Search results for "Isoenzyme"

showing 10 items of 247 documents

Leptin: A pivotal mediator of intestinal inflammation in mice

2002

Abstract Background & Aims: In addition to acting as a regulator of food intake and energy expenditure, leptin can also modulate immune and inflammatory responses. The role of leptin in intestinal inflammation is the focus of the present study. Methods: Acute and chronic colitis were induced in leptin-deficient ob/ob or wild-type (WT) mice using dextran sulfate sodium (DSS) or trinitrobenzene sulfonic acid (TNBS). The severity of colitis was evaluated, and possible mechanisms were studied. Results: Leptin directly stimulates intraepithelial lymphocytes (IELs) and lamina propria mononuclear cells (LPMCs). In the DSS acute model, ob/ob mice exhibited a 72% reduction of colitis severity and sp…

LeptinSTAT3 Transcription Factormedicine.medical_specialtyColonanimal diseasesdigestive systemMonocytesProinflammatory cytokineMiceReference ValuesInternal medicinemedicineAnimalsInterferon gammaLymphocytesObesityIntestinal MucosaColitisMacrophage inflammatory proteinCells CulturedLeptin DeficiencyHepatologybusiness.industryLeptinDextran SulfateGastroenterologyColitismedicine.diseasedigestive system diseasesDNA-Binding ProteinsIsoenzymesMice Inbred C57BLEndocrinologyTrinitrobenzenesulfonic AcidCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesEnzyme InductionChronic DiseaseImmunologyTrans-ActivatorsCytokinesIntraepithelial lymphocyteFemaleTumor necrosis factor alphaDisease SusceptibilityChemokinesbusinessmedicine.drugGastroenterology
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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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eNOS S-nitrosylates β-actin on Cys374 and regulates PKC-θ at the immune synapse by impairing actin binding to profilin-1.

2017

The actin cytoskeleton coordinates the organization of signaling microclusters at the immune synapse (IS); however, the mechanisms involved remain poorly understood. We show here that nitric oxide (NO) generated by endothelial nitric oxide synthase (eNOS) controls the coalescence of protein kinase C-¿ (PKC-¿) at the central supramolecular activation cluster (c-SMAC) of the IS. eNOS translocated with the Golgi to the IS and partially colocalized with F-actin around the c-SMAC. This resulted in reduced actin polymerization and centripetal retrograde flow of ß-actin and PKC-¿ from the lamellipodium-like distal (d)-SMAC, promoting PKC-¿ activation. Furthermore, eNOS-derived NO S-nitrosylated ß-…

Life Sciences & Biomedicine - Other Topics0301 basic medicinePOLARIZATIONIMMUNOLOGICAL SYNAPSEImmunological SynapsesT-LymphocytesPROTEINGolgi ApparatusCYTOSKELETONRetrograde FlowBiochemistryARP2/3 COMPLEXT-CELL-ACTIVATIONProfilinsWhite Blood CellsContractile ProteinsFluorescence MicroscopyAnimal CellsMedicine and Health SciencesPseudopodiaBiology (General)Post-Translational ModificationCells CulturedProtein Kinase CMicroscopyT CellsGeneral NeuroscienceLight MicroscopyNeurochemistryRecombinant Proteins3. Good healthIsoenzymesPOLYMERIZATIONProtein TransportCell ProcessesRNA InterferenceCellular TypesNeurochemicalsGeneral Agricultural and Biological SciencesLife Sciences & BiomedicineResearch ArticleBiochemistry & Molecular BiologyNitric Oxide Synthase Type IIIQH301-705.5Imaging TechniquesRecombinant Fusion ProteinsImmune CellsImmunologyLibrary scienceAntigen-Presenting Cellsmacromolecular substancesBiologyNitric OxideResearch and Analysis MethodsGeneral Biochemistry Genetics and Molecular BiologyCell Line03 medical and health sciencesFluorescence ImagingHumansCysteineNITRIC-OXIDE SYNTHASEBiologyScience & TechnologyBlood CellsRECEPTORGeneral Immunology and MicrobiologyBiology and Life SciencesProteinsCell BiologyActinsS-NitrosylationEnzyme ActivationLuminescent ProteinsCytoskeletal Proteins030104 developmental biologyAmino Acid SubstitutionRETROGRADE FLOWProtein Kinase C-thetaMutationProtein Processing Post-TranslationalNeuroscienceActin PolymerizationPLoS biology
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An anti-inflammatory ditriazine inhibiting leukocyte functions and expression of inducible nitric oxide synthase and cyclo-oxygenase-2.

2000

A ditriazine derivative (4,10-dichloropyrido[5,6:4,5]thieno[3,2-d':3, 2-d]-1,2,3-ditriazine (DTD)) inhibited neutrophil functions, including degranulation, superoxide generation, and leukotriene B(4) production, without any effect on 5-lipoxygenase activity. This compound reduced nitric oxide (NO) and prostaglandin E(2) production in mouse peritoneal macrophages stimulated with lipopolysaccharide, whereas no influence on the activity of inducible NO synthase, cyclo-oxygenase-2 or cyclo-oxygenase-1 was observed. DTD significantly reduced mouse paw oedema induced by carrageenan and also markedly reduced NO and prostaglandin E(2) levels in exudates from 24-h zymosan-stimulated mouse air pouch.…

LipopolysaccharideLeukotriene B4Neutrophilsmedicine.medical_treatmentAnti-Inflammatory AgentsNitric Oxide Synthase Type IICarrageenanNeutrophil Activationchemistry.chemical_compoundMiceLeukocytesEdemaProstaglandin E2biologyPancreatic ElastaseSuperoxideTriazinesHindlimbNitric oxide synthaseIsoenzymesBiochemistryFemalemedicine.drugProstaglandin EBlood PlateletsLeukotriene B4DinoprostonePhospholipases ANitric oxideMicrosomesmedicineAnimalsHumansNitritesPharmacologyInflammationCell-Free SystemDose-Response Relationship DrugZymosanMembrane ProteinsMolecular biologyThromboxane B2chemistryEicosanoidCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesLuminescent Measurementsbiology.proteinMacrophages PeritonealNitric Oxide SynthaseEuropean journal of pharmacology
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Novel anti-inflammatory chalcone derivatives inhibit the induction of nitric oxide synthase and cyclooxygenase-2 in mouse peritoneal macrophages

1999

AbstractIn a previous work, we tested a series of chalcone derivatives as possible anti-inflammatory compounds. We now investigate the effects of three of those compounds, CH1, CH8 and CH12, on nitric oxide and prostanoid generation in mouse peritoneal macrophages stimulated with lipopolysaccharide and in the mouse air pouch injected with zymosan, where they showed a dose-dependent inhibition with inhibitory concentration 50% values in the μM range. This effect was not the consequence of a direct inhibitory action on enzyme activities. Our results demonstrated that chalcone derivatives inhibited de novo inducible nitric oxide synthase and cyclooxygenase-2 synthesis, being a novel therapeuti…

LipopolysaccharidesChalconeLipopolysaccharidemedicine.drug_classBiophysicsNitric Oxide Synthase Type IILipopolysaccharidePharmacologyBiochemistryDinoprostoneAnti-inflammatoryNitric oxideMicechemistry.chemical_compoundChalconeStructural BiologyGeneticsmedicineAnimalsCyclooxygenase-2Mouse air pouchInducible nitric oxide synthaseMolecular BiologyNitritesDose-Response Relationship DrugbiologyAnti-Inflammatory Agents Non-SteroidalZymosanZymosanProstanoidMouse peritoneal macrophageCell BiologyIsoenzymesNitric oxide synthasechemistryBiochemistryCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesEnzyme InductionMacrophages Peritonealbiology.proteinFemaleCyclooxygenaseNitric Oxide SynthaseFEBS Letters
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Expressional control of the ‘constitutive’ isoforms of nitric oxide synthase (NOS I and NOS III)

1998

Nitric oxide synthase (NOS) exists in three established isoforms. NOS I (NOS1, ncNOS) was originally discovered in neurons. This enzyme and splice variants thereof have since been found in many other cells and tissues. NOS II (NOS2, iNOS) was first identified in murine macrophages, but can also be induced in many other cell types. NOS III (NOS3, ecNOS) is expressed mainly in endothelial cells. Whereas NOS II is a transcriptionally regulated enzyme, NOS I and NOS III are considered constitutively expressed proteins. However, evidence generated in recent years indicates that these two isoforms are also subject to expressional regulation. In view of the important biological functions of these …

LipopolysaccharidesGene isoformNitric Oxide Synthase Type IIITranscription GeneticNOS1Nitric Oxide Synthase Type IBiochemistryTranscription (biology)GeneticsTranscriptional regulationAnimalsHumansRNA MessengerGrowth SubstancesMolecular BiologyTranscription factorRegulation of gene expressionPolymorphism GeneticbiologyChemistryChromosome MappingLysophosphatidylcholinesNitric Oxide Synthase Type IIIEstrogensExonsCell biologyIsoenzymesLipoproteins LDLOxygenNitric oxide synthaseGene Expression Regulationbiology.proteinCytokinesNitric Oxide SynthaseGene DeletionBiotechnologyThe FASEB Journal
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Solid-phase synthesis and inhibitory effects of some pyrido[1,2-c]pyrimidine derivatives on leukocyte formations and experimental inflammation.

2001

A number of pyrido[1,2-c]pyrimidines bearing a nitrogen, oxygen, or sulfur functionality at C-1 were synthesized on solid-phase using the iminophosphorane methodology and tested for their effects on leukocyte functions in vitro and antiinflammatory activity. Compound 5c was found to be a strong scavenger of superoxide anion and an inhibitor of chemiluminescence induced by 12-O-tetradecanoylphorbol 13-acetate in human neutrophils. These pyrido[1,2-c]pyrimidines inhibited the generation of PGE(2) by COX-2 in RAW 264.7 macrophages stimulated with lipopolysaccharide. Compounds 7, 5f, 6, and 8 inhibited enzyme activity, whereas the remaining compounds also acted on the induction phase. In additi…

LipopolysaccharidesLipopolysaccharideNeutrophilsChemical synthesisDinoprostoneNeutrophil Activationchemistry.chemical_compoundMiceStructure-Activity RelationshipDrug DiscoveryAnimalsEdemaHumansCells CulturedbiologyPancreatic ElastaseSuperoxideMacrophagesAnti-Inflammatory Agents Non-SteroidalMembrane ProteinsBiological activityFree Radical ScavengersIn vitroEnzyme assayCarrageenanIsoenzymesPyrimidineschemistryEicosanoidBiochemistryCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesLuminescent Measurementsbiology.proteinMolecular MedicineTetradecanoylphorbol AcetateJournal of medicinal chemistry
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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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ttCH, a selective inhibitor of inducible nitric oxide synthase expression with antiarthritic properties

2003

In a previous work, we investigated the effects of a series of dimethoxy- and trimethoxychalcone derivatives, with various patterns of fluorination, on nitric oxide production in lipopolysaccharide-stimulated murine RAW 264.7 cells. The present study was designed to determine if 2,4,6-trimethoxy-2'-trifluoromethylchalcone (ttCH) could modulate the production of nitric oxide (NO) and/or prostaglandins in vitro and in vivo. On the mouse macrophage cell line RAW 264.7, ttCH inhibited dose-dependently NO and prostaglandin E(2) production, with IC(50) in the micromolar range. This compound had no direct inhibitory effect on inducible nitric oxide synthase (iNOS) and cyclooxygenase-2 activities. …

LipopolysaccharidesMalemedicine.medical_treatmentBlotting WesternNitric Oxide Synthase Type IIPharmacologyCarrageenanNitric OxideDinoprostoneCell LineNitric oxideMicechemistry.chemical_compoundIn vivomedicineAnimalsEdemaEnzyme InhibitorsProstaglandin E2InflammationPharmacologybiologyChemistryMacrophagesAnti-Inflammatory Agents Non-SteroidalBiological activityArthritis ExperimentalHindlimbRatsCarrageenanIsoenzymesRadiographyNitric oxide synthaseMechanism of actionBiochemistryCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesRats Inbred Lewbiology.proteinFemaleNitric Oxide Synthasemedicine.symptomProstaglandin Emedicine.drugEuropean Journal of Pharmacology
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Reduced mRNA abundance of the main enzymes involved in methionine metabolism in human liver cirrhosis and hepatocellular carcinoma

2000

Abstract Background/Aims: It has been known for at least 50 years that alterations in methionine metabolism occur in human liver cirrhosis. However, the molecular basis of this alteration is not completely understood. In order to gain more insight into the mechanisms behind this condition, mRNA levels of methionine adenosyltransferase ( MAT1A ), glycine methyltransferase ( GNMT ), methionine synthase ( MS ), betaine homocysteine methyltransferase ( BHMT ) and cystathionine β-synthase ( CBS ) were examined in 26 cirrhotic livers, five hepatocellular carcinoma (HCC) tissues and ten control livers. Methods: The expression of the above-mentioned genes was determined by quantitative RT-PCR analy…

Liver Cirrhosismedicine.medical_specialtyCarcinoma HepatocellularMethyltransferaseBetaine—homocysteine S-methyltransferaseMethylationHepatocarcinemachemistry.chemical_compoundMethionineInternal medicinemedicineHumansRNA MessengerMethionine synthasePromoter Regions GeneticDNA methylationMethionineHepatologybiologyLiver NeoplasmsMethionine Adenosyltransferasemedicine.diseaseCystathionine beta synthaseEnzymesIsoenzymesEndocrinologyCirrhosisLiverchemistryMethionine AdenosyltransferaseGNMTbiology.proteinHypermethioninemia
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