineFructosediphosphatesPremovement neuronal activityAnimalsGlycolysisProtein kinase AMuscle SkeletalOctopamineNeuronsbiologyGeneral NeuroscienceMigratory locustbiology.organism_classificationCyclic AMP-Dependent Protein KinasesEndocrinologyFlight AnimalOctopamine (neurotransmitter)FemaleGlycolysisLocustSignal Transduction
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Betulin binds to melanocortin receptors and antagonizes alpha-melanocyte stimulating hormone induced cAMP generation in mouse melanoma cells.

2007

Betulin is a principal component of birch bark and is known to possess a broad range of biological activities, including antiinflammatory, antiviral and anticancer actions. The present study was carried out in vitro to clarify the influence of betulin on melanocortin (MC) receptor-ergic signalling by using COS-7 cells transfected with corresponding human MC receptor DNA. The results showed that betulin binds to the human melanocortin MC1, three to five receptors with selectivity to the MC1 subtype (K(i) value 1.022 +/- 0.115 microM). Betulin binds to the MC receptors with the following potency order-MC > MC3 > MC5 > MC4. Betulin itself does not stimulate cAMP generation, however, it slightl…

Clinical BiochemistryBiologyBiochemistryBinding Competitivechemistry.chemical_compoundMiceBetulinic acidChlorocebus aethiopsCyclic AMPAnimalsHumansReceptorMelanomaBetulinReceptors MelanocortinCell BiologyGeneral MedicineTransfectionIn vitroalpha-Melanocyte-stimulating hormoneTriterpenesKineticsBiochemistrychemistryCell culturealpha-MSHCOS CellsMelanocortinCell biochemistry and function
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Aryl hydrocarbon receptor activation by cAMP vs. dioxin: divergent signaling pathways.

2005

Even before the first vertebrates appeared on our planet, the aryl hydrocarbon receptor ( AHR ) gene was present to carry out one or more critical life functions. The vertebrate AHR then evolved to take on functions of detecting and responding to certain classes of environmental toxicants. These environmental pollutants include polycyclic aromatic hydrocarbons (e.g., benzo[ a ]pyrene), polyhalogenated hydrocarbons, dibenzofurans, and the most potent small-molecular-weight toxicant known, 2,3,7,8-tetrachlorodibenzo- p -dioxin (TCDD or dioxin). After binding of these ligands, the activated AHR translocates rapidly from the cytosol to the nucleus, where it forms a heterodimer with aryl hydroc…

Conservation of Natural ResourcesAryl hydrocarbon receptor nuclear translocatorPolychlorinated DibenzodioxinsTime FactorsTranscription GeneticGenetic VectorsGreen Fluorescent ProteinsImmunoblottingActive Transport Cell NucleusEnvironmentDioxinsLigandschemistry.chemical_compoundMiceCytosolGenes ReporterCell Line TumorCyclic AMPAnimalsImmunoprecipitationReceptorFluorescent Antibody Technique IndirectCell NucleusMultidisciplinarybiologyChemistryColforsinEndogenous mediatorrespiratory systemBiological SciencesAryl hydrocarbon receptorCyclic AMP-Dependent Protein KinasesCytosolProtein TransportBiochemistryBucladesineMicroscopy FluorescenceReceptors Aryl HydrocarbonSecond messenger systembiology.proteinProstaglandinsEnvironmental PollutantsSignal transductionDimerizationToxicantPlasmidsProtein BindingSignal TransductionProceedings of the National Academy of Sciences of the United States of America
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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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