Search results for "Pyrroles"

showing 10 items of 121 documents

The relaxant effects of cromakalim (BRL 34915) on human isolated airway smooth muscle

1992

Cromakalim (BRL 34915) is a potassium channel opener with therapeutic potential as a bronchodilator in asthma. Cromakalim (0.1–30 μmol/l) inhibited the spontaneous tone of human isolated bronchi n a concentration-related manner being nearly as effective as isoprenaline or theophylline. The order of relaxant potencies (expressed as -log10 IC50 mol/l; mean ±SEM) was isoprenaline (7.29 ± 0.27; n = 8) > cromakalim (5.89 ± 0.12; n = 7) > theophylline (4.07 ±0.13; n = 10). In human bronchi where tone had been raised by addition of histamine (0.1 mmol/l), acetylcholine (0.1 mmol/l) or leukotriene D4 (LTD4, 0.1 μmol/l), the relaxant effect of cromakalim was substantially reduced. Cromakalim suppres…

CromakalimMuscle RelaxationBronchiPharmacologyGlibenclamidechemistry.chemical_compoundTheophyllineIsoprenalinemedicineHumansBenzopyransDrug InteractionsPyrrolesPharmacologyTetraethylammoniumIsoproterenolMuscle SmoothGeneral MedicineAcetylcholineBronchodilator AgentschemistryAnesthesiaSRS-APotassium channel openermedicine.symptomCromakalimHistamineAcetylcholineHistamineMuscle contractionmedicine.drugNaunyn-Schmiedeberg's Archives of Pharmacology
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Effects of SCA40 on human isolated bronchus and human polymorphonuclear leukocytes: comparison with rolipram, SKF94120 and levcromakalim

1996

1. SCA40 (0.1 nM-0.1 mM) produced concentration-dependent suppression of the spontaneous tone of human isolated bronchus (-log EC50 = 6.85 +/- 0.09; n = 10) and reached a maximal relaxation similar to that of theophylline (3 mM). The potency (-log EC50 values) of SCA40 compared to other relaxants was rolipram (7.44 +/- 0.12; n = 9) > SCA40 > or = levcromakalim (6.49 +/- 0.04; n = 6) > SKF94120 (5.87 +/- 0.10; n = 9). 2. When tested against the activity of the isoenzymes of cyclic nucleotide phosphodiesterase (PDE) isolated from human bronchus, SCA40 proved highly potent against PDE III (-log IC50 = 6.47 +/- 0.16; n = 4). It was markedly less potent against PDE IV (4.82 +/- 0.18; n = 4) and …

Cromakalimmedicine.medical_specialtyCardiotonic AgentsNeutrophilsLeukotriene B4Muscle Relaxationchemistry.chemical_elementBronchiIn Vitro TechniquesCalciumPharmacologyLeukotriene B4chemistry.chemical_compound3'5'-Cyclic-GMP PhosphodiesterasesSuperoxidesInternal medicinemedicineHumansBenzopyransPyrrolesRolipramCyclic Nucleotide Phosphodiesterases Type 5PharmacologyCyclic nucleotide phosphodiesterasePhosphoric Diester HydrolasesSuperoxideAnti-Inflammatory Agents Non-SteroidalElastaseImidazolesN-Formylmethionine leucyl-phenylalanineCyclic Nucleotide Phosphodiesterases Type 3PyrrolidinonesBronchodilator AgentsCyclic Nucleotide Phosphodiesterases Type 4N-Formylmethionine Leucyl-PhenylalanineEndocrinologychemistry3'5'-Cyclic-AMP PhosphodiesterasesPyrazinesCalciumLeukocyte ElastaseRolipramCromakalimResearch Articlemedicine.drugBritish Journal of Pharmacology
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Mechanical and electrophysiological effects of cromakalim on the human urinary bladder.

1994

The effects of cromakalim on spontaneous and induced mechanical activity of human detrusor muscle were investigated in vitro. Cromakalim produces a concentration-related decrease of spontaneous as well as carbachol- and K(+)-evoked contractions. This is the first study to utilize the patch clamp technique to elucidate the mechanism of action of cromakalim on human detrusor cells. Cromakalim hyperpolarizes the detrusor cells by increasing the net outward current which is most likely carried by potassium ions. In the human urinary bladder, this effect is mediated by a glibenclamide-sensitive potassium channel, as glibenclamide is able to diminish the relaxant effect of cromakalim and to preve…

Detrusor muscleAdultMalemedicine.medical_specialtyCromakalimCarbacholPatch-Clamp TechniquesPotassium Channelsmedicine.drug_classUrologyGuinea PigsUrinary BladderIn Vitro Techniquesurologic and male genital diseasesMembrane Potentialschemistry.chemical_compoundInternal medicineMedicineAnimalsHumansBenzopyransPyrrolesPatch clampUrinary bladderbusiness.industryParasympatholyticsMuscle relaxantMuscle SmoothHyperpolarization (biology)Middle Agedmusculoskeletal systemfemale genital diseases and pregnancy complicationsPotassium channelRatsElectrophysiologyEndocrinologymedicine.anatomical_structurechemistrycardiovascular systemFemaleStress MechanicalbusinessCromakalimmedicine.drugMuscle ContractionInvestigative urology (Berlin, Germany)
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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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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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Self-Assembly-Directed Organization of a Fullerene–Bisporphyrin into Supramolecular Giant Donut Structures for Excited-State Charge Stabilization

2021

Functional materials composed of spontaneously self-assembled electron donor and acceptor entities capable of generating long-lived charge-separated states upon photoillumination are in great demand as they are key in building the next generation of light energy harvesting devices. However, creating such well-defined architectures is challenging due to the intricate molecular design, multistep synthesis, and issues associated in demonstrating long-lived electron transfer. In this study, we have accomplished these tasks and report the synthesis of a new fullerene–bis-Zn-porphyrin e-bisadduct by tether-directed functionalization of C60 via a multistep synthetic protocol. Supramolecular oligom…

FullereneSupramolecular structures and assembliesChemistrySupramolecular chemistryGeneral ChemistryBiochemistryAcceptorArticleCatalysisElectron transferColloid and Surface ChemistryCharge transferChemical structureChemical physicsExcited stateEnergy levelMoleculePyrrolesSelf-assemblyMolecular structure
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Synthesis and antiproliferative activity of thiazolyl-bis-pyrrolo[2,3-b]pyridines and indolyl-thiazolyl-pyrrolo[2,3-c]pyridines, nortopsentin analogu…

2015

Two new series of nortopsentin analogues, in which the imidazole ring of the natural product was replaced by thiazole and indole units were both substituted by 7-azaindole moieties or one indole unit was replaced by a 6-azaindole portion, were efficiently synthesized. Compounds belonging to both series inhibited the growth of HCT-116 colorectal cancer cells at low micromolar concentrations, whereas they did not affect the viability of normal-like intestinal cells. A compound of the former series induced apoptosis, evident as externalization of plasma membrane phosphatidylserine (PS), and changes of mitochondrial trans-membrane potential, while blocking the cell cycle in G2/M phase. In contr…

G2 Phaseantiproliferative activitybis-indolyl alkaloidsStereochemistryPyridinesPharmaceutical ScienceNortopsentin analoguesthiazolyl-bis-pyrrolo [23-b]pyridinesVacuoleArticlechemistry.chemical_compoundDrug DiscoveryImidazoleHumansPyrrolesautophagic deathThiazolelcsh:QH301-705.5Pharmacology Toxicology and Pharmaceutics (miscellaneous)Cell ProliferationIndole testMembrane Potential MitochondrialnortopsentinsDose-Response Relationship DrugMolecular Structureindolyl-thiazolyl-pyrrolo[23-c]pyridinesthiazolyl-bis-pyrrolo[23-b]pyridinesapoptosisPhosphatidylserineCell cycleHCT116 CellsSettore CHIM/08 - Chimica Farmaceuticaindolyl-thiazolyl-pyrrolo[23-<i>c</i>]pyridinesThiazoleslcsh:Biology (General)chemistryCytoplasmApoptosismarine alkaloidsthiazolyl-bis-pyrrolo [23-<i>b</i>]pyridinesMarine drugs
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High osmolarity glycerol (HOG) signalling in Magnaporthe oryzae: Identification of MoYPD1 and its role in osmoregulation, fungicide action, and patho…

2015

AbstractThis study comprises a first functional analysis of an YPD1-homologue in filamentous phytopathogenic fungi and its role in the HOG signalling pathway. We generated a gene deletion mutant of the gene MoYPD1 in Magnaporthe oryzae and characterized the resulting mutant strain. We have shown that MoYpd1p is a component of the phosphorelay system acting in the HOG pathway due to its Y2H protein interaction with the HKs MoHik1p and MoSln1p as well as with the response regulator MoSsk1p. Fungicidal activity of fludioxonil was reported to be based on the inhibition of MoHik1p resulting in hyperactivation of the HOG signalling pathway and lethality. Western analysis proved that both, osmotic…

GlycerolFilamentous fungiOsmotic shockMutantVirulenceFludioxonilDioxolesPlant ScienceFludioxonilBiologyMicrobiologyFungal ProteinsOsmoregulationOsmotic PressureGeneticsPyrrolesPhosphotransferGeneEcology Evolution Behavior and SystematicsPlant DiseasesVirulenceOsmolar ConcentrationOryzaHedgehog signaling pathwayFungicides IndustrialCell biologyMagnaportheResponse regulatorInfectious DiseasesPhosphorylationSignal TransductionEnvironmental signallingFungal Biology
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Rapid adaptation of signaling networks in the fungal pathogen Magnaporthe oryzae

2019

Abstract Background One fundamental question in biology is how the evolution of eukaryotic signaling networks has taken place. “Loss of function” (lof) mutants from components of the high osmolarity glycerol (HOG) signaling pathway in the filamentous fungus Magnaporthe oryzae are viable, but impaired in osmoregulation. Results After long-term cultivation upon high osmolarity, stable individuals with reestablished osmoregulation capacity arise independently from each of the mutants with inactivated HOG pathway. This phenomenon is extremely reproducible and occurs only in osmosensitive mutants related to the HOG pathway – not in other osmosensitive Magnaporthe mutants. The major compatible so…

GlycerolMagnaportheved/biology.organism_classification_rank.speciesMutantGenomeSalt StressTranscriptome0302 clinical medicineOsmoregulationLoss of Function MutationGene Expression Regulation FungalGene Regulatory NetworksSuppressorReestablishment of osmoregulation0303 health sciencesbiologyMagnaporthe oryzaeRewiringAdaptation PhysiologicalRapid adaptationCell biologyMagnaportheOsmoregulationEpigeneticsGenome FungalBiotechnologySignal TransductionResearch Articlelcsh:QH426-470lcsh:BiotechnologyDioxolesFungal Proteins03 medical and health sciencesDrug Resistance Fungallcsh:TP248.13-248.65GeneticsPyrrolesModel organismGene030304 developmental biologyPlant DiseasesOsmotic concentrationved/biologyGene Expression ProfilingEvolution of signaling networksHOG pathwayOryzabiology.organism_classificationlcsh:Genetics030217 neurology & neurosurgery
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Profile and molecular modeling of 3-(indole-3-yl)-4-(3,4,5-trimethoxyphenyl)-1 H-pyrrole-2,5-dione (1) as a highly selective VEGF-R2/3 inhibitor.

2006

We report on selectivity profiling of 1 in a panel of 20 protein kinases and molecular modeling indicating 1 to be highly active and selective for VEGF-R2/3. Sequence alignment analysis and detailed insights into the ATP binding pockets of targeted protein kinases from the panel result in a unique structural architecture of VEGF-R2 mainly caused by the hydrophobic pocket I, determining the molecular basis for activity and selectivity of 1.

Indole testModels MolecularBinding SitesIndolesMolecular modelStereochemistryChemistryKinaseMolecular Sequence DataBiological activitySequence alignmentCrystallography X-RayVascular Endothelial Growth Factor Receptor-3Vascular Endothelial Growth Factor Receptor-2Drug DiscoveryMolecular MedicinePyrrolesAmino Acid SequenceBinding siteSelectivityPeptide sequenceHydrophobic and Hydrophilic InteractionsJournal of medicinal chemistry
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