Search results for "Cyclooxygenase Inhibitor"

showing 10 items of 77 documents

Diclofenac sodium and cyclosporin A inhibit human lens epithelial cell proliferation in culture.

1997

• Purpose: To investigate the effect of diclofenac sodium salt and cyclosporin A (CsA) on human lens epithelial cell (HLEC) growth in culture. • Methods: Cultures of HLEC were obtained from anterior capsules from extracapsular cataract surgery. Third-passage cells were seeded in 96-well plates in 0.1 ml culture medium. Cytotoxicity was estimated by the tetrazolium test in confluent monolayers after 24 h exposure to a wide range of concentrations of diclofenac and CsA. The effect of subcytotoxic concentrations of diclofenac and CsA on HLEC proliferation in subconfluent cultures was evaluated after 24 and 72 h of exposure. To investigate the relationship between PGEZ synthesis and the inhibit…

DiclofenacCell SurvivalBiologyPharmacologyDinoprostoneEpitheliumCellular and Molecular NeuroscienceDiclofenacIn vivoCyclosporin aChlorocebus aethiopsLens CrystallinemedicineAnimalsHumansCyclooxygenase InhibitorsCytotoxicityVero CellsCells CulturedAgedRadioimmunoassayEpithelial CellsDiclofenac SodiumMiddle AgedSensory Systemsstomatognathic diseasesOphthalmologyBiochemistryCell cultureCyclosporineLens epithelial cell proliferationCell DivisionImmunosuppressive Agentsmedicine.drugGraefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie
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The pyrrole moiety as a template for COX-1/COX-2 inhibitors

2000

Aroyl- and thiophene-substituted pyrrole derivatives have been synthesized as a new class of COX-1/COX-2 inhibitors. The inhibition of COX-1 was evaluated in a biological system using bovine PMNLs as the enzyme source, whereas LPS-stimulated human monocytes served as the enzyme source for inducible COX-2. The determination of the concentration of arachidonic acid metabolites was performed by HPLC for COX-1 and RIA for COX-2. Variation of the substitution pattern led to a series of active compounds which showed inhibition for COX-1 and COX-2. Structural requirements for the development of COX-1/COX-2 inhibitors are discussed.

DiclofenacNeutrophilsStereochemistryIndomethacinThiophenesHigh-performance liquid chromatographyMonocytesPyrrole derivativeschemistry.chemical_compoundDrug DiscoveryAnimalsHumansStructure–activity relationshipMoietyCyclooxygenase InhibitorsPyrrolesSulfonesPyrrolePharmacologychemistry.chemical_classificationArachidonic AcidCyclooxygenase 2 InhibitorsMolecular StructureAnti-Inflammatory Agents Non-SteroidalOrganic ChemistryMembrane ProteinsGeneral MedicineIsoenzymesEnzymechemistryMembrane proteinBiochemistryCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesCyclooxygenase 1Leukocytes MononuclearCattleArachidonic acidEuropean Journal of Medicinal Chemistry
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Biowaiver monograph for immediate-release solid oral dosage forms: acetylsalicylic acid.

2012

A biowaiver monograph for acetylsalicylic acid (ASA) is presented. Literature and experimental data indicate that ASA is a highly soluble and highly permeable drug, leading to assignment of this active pharmaceutical ingredient (API) to Class I of the Biopharmaceutics Classification System (BCS). Limited bioequivalence (BE) studies reported in the literature indicate that products that have been tested are bioequivalent. Most of the excipients used in products with a marketing authorization in Europe are not considered to have an impact on gastrointestinal motility or permeability. Furthermore, ASA has a wide therapeutic index. Thus, the risks to the patient that might occur if a nonbioequi…

Drugmedia_common.quotation_subjectPharmaceutical ScienceAdministration OralBiological AvailabilityPharmacologyBioequivalenceMarketing authorizationDosage formDrug StabilityFibrinolytic AgentsAnimalsHumansCyclooxygenase Inhibitorsmedia_commonActive ingredientAspirinChemistryAnti-Inflammatory Agents Non-SteroidalBiopharmaceutics Classification SystemSolubilityTherapeutic EquivalencyPlatelet aggregation inhibitorCaco-2 CellsFibrinolytic agentPlatelet Aggregation InhibitorsTabletsJournal of pharmaceutical sciences
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Licofelone, a novel 5-LOX/COX-inhibitor, attenuates leukocyte rolling and adhesion on endothelium under flow

2005

The main mechanism of action of non-steroidal anti-inflammatory drugs (NSAIDs) is the inhibition of cycloxygenases COX-1 and COX-2. During recent years, combined 5-LOX/COX-inhibition, interfering with the biosynthesis of both prostaglandins and leukotrienes (LTs), has emerged as a possibility to avoid side effects related to COX-inhibition. The aim of the present study was to investigate if there is a contribution of mechanisms other than the reduction of inflammatory prostaglandins and leukotrienes to the anti-inflammatory effect of the LOX/COX inhibitor licofelone. In a flow chamber assay, licofelone (10-30 microM) dose-dependently decreased both the rolling and adhesion of leukocytes on …

EndotheliumAcetatesPharmacologyBiochemistrychemistry.chemical_compoundCell MovementIn vivoCell AdhesionLeukocytesmedicineHumansCyclooxygenase InhibitorsPyrrolesLipoxygenase InhibitorsRNA MessengerCells CulturedPharmacologybiologyChemistryEndothelial Cellsmedicine.anatomical_structureMechanism of actionImmunologyArachidonate 5-lipoxygenaseCelecoxibbiology.proteinCyclooxygenasemedicine.symptomLicofeloneCell Adhesion MoleculesSelectinmedicine.drugBiochemical Pharmacology
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Diverse compounds mimic Alzheimer disease–causing mutations by augmenting Aβ42 production

2004

Increased Abeta42 production has been linked to the development of Alzheimer disease. We now identify a number of compounds that raise Abeta42. Among the more potent Abeta42-raising agents identified are fenofibrate, an antilipidemic agent, and celecoxib, a COX-2-selective NSAID. Many COX-2-selective NSAIDs tested raised Abeta42, including multiple COX-2-selective derivatives of two Abeta42-lowering NSAIDs. Compounds devoid of COX activity and the endogenous isoprenoids FPP and GGPP also raised Abeta42. These compounds seem to target the gamma-secretase complex, increasing gamma-secretase-catalyzed production of Abeta42 in vitro. Short-term in vivo studies show that two Abeta42-raising comp…

Enzyme-Linked Immunosorbent AssayEndogenyProtein Serine-Threonine KinasesPharmacologyTransfectionMass SpectrometryGeneral Biochemistry Genetics and Molecular BiologyPresenilinCell LineFenofibrateAlzheimer DiseaseIn vivoEndopeptidasesmedicineAspartic Acid EndopeptidasesHumansImmunoprecipitationCyclooxygenase InhibitorsProtein precursorHypolipidemic AgentsSulfonamidesrho-Associated KinasesAmyloid beta-PeptidesFenofibratebusiness.industryAnti-Inflammatory Agents Non-SteroidalIntracellular Signaling Peptides and ProteinsBrainGeneral Medicinemedicine.diseaseIn vitroEnzyme ActivationBiochemistryCelecoxibPyrazolesFemaleAmyloid Precursor Protein SecretasesAlzheimer's diseaserhoA GTP-Binding ProteinbusinessAntilipidemic Agentmedicine.drugNature Medicine
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Flavonoids from Acacia pennata and their Cyclooxygenase (COX-1 and COX-2) Inhibitory Activities

2007

Two new flavonoids quercetin 4'-O-alpha-L-rhamnopyranosyl-3-O-beta-D-allopyranoside (1) and apigenin 6-C-[2''-O-(E)-feruloyl- beta-D-glucopyranosyl]-8-C-beta-glucopyranoside (2), along with the known isorhamnetin 3-O-alpha-L-rhamnopyranoside (3), kaempferol 3-O-alpha-L-rhamnopyranosyl-(1-->4)-beta-D-glucopyranoside (4), and isovitexin (5) were isolated from the leaves of Acacia pennata Willd. (Mimosaceae) and tested for their anti-inflammatory activity. Their structures were determined by 1D and 2D NMR and mass spectrometry. They were tested for an inhibitory effect on COX-1 and COX-2, showing 60-90% inhibition at 10(-4) g/mL and 5-14% inhibition at 10(-4) g/mL, respectively.

FlavonoidIsovitexinPharmaceutical ScienceBiologyPharmacognosyAnalytical ChemistryInhibitory Concentration 50chemistry.chemical_compoundDrug DiscoveryHumansCyclooxygenase InhibitorsPhenolsIsorhamnetinPharmacologychemistry.chemical_classificationTraditional medicinePlant ExtractsOrganic ChemistryAcaciaFlavonesPlant LeavesComplementary and alternative medicinechemistryBiochemistryCyclooxygenase 2ApigeninCyclooxygenase 1Molecular MedicineKaempferolQuercetinPhytotherapyPlanta Medica
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Effects of some isoxazolpyrimidine derivatives on nitric oxide and eicosanoid biosynthesis

2000

Abstract The inhibitory effect of some isoxazolpyrimidine derivatives on iNOS and COX-2 endotoxin induction in mouse peritoneal macrophages has been studied. Three of these compounds inhibited nitrite and PGE2 accumulation in a concentration dependent-manner at μM range. None of these active compounds affected iNOS, COX-2, COX-1 or PLA2 activities, although some reduced iNOS or COX-2 expression. Besides, no effect was observed on human neutrophil inflammatory responses (LTB4 biosynthesis and Superoxide or elastase release). Active compounds were assayed by oral administration in the mouse air pouch model, where they inhibited nitrite accumulation without affecting PGE 2 levels or leukocyte …

Leukocyte migrationNeutrophilsBlotting WesternPharmacologyNitric OxideLeukotriene B4DinoprostonePhospholipases AGeneral Biochemistry Genetics and Molecular BiologyNitric oxideMicechemistry.chemical_compoundSuperoxidesOral administrationAnimalsHumansCyclooxygenase InhibitorsGeneral Pharmacology Toxicology and PharmaceuticsNitriteOxazolesInhibitory effectCyclooxygenase 2 InhibitorsPancreatic ElastaseSuperoxideElastaseMembrane ProteinsGeneral MedicineIsoenzymesPhospholipases A2PyrimidinesBiochemistrychemistryCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesLuminescent MeasurementsCyclooxygenase 1EicosanoidsFemalelipids (amino acids peptides and proteins)Eicosanoid biosynthesis
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6-Dimethylamino 1H-pyrazolo[3,4-d]pyrimidine derivatives as new inhibitors of inflammatory mediators in intact cells.

2003

The synthesis of 6-dimethylamino 1H-pyrazolo[3,4-d]pyrimidines substituted at positions 1 and 4, and their effects on murine macrophage and human neutrophil functions are described. Several compounds and especially 4b-6b are potent inhibitors of PGE2 generation in murine macrophages. This action is related to a direct effect on COX-2 activity without affecting the enzyme expression. Some of these compounds also inhibited COX-1 and COX-2 in human monocytes and 4b showed selectivity for COX-2 inhibition. © 2003 Elsevier Science Ltd. All rights reserved.

LipopolysaccharidesMagnetic Resonance SpectroscopyPyrimidineClinical BiochemistryBlotting WesternPharmaceutical ScienceBiochemistryLeukotriene B4Pyrazolopyrimidinechemistry.chemical_compoundMiceStructure-Activity RelationshipDrug DiscoverymedicineLeukocytesMacrophageAnimalsHumansCyclooxygenase InhibitorsMolecular Biologychemistry.chemical_classificationbiologyCyclooxygenase 2 InhibitorsPancreatic ElastaseMonocyteOrganic ChemistryMembrane ProteinsBiological activityIn vitroIsoenzymesEnzymemedicine.anatomical_structurePyrimidineschemistryBiochemistryEnzyme inhibitorCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesLuminescent Measurementsbiology.proteinCyclooxygenase 1Macrophages PeritonealMolecular MedicinePyrazolesInflammation MediatorsBioorganicmedicinal chemistry
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Potentiation of the antitumor effects of both selective cyclooxygenase-1 and cyclooxygenase-2 inhibitors in human hepatic cancer cells by inhibition …

2007

The molecular mechanisms behind the anti-neoplastic effects of non-steroidal anti-inflammatory drugs (NSAIDs) are not completely understood and cannot be explained by the inhibition of the cyclooxygenase (COX) enzymes COX-1 and COX-2 alone. We previously reported that both the selective COX-1 inhibitor SC-560 and the selective COX-2 inhibitor CAY10404 exhibit anti-tumor effects in human hepatoma cells. NSAID inhibitors have many COX-independent actions and, among others, the mitogen-activated protein kinase (MAPK) pathways are targets for NSAIDs. Here, we examined the role of MEK/ERK1/2 signaling in the anti-neoplastic effects of both selective COX-1 and COX-2 inhibitors in two human hepato…

MAPK/ERK pathwayCancer ResearchCarcinoma HepatocellularTime FactorsBlotting WesternApoptosisPharmacologyCOX-1 COX-2 NSAIDs MEK1/2 ERK1/2NitrilesButadienesTumor Cells CulturedHumansCyclooxygenase InhibitorsSulfonesEnzyme InhibitorsPhosphorylationProtein kinase ACell ProliferationPharmacologychemistry.chemical_classificationMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase KinasesMitogen-Activated Protein Kinase 3biologyDose-Response Relationship DrugLiver NeoplasmsCytochromes cLong-term potentiationDrug SynergismIsoxazolesFlow CytometryEnzymeOncologychemistryCyclooxygenase 2CaspasesCancer cellbiology.proteinCyclooxygenase 1Molecular MedicineMEK-ERK PathwayPyrazolesDrug Therapy CombinationCyclooxygenaseHepatoma cellCancer biologytherapy
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Convergent synthesis and preliminary biological evaluations of the stilbenolignan (±)-aiphanol and various congeners

2003

Treatment of an equimolar mixture of stilbene 7 and cinnamyl alcohol 8 with silver carbonate in acetone–benzene afforded a ca. 2 : 1 : 2 : 1 mixture of the stilbenolignan (±)-aiphanol (1) and congeners 2–4 each of which show significant anti-angiogenic and COX-2 inhibitory properties.

Magnetic Resonance SpectroscopyConvergent synthesisAngiogenesis InhibitorsBiochemistryInhibitory Concentration 50chemistry.chemical_compoundStilbenesAnimalsOrganic chemistryBioassayCyclooxygenase InhibitorsPhysical and Theoretical ChemistryBenzeneAortaSilver carbonateCyclooxygenase 2 InhibitorsDose-Response Relationship DrugCinnamyl alcoholChemistryOrganic ChemistryMembrane ProteinsStereoisomerismRatsIsoenzymesEnzyme inhibitionCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesCyclooxygenase 1Org. Biomol. Chem.
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