Search results for "TAGL"

showing 10 items of 296 documents

Mechanisms involved in the relaxant action of testosterone in the renal artery from male normoglycemic and diabetic rabbits.

2009

Kidney disease is a frequent complication in diabetes, and significant differences have been reported between male and female patients. Our working hypothesis was that diabetes might modify the vascular actions of testosterone in isolated rabbit renal arteries and the mechanisms involved in these actions. Testosterone (10(-8) to 10(-4)M) induced relaxation of precontracted arteries, without significant differences between control and diabetic rabbits. Both in control and diabetic rabbits endothelium removal inhibited testosterone relaxant action. In arteries with endothelium, incubation with indomethacin (10(-5)M), N(G)-nitro-l-arginine (10(-5)M) or tetraethylammonium (10(-5)M) did not modi…

Blood GlucoseMalemedicine.medical_specialtyEndotheliumNitric Oxide Synthase Type IIIThromboxaneBlotting WesternIndomethacinNitric Oxide Synthase Type IIProstacyclinVasodilationNitroarginineMuscle Smooth VascularDiabetes Mellitus ExperimentalImmunoenzyme TechniquesThromboxane A2Renal ArteryEnosInternal medicinemedicine.arteryDiabetes mellitusmedicinePotassium Channel BlockersAnimalsCyclooxygenase InhibitorsProstaglandins ITestosteroneRenal arteryPharmacologybiologyDose-Response Relationship Drugbusiness.industryTetraethylammoniumTestosterone (patch)medicine.diseasebiology.organism_classificationVasodilationEndocrinologymedicine.anatomical_structureCyclooxygenase 2Cyclooxygenase 1PotassiumCalciumEndothelium VascularRabbitsbusinessmedicine.drugSignal TransductionPharmacological research
researchProduct

Native, Intact Glucagon-Like Peptide 1 Is a Natural Suppressor of Thrombus Growth Under Physiological Flow Conditions

2020

Objective: In patients with diabetes mellitus, increased platelet reactivity predicts cardiac events. Limited evidence suggests that DPP-4 (dipeptidyl peptidase 4) influences platelets via GLP-1 (glucagon-like peptide 1)-dependent effects. Because DPP-4 inhibitors are frequently used in diabetes mellitus to improve the GLP-1-regulated glucose metabolism, we characterized the role of DPP-4 inhibition and of native intact versus DPP-4-cleaved GLP-1 on flow-dependent thrombus formation in mouse and human blood. Approach and Results: An ex vivo whole blood microfluidics model was applied to approach in vivo thrombosis and study collagen-dependent platelet adhesion, activation, and thrombus for…

Blood Platelets0301 basic medicineendocrine systemmedicine.medical_specialtyPlatelet AggregationPLATELET ACTIVATIONLinagliptin030204 cardiovascular system & hematologyDPP4Glucagon-Like Peptide-1 Receptorlaw.invention03 medical and health sciences0302 clinical medicinedipeptidyl peptidase 4Fibrinolytic AgentslawInternal medicineDiabetes mellitusmedicineAnimalsHumansPlateletIn patientThrombusglucose610 Medicine & healthDipeptidyl peptidase-4Mice KnockoutDipeptidyl-Peptidase IV InhibitorsChemistryPharmacology. TherapySitagliptin Phosphatedigestive oral and skin physiologyThrombosismedicine.diseaseGlucagon-like peptide-1Peptide Fragmentsglucagon-like peptide 1Mice Inbred C57BLMICE030104 developmental biologyEndocrinologyPhysiological flowdiabetes mellitusplateletsSuppressorHuman medicineCardiology and Cardiovascular MedicineSignal Transduction
researchProduct

Synthesis and Evaluation of a Novel Series of Pyrrolizine Derivatives as Dual Cyclooxygenase-1 and 5-Lipoxygenase Inhibitors

1997

The aim of our study was to investigate structure activity relationship following the replacement of the 6-phenyl substituent at the 6,7-diaryl-2,3-dihydropyrrolizine template by various heteroaromatic residues. In this context we developed a new, efficient, and highly sensitive test method for the screening of dual cyclooxygenase-1 (COX-1) and 5-lipoxygenase (5-LOX) inhibitors. We used human platelets as a source of COX-1 and human PMNLs as a source of 5-LOX. Both cell types were isolated from the same volume of blood. PGE2 and LTB4 respectively were determined by highly selective and sensitive ELISA kits, using monoclonal antibodies. For a single determination at most 0.5 mL whole blood i…

Blood PlateletsMaleNeutrophilsmedicine.drug_classPharmaceutical ScienceContext (language use)Monoclonal antibodyChemical synthesisDrug DiscoverymedicineHumansStructure–activity relationshipCyclooxygenase InhibitorsPyrrolesLipoxygenase InhibitorsWhole bloodArachidonate 5-LipoxygenasebiologyChemistryMembrane ProteinsIn vitroIsoenzymesBiochemistryProstaglandin-Endoperoxide SynthasesEnzyme inhibitorArachidonate 5-lipoxygenaseCyclooxygenase 1biology.proteinFemaleArchiv der Pharmazie
researchProduct

Anti-inflammatory and analgesic activity of a novel inhibitor of microsomal prostaglandin E synthase-1 expression

2009

Abstract In a previous study, we reported a new γ-hydroxybutenolide derivative, 4-benzo[ b ]thiophen-2-yl-3-bromo-5-hydroxy-5 H -furan-2-one (BTH), as inhibitor of microsomal prostaglandin E synthase-1 (mPGES-1) expression in lypopolysaccharide (LPS) stimulated RAW 264.7 and TPH-1 cells, without affecting cyclooxygenase-2 (COX-2). In this study, we evaluated the in vivo effect of BTH on some acute and chronic inflammatory animal models in relation to its inhibitory profile on mPGES-1 expression. In the zymosan-induced mouse air pouch model, BTH produced a dose-dependent inhibition of prostaglandin E 2 (PGE 2 ) production and mPGES-1 protein expression in pouch exudates without any effect on…

Blood PlateletsMaleNeutrophilsmedicine.drug_classmedicine.medical_treatmentAnti-Inflammatory AgentsProstaglandinInflammationThiophenesAcetatesPharmacologyProstaglandin E synthaseLeukotriene B4Gene Expression Regulation EnzymologicAnti-inflammatoryMicechemistry.chemical_compound4-ButyrolactoneIn vivomedicineAnimalsHumansProstaglandin-E SynthasesInflammationPharmacologyAnalgesicsBehavior AnimalbiologyArthritis ExperimentalIntramolecular OxidoreductasesThromboxane B2BiochemistrychemistryHyperalgesiaChronic DiseaseHyperalgesiabiology.proteinCattlelipids (amino acids peptides and proteins)Arachidonic acidmedicine.symptomProstaglandin E
researchProduct

Cyclooxygenase-1/2 (COX-1/COX-2) and 5-lipoxygenase (5-LOX) inhibitors of the 6,7-diaryl-2,3-1H-dihydropyrrolizine type

2003

A series of 6,7-diaryl-2,3-1H-dihydropyrrolizines was prepared as COX-1/COX-2 and 5-LOX inhibitors. The inhibition of COX-1 was evaluated using intact bovine platelets as the enzyme source, whereas LPS-stimulated human monocytes served as the enzyme source for inducible COX-2. The determination of arachidonic metabolites was performed by HPLC for COX-1 and RIA for COX-2. The balance between COX-1/COX-2 and 5-LOX inhibition can be shifted by modifying the substitution pattern of the phenyl moiety at the 6- and 7-position of the pyrrolizine nucleus. Structure-activity relationships are discussed.

Blood PlateletsRadioimmunoassayHigh-performance liquid chromatographyIsozymeMonocytesDrug DiscoverymedicineCox 1 cox 2AnimalsHumansMoietyStructure–activity relationshipPyrrolesPlateletLipoxygenase InhibitorsEnzyme InhibitorsChromatography High Pressure LiquidPharmacologychemistry.chemical_classificationbiologyChemistryOrganic ChemistryMembrane ProteinsGeneral MedicineIn vitroIsoenzymesmedicine.anatomical_structureEnzymeBiochemistryCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesEnzyme inhibitorDrug DesignArachidonate 5-lipoxygenaseCyclooxygenase 1biology.proteinCattleCyclooxygenaseNucleusEuropean Journal of Medicinal Chemistry
researchProduct

Reciprocal regulation of human platelet function by endogenous prostanoids and through multiple prostanoid receptors

2014

Platelets are permanently exposed to a variety of prostanoids formed by blood cells or the vessel wall. The two major prostanoids, prostacyclin and thromboxane act through well established pathways mediated by their respective G-protein coupled receptors inhibiting or promoting platelet aggregation accordingly. Yet the role of other prostanoids and prostanoid receptors for platelet function regulation has not been thoroughly investigated. We aimed at a comprehensive analysis of prostanoid effects on platelets, the receptors and pathways involved and functional consequences. We analyzed cAMP formation and phosphorylation of proteins pivotal to platelet function as well as functional platelet…

Blood PlateletsSerotoninmedicine.medical_specialtyPlatelet AggregationProstaglandin E2 receptorReceptors ProstaglandinProstaglandinProstacyclinchemistry.chemical_compoundAdenosine TriphosphateP2Y12Internal medicineCyclic AMPmedicineHumansPlateletPlatelet activationReceptorMitogen-Activated Protein Kinase KinasesPharmacologyChemistryMicrofilament Proteinsrap1 GTP-Binding ProteinsProstanoidrespiratory systemPhosphoproteinsCell biologyAdenosine DiphosphateP-SelectinEndocrinologyProstaglandinscardiovascular systemCalciumlipids (amino acids peptides and proteins)Cell Adhesion Moleculesmedicine.drugEuropean Journal of Pharmacology
researchProduct

COX-1/COX-2 inhibitors based on the methanone moiety

2002

This paper focuses on the synthesis and the in vitro testing of dual COX-1/COX-2 inhibitors. Starting from structures of non-steroidal anti-inflammatory drugs (NSAIDs) the diaryl methanone element was chosen as a lead. Modifications were carried out on this scaffold to obtain potent inhibitors of the COX enzymes. The N-(2-aroylphenyl)sulphonamides and -amides were studied in detail, and to consolidate the data evaluated the corresponding 3- and 4-regioisomers were also investigated. The potency and the enzyme selectivity were varied by structural modifications of the lead.

Blood PlateletsStereochemistrymedicine.drug_classDrug Evaluation PreclinicalCarboxamideIsozymeChemical synthesisStructure-Activity RelationshipOxazinesDrug DiscoverymedicineAnimalsPotencyMoietyCyclooxygenase InhibitorsPharmacologychemistry.chemical_classificationCyclooxygenase 2 InhibitorsMolecular StructurebiologyChemistryAnti-Inflammatory Agents Non-SteroidalOrganic ChemistryGeneral MedicineIn vitroIsoenzymesEnzymeCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesEnzyme inhibitorCyclooxygenase 1biology.proteinEuropean Journal of Medicinal Chemistry
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

Griffonianone D, an isoflavone with anti-inflammatory activity from the root bark of Millettia griffoniana.

2003

A new isoflavone, griffonianone D (1), and the previously known compounds durmillone and odorantin were isolated from a chloroform extract of the root bark of Millettia griffoniana. The structure of 1 was established as (7E)-(6",7"-dihydroxy-3",7"-dimethyloct-2"-enyl)oxy-4'-methoxyisoflavone on the basis of its spectral data. The chloroform extract of the root bark of M. griffoniana and compound 1 showed anti-inflammatory effects in different experimental models of inflammation.

Blood Plateletsmedicine.drug_classFlavonoidPharmaceutical SciencePlant RootsAnti-inflammatoryMillettiaPhospholipases AAnalytical Chemistrychemistry.chemical_compoundDrug DiscoveryBotanymedicineLeukocytesAnimalsEdemaHumansCameroonSpectral dataNuclear Magnetic Resonance BiomolecularPharmacologychemistry.chemical_classificationFlavonoidsChloroformPlants MedicinalTraditional medicinebiologyMolecular StructureOrganic ChemistryAnti-Inflammatory Agents Non-SteroidalGriffonianone DEarStereoisomerismbiology.organism_classificationIsoflavonesMillettiaRatsPhospholipases AComplementary and alternative medicinechemistryProstaglandin-Endoperoxide Synthasesvisual_artvisual_art.visual_art_mediumPlant BarkMolecular MedicineBarkJournal of natural products
researchProduct

Synergistic interaction of adenylate cyclase activators and nitric oxide donor SIN-1 on platelet cyclic AMP

1995

Abstract The molecular mechanism of the synergistic platelet inhibition by activators of adenylate cyclase and guanylate cyclase in human platelets was investigated. The adenylate cyclase activators iloprost and prostaglandin E 1 and the guanylate cyclase activator 3-morpholino-synonimine (SIN-1) dose-dependently inhibited thrombin-induced aggregation of washed human platelets. Furthermore, SIN-1 at a concentration inhibiting platelet aggregation by only 10% shifted the IC 50 values of iloprost and prostaglandin E 1 by one order of magnitude to the left, indicating a synergistic action of adenylate cyclase and guanylate cyclase activators. Iloprost and prostaglandin E 1 dose-dependently ele…

Blood Plateletsmedicine.medical_specialtyGUCY1B3Platelet Aggregationmedicine.medical_treatmentAdenylate kinaseIn Vitro TechniquesNitric OxideCyclasechemistry.chemical_compoundInternal medicineCyclic AMPmedicineHumansPlateletIloprostAlprostadilCyclic GMPPharmacologyForskolinGUCY1A3PhosphodiesteraseDrug SynergismEnzyme ActivationEndocrinologychemistryGuanylate CyclaseMolsidominelipids (amino acids peptides and proteins)Platelet Aggregation InhibitorsAdenylyl CyclasesProstaglandin EEuropean Journal of Pharmacology: Molecular Pharmacology
researchProduct