Search results for "Enzyme Activation"

showing 10 items of 304 documents

Glutamate Activates Phospholipase D in Hippocampal Slices of Newborn and Adult Rats

1993

Phospholipase D (PLD) is activated by many neurotransmitters in a novel signal transduction pathway. In the present work, PLD activity was studied comparatively in hippocampal slices of newborn and adult rats. Basal PLD activity in adult rats was almost three times higher than in newborn rats. In newborn rats, L-glutamate and 1S,3R-1-aminocyclopentane-1,3-dicarboxylic acid (1S,3R-ACPD) time- and concentration-dependently enhanced the formation of [3H]phosphatidylpropanol ([3H]PP) and of [3H]phosphatidic acid in the presence of 2% propanol. N-Methyl-D-aspartate and kainate (both 1 mM) caused small, but significant increases (approximately 50%), whereas alpha-amino-3-hydroxy-5-methylisoxazole…

Agingmedicine.medical_specialtyGlutamic AcidKainate receptorIn Vitro TechniquesBiologyHippocampal formationKynurenateHippocampusBiochemistryCellular and Molecular Neurosciencechemistry.chemical_compoundGlutamatesInternal medicinePhospholipase DmedicineAnimalsCycloleucineNeurotransmitterPhospholipase DGlutamate receptorPhosphatidic acidRatsEnzyme ActivationMetabotropic receptorEndocrinologyAnimals NewbornchemistryBiochemistryJournal of Neurochemistry
researchProduct

5-HT3 receptor-channels coupled with Na+ influx in human T cells: role in T cell activation.

1999

The study was conducted on a human (Jurkat) T cell line, loaded with a Na+ fluorescent probe, SBFI/AM. Serotonin and an agonist of 5-HT3 receptor-channels, 2-methyl-5HT, evoked Na+ influx, whereas the agonists of other serotonergic receptor subtypes, i.e., 5-HT1A and 5-HT1B receptors, failed to induce Na+ influx in these cells. By using 3H-BRL43694, an agonist of 5-HT3 receptor-channels, we characterized 5-HT3 lymphocyte receptors which exhibited a density (Bmax) of 300 +/- 20 fmol/10(6) cells and a Kd of 30 nM in Jurkat T cells. The T-cell 5-HT3 receptor-channel is not regulated either by the protein kinase C or by the free intracellular calcium concentrations as the agents known to activa…

AgonistSerotoninmedicine.drug_classMetoclopramideT cellT-LymphocytesImmunologyBiologyLymphocyte ActivationJurkat cellsCalcium in biologyPiperazinesSodium ChannelsGranisetronJurkat CellsQuinoxalinesmedicineImmunology and AllergyHumansCalcium SignalingPhytohemagglutininsReceptorProtein kinase C5-HT receptorProtein Kinase C8-Hydroxy-2-(di-n-propylamino)tetralinIon TransportRyanodineCell CycleSodiumCell biologyNeoplasm ProteinsSerotonin Receptor AgonistsEnzyme Activationmedicine.anatomical_structureNeurologyReceptors SerotoninReceptor Serotonin 5-HT1BThapsigarginNeurology (clinical)Serotonin AntagonistsReceptors Serotonin 5-HT3Ion Channel GatingReceptors Serotonin 5-HT1IntracellularJournal of neuroimmunology
researchProduct

Activation of phospholipases C and D by the novel metabotropic glutamate receptor agonist tADA.

1997

Abstract In hippocampal slices taken from 8-day-old rats, trans-azetidine-2,4-dicarboxylic acid (tADA), a novel glutamatergic agonist acting preferentially at class I mGluR receptors, activates phosphoinositide and phosphatidylcholine hydrolysis with widely different potencies. Inositol phosphate formation was maximally increased at 10 μM tADA ( ec 50: 1.2 μM), while phospholipase D activation was observed at a tADA concentration of 1 mM. This is the first report of a tADA-induced phospholipase D activity. © 1997 Elsevier Science Ltd. All rights reserved.

Agonistmedicine.drug_classInositol PhosphatesPhospholipaseBiologyIn Vitro TechniquesReceptors Metabotropic GlutamateHippocampusRats Sprague-DawleyCellular and Molecular NeurosciencemedicineExcitatory Amino Acid AgonistsPhospholipase DPhospholipase D activityAnimalsInositol phosphatePharmacologychemistry.chemical_classificationPhospholipase CPhospholipase DRatsEnzyme ActivationMetabotropic receptorBiochemistrychemistryMetabotropic glutamate receptorType C PhospholipasesAzetidinecarboxylic AcidNeuropharmacology
researchProduct

Activation of c-Jun N-terminal kinase 1 by UV irradiation is inhibited by wortmannin without affecting c-iun expression.

1999

Activation of c-Jun N-terminal kinases (JNKs)/stress-activated protein kinases is an early response of cells upon exposure to DNA-damaging agents. JNK-mediated phosphorylation of c-Jun is currently understood to stimulate the transactivating potency of AP-1 (e.g., c-Jun/c-Fos; c-Jun/ATF-2), thereby increasing the expression of AP-1 target genes. Here we show that stimulation of JNK1 activity is not a general early response of cells exposed to genotoxic agents. Treatment of NIH 3T3 cells with UV light (UV-C) as well as with methyl methanesulfonate (MMS) caused activation of JNK1 and an increase in c-Jun protein and AP-1 binding activity, whereas antineoplastic drugs such as mafosfamide, mito…

Alkylating AgentsProto-Oncogene Proteins c-junUltraviolet RaysStimulationBiologyenvironment and public healthWortmanninTransactivationchemistry.chemical_compoundMiceAnimalsPhosphatidylinositolCollagenasesProtein kinase AMolecular BiologyCell Growth and DevelopmentMitogen-Activated Protein Kinase 1Kinasec-junJNK Mitogen-Activated Protein KinasesCell Biology3T3 CellsMethyl MethanesulfonateMolecular biologyAndrostadienesEnzyme ActivationGene Expression Regulation NeoplasticTranscription Factor AP-1chemistryCalcium-Calmodulin-Dependent Protein KinasesPhosphorylationMitogen-Activated Protein KinasesWortmanninMolecular and cellular biology
researchProduct

Activation of classical protein kinase C decreases transport via systems y+and y+L

2007

Activation of protein kinase C (PKC) downregulates the human cationic amino acid transporters hCAT-1 (SLC7A1) and hCAT-3 (SLC7A3) (Rotmann A, Strand D, Martiné U, Closs EI. J Biol Chem 279: 54185–54192, 2004; Rotmann A, Vekony N, Gassner D, Niegisch G, Strand D, Martine U, Closs EI. Biochem J 395: 117–123, 2006). However, others found that PKC increased arginine transport in various mammalian cell types, suggesting that the expression of different arginine transporters might be responsible for the opposite PKC effects. We thus investigated the consequence of PKC activation by phorbol-12-myristate-13-acetate (PMA) in various human cell lines expressing leucine-insensitive system y+[hCAT-1, h…

Amino Acid Transport System y+ArgininePhysiologyBiological Transport ActiveBiologyArginineEnzyme activatorLeucineCell Line TumorHumansRNA MessengerCationic Amino Acid TransportersProtein Kinase CProtein kinase CRegulation of gene expressionchemistry.chemical_classificationBase SequenceAmino Acid Transport System y+LCell BiologyMolecular biologyEnzyme ActivationEnzymeGene Expression RegulationchemistryTetradecanoylphorbol AcetateTetradecanoylphorbol AcetateLeucineAmerican Journal of Physiology-Cell Physiology
researchProduct

Inhibitory effects of N-acetylcysteine on superoxide anion generation in human polymorphonuclear leukocytes.

1997

Abstract It has been suggested that reactive oxygen species released by activated polymorphonuclear leukocytes (PMN) in man is one mechanism of tissue injury. Therapeutic action aimed at increasing antioxidant defence mechanisms is still a clinical challenge. This study examines the activity of N-acetylcysteine, a known antioxidant, in the protection of PMN exposed in-vitro to the chemoattractant peptide fMet-Leu-Phe (FMLP), the protein kinase C activator phorbol myristate acetate or the lipid peroxidation promoter t-butyl hydroperoxide. FMLP (3–300 nm) and phorbol myristate acetate (160 pm–160 nm) induced concentration-related superoxide anion generation. Pre-treatment with N-acetylcystein…

AnionsAntioxidantNeutrophilsmedicine.medical_treatmentPharmaceutical Sciencechemistry.chemical_elementCalciumLipid peroxidationchemistry.chemical_compoundtert-ButylhydroperoxideSuperoxidesmedicineHumansProtein kinase CProtein Kinase CPharmacologychemistry.chemical_classificationReactive oxygen speciesSuperoxideGlutathioneMalondialdehydeMolecular biologyGlutathioneAcetylcysteinePeroxidesEnzyme ActivationN-Formylmethionine Leucyl-PhenylalanineBiochemistrychemistryTetradecanoylphorbol AcetateCalciumLipid PeroxidationThe Journal of pharmacy and pharmacology
researchProduct

Resistance to Gemcitabine in a Lymphoma Cell Line Resistant to Fas-mediated Apoptosis

2004

BACKGROUND: The T-cell lymphoma cell line HuT78B1, selected for resistance to Fas-mediated apoptosis, resulted unexpectedly resistant to the apoptotic and cytotoxic effects of gemcitabine (dFdC). We investigated whether this resistance was due to the impairment of the Fas/Fas-ligand (FasL) system. MATERIALS AND METHODS: dFdC effects were studied in HuT78B1 and in the parental Fas-sensitive HuT78 cells exposed to inhibitors of the Fas/FasL system. RESULTS: FasL- and Fas-blocking antibodies did not interfere with dFdC-induced apoptosis in HuT78 cells, whereas inhibitors of caspase-8, -9, -1 or -3 had partial inhibitory effects. Notably, in HuT78B1 cells there was a markedly reduced dFdC accum…

Antimetabolites AntineoplasticFas Ligand ProteinMembrane GlycoproteinsApoptosisLymphoma T-CellCaspase InhibitorsDeoxycytidineGemcitabineEnzyme ActivationLymphoma T-Cell Cell Line Tumor gemcitabineDrug Resistance NeoplasmCaspasesCell Line TumorDeoxycytidine KinaseHumansfas Receptor
researchProduct

PTEN Mediates the Antioxidant Effect of Resveratrol at Nutritionally Relevant Concentrations

2014

Introduction.Antioxidant properties of resveratrol have been intensively studied for the last years, bothin vivoandin vitro. Its bioavailability after an oral dose is very low and therefore it is very important to make sure that plasma concentrations of free resveratrol are sufficient enough to be active as antioxidant.Aims.In the present study, using nutritionally relevant concentrations of resveratrol, we aim to confirm its antioxidant capacity on reducing peroxide levels and look for the molecular pathway involved in this antioxidant effect.Methods.We used mammary gland tumor cells (MCF-7), which were pretreated with different concentrations of resveratrol for 48 h, and/or a PTEN inhibit…

Antioxidantendocrine system diseasesArticle Subjectmedicine.medical_treatmentlcsh:MedicineResveratrolGeneral Biochemistry Genetics and Molecular BiologyAntioxidantschemistry.chemical_compoundDownregulation and upregulationStilbenesmedicinePTENHumansPhosphorylationskin and connective tissue diseasesHydrogen peroxidePI3K/AKT/mTOR pathwayGeneral Immunology and MicrobiologybiologyAkt/PKB signaling pathwaySuperoxide Dismutaseorganic chemicalslcsh:RPTEN Phosphohydrolasefood and beveragesGeneral MedicineHydrogen PeroxideCatalaseUp-RegulationEnzyme ActivationBiochemistrychemistryCatalaseResveratrolbiology.proteinMCF-7 CellsProto-Oncogene Proteins c-akthormones hormone substitutes and hormone antagonistsSignal TransductionResearch Article
researchProduct

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
researchProduct

Arginine vasopressin, via activation of post-junctional V1 receptors, induces contractile effects in mouse distal colon

2013

The aim of this study was to analyze whether arginine vasopressin (AVP) may be considered a modulator of intestinal motility. In this view, we evaluated, in vitro, the effects induced by exogenous administration of AVP on the contractility of mouse distal colon, the subtype(s) of receptor(s) activated and the action mechanism. Isometric recordings were performed on longitudinal and circular muscle strips of mouse distal colon. AVP (0.001 nM-100 nM) caused concentration-dependent contractile effects only on the longitudinal muscle, antagonized by the V1 receptor antagonist, V-1880. AVP-induced effect was not modified by tetrodotoxin, atropine and indomethacin. Contractile response to AVP was…

AtropineMaleReceptors Vasopressinmedicine.medical_specialtyVasopressinCarbacholNifedipineColonPhysiologyIndomethacinClinical BiochemistryMuscarinic AntagonistsTetrodotoxinCholinergic AgonistsIn Vitro TechniquesBiologyBiochemistryContractilityMiceCellular and Molecular Neurosciencechemistry.chemical_compoundPhosphoinositide Phospholipase CEndocrinologyInternal medicinemedicineAnimalsCyclooxygenase InhibitorsReceptorVasopressin receptorPhospholipase CArginine vasopressin receptor 1AMuscle SmoothCalcium Channel BlockersArginine vasopressinIntestinalcontractility V1 receptorsPhospholipase C Mouse colonArginine VasopressinEnzyme ActivationMice Inbred C57BLEndocrinologychemistryCarbacholGastrointestinal MotilityCyclopiazonic acidhormones hormone substitutes and hormone antagonistsMuscle ContractionSignal Transductionmedicine.drugRegulatory Peptides
researchProduct