Search results for "Phospholipases A2"

showing 10 items of 52 documents

Ergosterol elicits oxidative burst in tobacco cells via phospholipase A2 and protein kinase C signal pathway

2004

Ergosterol, a typical fungal sterol, induced in tobacco (Nicotiana tabacum L. cv. Xanthi) suspension cells the synthesis of reactive oxygen species and alkalization of the external medium that are dependent on the mobilization of calcium from internal stores. We used specific inhibitors to elucidate the signal pathway triggered by ergosterol compared with cryptogein, a proteinaceous elicitor of Phytophthora cryptogea. HerbimycinA and genistein, inhibitors of tyrosine protein kinases, had no effect on the oxidative burst and pH changes induced by bothelicitors.Similarly,H-89,aninhibitorofproteinkinaseA,hadnoeffectontheinductionofthesedefensereactions.However,theresponse to both elicitors was…

0106 biological sciencesTime FactorsCell SurvivalPhysiologyPlant Science01 natural sciencesPhospholipases AFungal Proteins03 medical and health scienceschemistry.chemical_compoundPhospholipase A2ErgosterolPROTEINE KINASE CTobacco[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biologypolycyclic compoundsGenetics[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyEnzyme InhibitorsEstrenesProtein kinase ACells CulturedProtein Kinase CProtein kinase CComputingMilieux_MISCELLANEOUS030304 developmental biologySulfonamides0303 health sciencesErgosterolbiologyPhospholipase CAlgal ProteinsNeomycinIsoquinolinesPyrrolidinonesSterolElicitorRespiratory burstOxidative StressPhospholipases A2chemistryBiochemistryType C Phospholipasesbiology.proteinlipids (amino acids peptides and proteins)Signal Transduction010606 plant biology & botany
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Generation of three human iPSC lines from PLAN (PLA2G6-associated neurodegeneration) patients

2021

© 2021 The Authors.

0301 basic medicineQH301-705.5Cellular differentiationInduced Pluripotent Stem CellsNeuroaxonal Dystrophies:Cells::Stem Cells::Adult Stem Cells::Induced Pluripotent Stem Cells [ANATOMY]Biologymedicine.disease_cause:células::células madre::células madre adultas::células madre pluripotentes inducidas [ANATOMÍA]Sistema nerviós - DegeneracióCell LineDermal fibroblastGroup VI Phospholipases A203 medical and health sciencesKruppel-Like Factor 40302 clinical medicineSOX2medicineHumans:enfermedades del sistema nervioso::enfermedades neurodegenerativas [ENFERMEDADES]Biology (General)Induced pluripotent stem cellMutationNeurodegenerationCell DifferentiationCell BiologyGeneral Medicinemedicine.diseaseCellular Reprogramming030104 developmental biologyKLF4:Nervous System Diseases::Neurodegenerative Diseases [DISEASES]MutationCancer researchMalalties raresReprogramming030217 neurology & neurosurgeryGenèticaDevelopmental BiologyStem Cell Research
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Spontaneous domain formation of phospholipase A2 at interfaces: fluorescence microscopy of the interaction of phospholipase A2 with mixed monolayers …

1992

Abstract Fluorescence microscopy has recently been proven to be an ideal tool to investigated the specific interaction of phospholipase A 2 with oriented substrate monolayers. Using a dual labeling technique, it could be shown that phospholipase A 2 can specifically attack and hydrolyze solid analogous l -α-DPPC domains. After a critical extent of monolayer hydrolysis the enzyme itself starts to aggregate forming regular shaped protein domains (Grainger et al. (1990) Biochim. Biophys. Acta 1023. 365–379). In order to confirm that the existence of hydrolysis products in the mononlayer is necessary for the observed aggregation of phospholipase A 2 , mixed monolayers of d - and l -α-DPPC, l -α…

12-DipalmitoylphosphatidylcholineCarboxylic acidProtein domainBiophysicsPhospholipidBiochemistryPhospholipases Achemistry.chemical_compoundPhospholipase A2MonolayerOrganic chemistryColoring Agentschemistry.chemical_classificationElapid VenomsPhospholipase AbiologyRhodaminesHydrolysisFatty AcidsSubstrate (chemistry)LysophosphatidylcholinesCell BiologyFluoresceinsEnzyme bindingPhospholipases A2chemistryMicroscopy Fluorescencebiology.proteinBiophysicsPhosphatidylcholinesFluoresceinDecanoic AcidsBiochimica et biophysica acta
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Zanhasaponins A and B, Antiphospholipase A2 Saponins from an Antiinflammatory Extract of Zanha africana Root Bark

1997

A MeOH extract from Z. africana was examined for topical antiinflammatory activity and proved to be active against arachidonic acid (AA) acute edema, 12-O-tetradecanoylphorbol 13-acetate (TPA)-induced chronic inflammation, and oxazolone delayed-type hypersensitivity in mice. The extract also showed significant inhibitory activity of Naja naja phospholipase A2 when a polarographic method was used. Two oleanane-type triterpene saponins, zanhasaponins A (1) and B (2), and the cyclitol pinitol (4), isolated from the extract, were active as inhibitors of PLA2. A further saponin, zanhasaponin C (3) was inactive in this assay.

Anti-Inflammatory AgentsSaponinPharmaceutical SciencePharmacognosyDermatitis ContactPhospholipases AAnalytical ChemistryMicechemistry.chemical_compoundPhospholipase A2Adjuvants ImmunologicTriterpeneDrug DiscoveryAnimalsEdemaEnzyme InhibitorsPeroxidaseSkinPharmacologychemistry.chemical_classificationintegumentary systembiologyTraditional medicineOrganic ChemistryOxazoloneGlycosideSaponinsTriterpenesTerpenoidPhospholipases A2Complementary and alternative medicinechemistryBiochemistryvisual_artvisual_art.visual_art_mediumbiology.proteinTetradecanoylphorbol AcetateMolecular MedicineFemaleBarkArachidonic acidJournal of Natural Products
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Type-IIA secreted phospholipase A2 is an endogenous antibiotic-like protein of the host.

2010

International audience; Type-IIA secreted phospholipase A(2) (sPLA(2)-IIA) has been proposed to play a role in the development of inflammatory diseases. It has been shown to release arachidonic acid, the precursor of proinflammatory eicosanoids, to hydrolyze phospholipids of pulmonary surfactant, and to bind to specific receptors located on cell surface membranes. However, the most established biological role of sPLA(2)-IIA is related to its potent bactericidal property in particular toward Gram-positive bacteria. This enzyme is present in animal and human biological fluids at concentrations sufficient to kill bacteria. Human recombinant sPLA(2)-IIA is able to kill Gram-positive bacteria at…

Bacterial Toxinsmedicine.disease_causeGroup II Phospholipases A2BiochemistryMicrobiologyAnthraxMice03 medical and health scienceschemistry.chemical_compound0302 clinical medicineImmune systemPhospholipase A2PhosphatidylcholinemedicineAnimalsHumansEscherichia coli030304 developmental biologyAntigens Bacterial0303 health sciencesPhospholipase AArachidonic AcidbiologyDrug Resistance MicrobialPathogenic bacteriaGeneral Medicinebiology.organism_classificationAnti-Bacterial Agents3. Good healthBacillus anthracisBiochemistrychemistryBacillus anthracisHost-Pathogen Interactionsbiology.protein[SDV.IMM.VAC]Life Sciences [q-bio]/Immunology/VaccinologyBacteria030215 immunology
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Small unilamellar liposomes from mixed natural and polymeric phospholipids: stability and susceptibility to phospholipase A2.

1991

The concept of the uncorkable liposome composed of phase-separated mixtures of a polymerized phospholipid and an enzymically digestible phospholipid has been investigated, using small unilamellar vesicles composed of mixtures of (polymerized) dienoylphosphatidylcholine (DENPC) and dimyristoylphosphatidylcholine (DMPC). Mixed liposomes, even those containing only 10% DENPC, were much more stable than DMPC liposomes, as indicated by the release of entrapped [3H]inulin or [14C]glucose. DMPC liposomes released entrapped solute on exposure to phospholipase A2, whereas mixed vesicles were resistant. The results are compared with those of an earlier study on monolayers of similar compositions. It …

BiophysicsPhospholipidSynthetic membraneTritiumBiochemistryPhospholipases Achemistry.chemical_compoundEndocrinologyPhospholipase A2MonolayerCarbon RadioisotopesPhospholipidsPhospholipase ALiposomeChromatographybiologyVesicleBilayertechnology industry and agricultureInulinTemperatureHydrogen-Ion ConcentrationPhospholipases A2GlucosechemistryLiposomesbiology.proteinlipids (amino acids peptides and proteins)DimyristoylphosphatidylcholineBiochimica et biophysica acta
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Dual role of the p38 MAPK/cPLA2 pathway in the regulation of platelet apoptosis induced by ABT-737 and strong platelet agonists.

2013

p38 Mitogen-activated protein (MAP) kinase is involved in the apoptosis of nucleated cells. Although platelets are anucleated cells, apoptotic proteins have been shown to regulate platelet lifespan. However, the involvement of p38 MAP kinase in platelet apoptosis is not yet clearly defined. Therefore, we investigated the role of p38 MAP kinase in apoptosis induced by a mimetic of BH3-only proteins, ABT-737, and in apoptosis-like events induced by such strong platelet agonists as thrombin in combination with convulxin (Thr/Cvx), both of which result in p38 MAP kinase phosphorylation and activation. A p38 inhibitor (SB202190) inhibited the apoptotic events induced by ABT-737 but did not influ…

Blood PlateletsCancer ResearchcPLA2p38 mitogen-activated protein kinasesImmunologyBlotting Westernp38 Mitogen-Activated Protein KinasesPiperazinesNitrophenolsCellular and Molecular NeurosciencePhospholipase A2Crotalid VenomsHumansLectins C-Typeddc:610Cells CulturedMembrane Potential MitochondrialplateletSulfonamidesbiologyKinaseGroup IV Phospholipases A2Biphenyl CompoundsapoptosisConvulxinCell BiologyFlow Cytometryp38 MAP kinaseCell biologyApoptosisMitogen-activated protein kinasebiology.proteinPhosphorylationOriginal ArticleSignal transductionReactive Oxygen SpeciesSignal TransductionCell deathdisease
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Effects of marine 2-polyprenyl-1,4-hydroquinones on phospholipase A2 activity and some inflammatory responses.

1995

Three 2-polyprenyl-1,4-hydroquinone derivatives (2-heptaprenyl-1,4-hydroquinone: IS1, 2-octaprenyl-1,4-hydroquinone: IS2 and 2-[24-hydroxy]-octaprenyl-1,4-hydroquinone: IS3) isolated from the Mediterranean sponge Ircinia spinosula, were evaluated for effects on phospholipase A2 activity of different origin (Naja naja venom, human recombinant synovial fluid and bee venom), as well as on human neutrophil function and mouse ear oedema induced by 12-O-tetradecanoylphorbol 13-acetate (TPA). IS1 interacted minimally with these responses. In contrast, IS2 and IS3 inhibited human recombinant synovial phospholipase A2 in a concentration-dependent manner, with minor effects on the rest of the enzymes…

Blood PlateletsLeukocyte migrationLeukotriene B4Cell SurvivalNeutrophilsPharmacologyBiologyIn Vitro TechniquesLeukotriene B4Phospholipases Achemistry.chemical_compoundMicePhospholipase A2SuperoxidesMicrosomesSynovial fluidAnimalsEdemaHumansPharmacologyPhospholipase AL-Lactate DehydrogenasePancreatic ElastaseAnti-Inflammatory Agents Non-SteroidalDegranulationBiological activityHydroquinonesPoriferaThromboxane B2Thromboxane B2Phospholipases A2Biochemistrychemistrybiology.proteinTetradecanoylphorbol AcetateEuropean journal of pharmacology
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Clonidine increases membrane-associated phospholipase A2

2005

Background and objective: An anti-inflammatory effect of α 2 -adrenoreceptor agonists has been suggested. Phospholipase A 2 is a key enzyme in the production of precursors of inflammatory lipid mediators. The aim of the present study was to investigate the effect of clonidine on phospholipase A 2 activity in an established in vitro model. Methods: Human being platelet membranes containing active phospholipase A 2 were exposed to buffer control or to three increasing concentrations of clonidine. Phospholipase A 2 was measured by a radioisotope technique. Results: A massive increase in phospholipase A 2 activity was measured after clonidine exposure leading to final values of 92.5 ′ 3.1 pmol …

Blood PlateletsMalemedicine.medical_specialtyAnti-Inflammatory AgentsInflammationIn Vitro TechniquesClonidinePhospholipases AInternal medicinemedicineHumansPlateletchemistry.chemical_classificationPhospholipase Abusiness.industryGroup IV Phospholipases A2Cell MembraneSubstrate (chemistry)Lipid signalingClonidinePhospholipases A2Anesthesiology and Pain MedicineEndocrinologyEnzymeMembranechemistryFemalemedicine.symptombusinessAdrenergic alpha-AgonistsAdjuvants Anesthesiamedicine.drugEuropean Journal of Anaesthesiology
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Inhibition of inflammatory responses by epitaondiol and other marine natural products

1995

The marine metabolites pacifenol, stypotriol triacetate and epitaondiol were tested for their effects on a number of inflammatory responses. Epitaondiol exhibited a potent topical anti-inflammatory activity related to inhibition of leukocyte accumulation. The other compounds showed a lower potency, similar to that of indomethacin. None of the compounds affected superoxide generation by human neutrophils but pacifenol effectively inhibited the degranulation response. This compound and epitaondiol decreased the release of eicosanoids with a higher potency on the cyclo-oxygenase pathway. Only epitaondiol inhibited human recombinant synovial phospholipase A2 activity in a concentration-dependen…

Blood PlateletsNeutrophilsmedicine.drug_classAnti-Inflammatory AgentsCytochrome c GroupBiologyLeukotriene B4Phospholipases AGeneral Biochemistry Genetics and Molecular BiologyAnti-inflammatorylaw.inventionMicechemistry.chemical_compoundPhospholipase A2SuperoxideslawmedicineAnimalsEdemaHumansPotencyEar ExternalGeneral Pharmacology Toxicology and PharmaceuticsEpitaondiolCalcimycinInflammationPhospholipase ATerpenesSuperoxideAnti-Inflammatory Agents Non-SteroidalDegranulationGeneral MedicineStimulation ChemicalThromboxane B2Phospholipases A2BiochemistrychemistryRecombinant DNAbiology.proteinTetradecanoylphorbol AcetateSteroidsOxidation-ReductionSesquiterpenesLife Sciences
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