Search results for "Cyclooxygenase pathway"

showing 5 items of 5 documents

Host-based lipid inflammation drives pathogenesis in Francisella infection

2017

Mass spectrometry imaging (MSI) was used to elucidate host lipids involved in the inflammatory signaling pathway generated at the host-pathogen interface during a septic bacterial infection. Using Francisella novicida as a model organism, a bacterial lipid virulence factor (endotoxin) was imaged and identified along with host phospholipids involved in the splenic response in murine tissues. Here, we demonstrate detection and distribution of endotoxin in a lethal murine F. novicida infection model, in addition to determining the temporally and spatially resolved innate lipid inflammatory response in both 2D and 3D renderings using MSI. Further, we show that the cyclooxygenase-2-dependent lip…

0301 basic medicineLipopolysaccharideDIVERSITYGene ExpressionLIPOPOLYSACCHARIDEhost-pathogen interactionmedicine.disease_cause01 natural sciencesMass SpectrometryVirulence factorMicechemistry.chemical_compoundlipid inflammationcyclooxygenase pathwayHETEROGENEITYFrancisellaPhospholipidsMice KnockoutMultidisciplinarybiologyTULAREMIABiological SciencesMolecular ImagingHost-Pathogen InteractionsFrancisellalipids (amino acids peptides and proteins)FemaleSignal TransductionLPSHost–pathogen interactionmicrobial pathogenesismass spectrometry imagingDinoprostoneMicrobiologyCyclooxygenase pathwayProinflammatory cytokine03 medical and health sciencesImmune systemIMAGING MASS-SPECTROMETRYmedicineAnimalsBIOSYNTHESISFrancisella novicidaInflammationMacrophages010401 analytical chemistrybacterial infections and mycosesbiology.organism_classificationSurvival AnalysisImmunity Innate0104 chemical sciencesEndotoxinsMice Inbred C57BL030104 developmental biologychemistryCyclooxygenase 2EicosanoidsGram-Negative Bacterial InfectionsSpleenProceedings of the National Academy of Sciences
researchProduct

Spectrofluorimetric Quantification of Malondialdehyde for Evaluation of Cyclooxygenase-1/Thromboxane Synthase Inhibition

1999

The in vitro assay developed by Hartmann and Ledergerber (1995) utilizing the spectrofluorimetric quantification of malondialdehyde after reaction with thiobarbituric acid was modified and used for further investigations. The human whole blood was replaced by a platelet suspension of pig blood, and calcium ionophore A23187 was used instead of collagen for inducing the arachidonic acid cascade. The modified assay represents a simple, time and cost saving method for the evaluation of cyclooxygenase-1/thromboxane synthase inhibition. The reproducibility and comparability of results is given. Additional experiments allow classification of selective phospholipase A2, cyclooxygenase-1, and thromb…

Blood PlateletsSwineThiobarbituric acidPharmaceutical ScienceCyclooxygenase pathwaychemistry.chemical_compoundPhospholipase A2MalondialdehydeDrug DiscoveryAnimalsHumansCyclooxygenase InhibitorsDrug InteractionsPlateletEnzyme InhibitorsDose-Response Relationship DrugbiologyImidazolesMembrane ProteinsReproducibility of ResultsThiobarbituratesMalondialdehydeIsoenzymesSpectrometry FluorescencechemistryBiochemistryProstaglandin-Endoperoxide SynthasesCyclooxygenase 1biology.proteinArachidonic acidThromboxane-A SynthaseThromboxane-A synthaseCyclooxygenaseArchiv der Pharmazie
researchProduct

Incorporation and metabolism of trans 20∶5 in endothelial cells. Effect on prostacyclin synthesis

2000

To study the ability of long-chain trans fatty acids (FA) to be incorporated and metabolized into endothelial cells, bovine aortic endothelial cells were incubated with medium enriched eicosapentaenoic acid (EPA) bound to albumin (M2) or one of its geometrical isomers: 20:5 5c,8c,11t,14c,17c (M3), 20:5 5c,8c,11c,14c,17t (M4), or 20:5 5c,8c,11t,14c,17t (M5). After 48 h of incubation, supernatant and cells were harvested and their lipids were analyzed, including prostacyclin synthesis. EPA and 22:5n-3 of endothelial cells incubated with M2 were, respectively, three and two times higher than in control cells (incubated in M1, without any fatty acid added), whereas 22:6n-3 increased only in the…

Endothelium030309 nutrition & dieteticsPhospholipidSerum albuminBiochemistryGas Chromatography-Mass SpectrometryMass SpectrometryCyclooxygenase pathway03 medical and health scienceschemistry.chemical_compoundmedicineAnimals[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM][SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]AortaChromatography High Pressure LiquidSerum AlbuminComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classification0303 health sciencesFourier AnalysisbiologyFatty AcidsOrganic ChemistryFatty acidCell BiologyMetabolismEpoprostenolLipidsEicosapentaenoic acidCulture Mediamedicine.anatomical_structureEicosapentaenoic AcidchemistryBiochemistryProstaglandin-Endoperoxide SynthasesProstaglandinsbiology.proteinCattleArachidonic acidEndothelium VascularLipids
researchProduct

Effect of indomethacin on the kinetics of tumour necrosis factor alpha release and tumour necrosis factor alpha gene expression by human blood monocy…

1991

Summary In this investigation we have examined the effects of indomethacin, an inhibitor of the cyclooxygenase pathway of arachidonic acid, upon the kinetics of the release of tumour necrosis factor alpha (TNF) and of the expression of TNF gene by lipopolysaccharide (LPS)-stimulated human blood monocytes (BM). Following stimulation of BM with LPS, TNF was released within 2 h, reached peak values at 8 h and declined at subsequent time-points (24 and 48 h). Indomethacin (10−5 m ) slightly stimulated the production of TNF at 2, 4, and 8 h and prevented the decline of TNF observed at 24 and 48 h. This effect was related to the persistence of TNF synthesis, as demonstrated by kinetics evaluation…

LipopolysaccharidesTranscription GeneticLipopolysaccharideNeutrophilsmedicine.medical_treatmentIndomethacinProstaglandinIn Vitro TechniquesPharmacologyDinoprostoneCyclooxygenase pathwaychemistry.chemical_compoundGene expressionmedicineHumansRNA MessengerPharmacologyTumor Necrosis Factor-alphabusiness.industryMonocyteKineticsmedicine.anatomical_structureCytokineGene Expression RegulationchemistryImmunologyIndicators and ReagentsArachidonic acidTumor necrosis factor alphabusinessPharmacological Research
researchProduct

Bradykinin Contracts Rat Urinary Bladder Largely Independently of Phospholipase C

2014

Several receptor systems in the bladder causing detrusor smooth muscle contraction stimulate phospholipase C (PLC). PLC inhibition abolishes bladder contraction via P2Y6 but not that via M3 muscarinic receptors, indicating a receptor-dependent role of PLC. Therefore, we explored the role of PLC in rat bladder contraction by bradykinin. The PLC inhibitor U 73,122 [1-(6-[([17β]-3-methoxyestra-1,3,5[10]-trien-17-yl)-amino]hexyl)-1H-pyrrole-2,5-dione] did not affect the bradykinin response to a significantly greater degree than its inactive analog U 73,343 [10 μM each; 1-(6-[-([17β]-3-methoxyestra-1,3,5[10]-trien-17-yl)-amino]hexyl)-2,5-pyrrolidinedione], whereas the phospholipase D inhibitor b…

Malemedicine.medical_specialtyUrinary BladderMedizinBradykininPharmacologyBradykininCyclooxygenase pathwaychemistry.chemical_compoundOrgan Culture TechniquesInternal medicinemedicineAnimalsCalphostinRats WistarBradykinin receptorPharmacologyDose-Response Relationship DrugPhospholipase CMuscle SmoothSmooth muscle contractionRatsChelerythrineEndocrinologychemistryRho kinase inhibitorType C PhospholipasesMolecular MedicineMuscle ContractionJournal of Pharmacology and Experimental Therapeutics
researchProduct