Search results for "ACETATE"

showing 10 items of 756 documents

Anti-inflammatory activity of berenjenol and related compounds.

2008

Berenjenol ( 1), isolated from OXANDRA cf. XYLOPIOIDES (Annonaceae), was tested on two different experimental models of inflammation. The compound showed anti-inflammatory activity in the test of acute mouse ear edema induced by TPA (54 % inhibition, 1 μmol/ear) as well as in the test of subchronic inflammation induced by repeated application of TPA (57 % inhibition, 7 × 1 μmol/ear). Moreover, while it reduced the expression of both COX-2 (65 % inhibition at 50 μM) and iNOS (80 % inhibition at 50 μM), it was not active against TNF- α and IL-1 β in murine macrophages (RAW 264.7) stimulated with LPS. Structural modification of 1 gave two derivatives, berenjenol acetate ( 2) and 3-oxo-berenjen…

Lipopolysaccharidemedicine.drug_classInterleukin-1betaAnti-Inflammatory AgentsPharmaceutical ScienceAnnonaceaeGene ExpressionNitric Oxide Synthase Type IIPharmacologyAnti-inflammatoryAnalytical Chemistrychemistry.chemical_compoundMiceDrug DiscoverymedicineAnimalsEdemaProtein kinase CPharmacologybiologyDimethyl sulfoxideTumor Necrosis Factor-alphaMacrophagesOrganic ChemistryTriterpenesNitric oxide synthaseComplementary and alternative medicinechemistryBiochemistryCyclooxygenase 2biology.proteinMolecular MedicineTetradecanoylphorbol AcetateTumor necrosis factor alphaFemaleCyclooxygenaseFetal bovine serumPlanta medica
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Modulation of protein tyrosine nitration and inflammatory mediators by isoprenylhydroquinone glucoside.

2007

The nitration of tyrosine caused by peroxynitrite and other reactive nitrogen species is clearly detrimental for some physiological processes; however, its signalling role is still open to controversy. Among the natural phenolics known for their ability to oppose free tyrosine nitration, isoprenylhydroquinone glucoside is investigated due to its unusual structure, which contains a simple hydroxybenzene alkylated by a hemiterpenoid moiety. This hydroquinone was shown to be an effective inhibitor of peroxynitrite-induced protein tyrosine nitration in 3T3 fibroblasts. When tested on bovine seroalbumin nitration, however, the potency was reduced by half and the effect was almost abolished in th…

LipopolysaccharidesCell SurvivalNeutrophilsBlotting WesternInterleukin-1betaPharmaceutical ScienceNitric Oxide Synthase Type IIHemeNitric oxidechemistry.chemical_compoundMiceGlucosideGlucosidesNitrationPeroxynitrous AcidAnimalsHumansTyrosineReactive nitrogen speciesCells CulturedNitritesNitratesbiologyCell-Free SystemReverse Transcriptase Polymerase Chain ReactionRhodaminesTumor Necrosis Factor-alphaNitrotyrosineSerum Albumin Bovine3T3 CellsHydrogen PeroxideFibroblastsStimulation ChemicalHydroquinonesNitric oxide synthasechemistryBiochemistrybiology.proteinTetradecanoylphorbol AcetateTyrosineInflammation MediatorsPeroxynitriteEuropean journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences
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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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Interaction of dicaffeoylquinic derivatives with peroxynitrite and other reactive nitrogen species.

2008

Plant phenolic antioxidants, among them catechins and hydroxycinnamoyl conjugates, constitute a well defined class of inhibitors of reactive nitrogen species (RNS). To gain deeper insight in this field, we examined the effects of 3,5-di-O-caffeoylquinic acid (DCA), its methyl ester (DCE) and epigallocatechin gallate (EGCG) in nitrative and oxidative processes. These compounds were found to be strong inhibitors of the nitration of tyrosine residues induced by ONOO- in bovine seroalbumin, with their IC50 values (10-40 microM) notably decreasing in the presence of bicarbonate. When studied on the intracellular protein tyrosine nitration induced by ONOO- in cultured murine fibroblasts as well a…

LipopolysaccharidesNeutrophilsBicarbonateBiophysicsQuinic AcidNitric Oxide Synthase Type IIEpigallocatechin gallateBiochemistryCatechinNitric oxidechemistry.chemical_compoundInhibitory Concentration 50MiceNitrationPeroxynitrous AcidAnimalsHumansTyrosineMolecular BiologyReactive nitrogen speciesNitritesNitratesNitrotyrosineMacrophagesSerum Albumin BovineFibroblastsReactive Nitrogen SpeciesStimulation ChemicalBicarbonateschemistryBiochemistryTetradecanoylphorbol AcetateTyrosineCattleOxidation-ReductionPeroxynitriteArchives of biochemistry and biophysics
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Rho protein inhibition blocks protein kinase C translocation and activation.

1998

Small GTP-binding proteins of the Ras and Rho family participate in various important signalling pathways. Large clostridial cytotoxins inactivate GTPases by UDP-glucosylation. Using Clostridium difficile toxin B-10463 (TcdB) for inactivation of Rho proteins (RhoA/Rac/Cdc42) and Clostridium sordellii lethal toxin-1522 (TcsL) for inactivation of Ras-proteins (Ras/Rac/Ral, Rap) the role of these GTPases in protein kinase C (PKC) stimulation was studied. Phorbol-myristate-acetate (PMA) induced a rapid PKC translocation to and activation in the particulate cell fraction as determined by PKC-activity measurements and Western blots for PKC alpha. These effects were blocked by TcdB inhibiting Rho …

LipopolysaccharidesRHOASwineBiophysicsClostridium difficile toxin ABronchiCell Cycle ProteinsGTPaseCDC42PKC alphaBiochemistryGTP-Binding ProteinsRHO protein GDP dissociation inhibitorAnimalsHumanscdc42 GTP-Binding ProteinMolecular BiologyProtein kinase CCells CulturedProtein Kinase CbiologyEpithelial CellsCell BiologyMolecular biologyCell biologyEnzyme ActivationCdc42 GTP-Binding Proteinbiology.proteinras ProteinsTetradecanoylphorbol AcetateEndothelium VascularrhoA GTP-Binding ProteinBiochemical and biophysical research communications
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Application of X-ray microanalysis to study of the expression of endothelial adhesion molecules on human umbilical vein endothelial cells in vitro

1994

A semi-quantitative procedure is described, which allows the evaluation of expression levels of endothelial adhesion molecules on cultured human umbilical vein endothelial cells (HUVEC) using energy dispersive X-ray microanalysis (EDX). As a model two adhesion molecules, E-selection (CD62E; ELAM-1/endothelial leukocyte adhesion molecule-1) and ICAM-1 (intercellular adhesion molecule-1; CD54), were localized by the use of the silver-enhancement colloidal gold method after stimulation of HUVEC with endotoxin lipopolysaccharide (LPS), tumour necrosis factor (TNF) or a phorbol ester (PMA). The analysis was performed in a scanning electron microscope (SEM) at an accelerating voltage of 15 kV wit…

LipopolysaccharidesUmbilical VeinsHistologyEndotheliumEnzyme-Linked Immunosorbent AssayIn Vitro TechniquesUmbilical veinE-selectinmedicineHumansMolecular BiologyCells CulturedbiologyTumor Necrosis Factor-alphaChemistryCell adhesion moleculeCell BiologyGeneral MedicineImmunogold labellingAdhesionIntercellular Adhesion Molecule-1ImmunohistochemistryMolecular biologyStimulation ChemicalIn vitroMedical Laboratory Technologymedicine.anatomical_structurebiology.proteinTetradecanoylphorbol AcetateTumor necrosis factor alphaEndothelium VascularAnatomyE-SelectinGeneral Agricultural and Biological SciencesCell Adhesion MoleculesElectron Probe MicroanalysisHistochemistry
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Does glatiramer acetate provoke hepatitis in multiple sclerosis?

2012

Abstract An association between multiple sclerosis and autoimmune hepatitis has been described. The latter can also be unmasked or exacerbated by a variety of therapies used in multiple sclerosis, such as beta-Interferon or glatiramer acetate. Two cases of hepatitis occurring after exposure to glatiramer acetate are described here: the first, was possibly due to autoimmune hepatitis, rather than glatiramer acetate induced liver injury, the second was definite autoimmune hepatitis. Both occurred in patients who had already experienced hepatitis exacerbations during previous beta-Interferon treatment. We suggest that glatiramer acetate can unmask hepatitis. Thus, liver enzyme monitoring shoul…

Liver injuryHepatitisbusiness.industryMultiple sclerosisGeneral MedicineAutoimmune hepatitismedicine.diseaseNeurologyInterferonLiver enzymeImmunologyMedicineIn patientNeurology (clinical)Glatiramer acetatebusinessmedicine.drugMultiple Sclerosis and Related Disorders
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Coupling of Contact Sensitizers to Thiol Groups is a Key Event for the Activation of Monocytes and Monocyte-Derived Dendritic Cells

2003

Strong contact sensitizers are able to induce distinct signal transduction mechanisms in antigen-presenting cells by coupling to cell proteins. The predominant target structures of haptens are thought to be thiol and amino groups in cysteine and lysine residues. We studied whether coupling of small reactive chemicals to thiol or amino groups might be responsible for the activation of monocytes and mature monocyte-derived dendritic cells. Human peripheral blood mononuclear cells were stimulated in vitro with subtoxic concentrations of the strong haptens 5-chloro-2-methylisothiazolinone plus 2-methylisothiazolinone and 2, 4, 6-trinitrochlorobenzene, the thiol-reactive reagents N-hydroxymaleim…

MAP Kinase Signaling SystemCD14SuccinimidesPicryl ChlorideDermatologyAcetatesPeripheral blood mononuclear cellBiochemistryamino groupsAntioxidantsMonocytesMaleimideschemistry.chemical_compoundAnti-Infective AgentsmedicineHumansCysteineSulfhydryl CompoundsPhosphorylationAntigen-presenting cellMolecular Biologythiol groupsChemistryMonocyteLysineSulfhydryl ReagentsTyrosine phosphorylationDendritic cellDendritic CellsCell BiologyThiazolesmedicine.anatomical_structureBiochemistryEthylmaleimidehaptenTyrosineSignal transductionsignal transductionCysteineInterleukin-1Journal of Investigative Dermatology
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Eicosapentaenoic acid and docosahexaenoic acid modulate MAP kinase (ERK1/ERK2) signaling in human T cells

2001

This study was conducted on human Jurkat T cell lines to elucidate the role of EPA and DHA, n-3 PUFA, in the modulation of two mitogen-activated protein (MAP) kinases, that is, extracellular signal-regulated kinases 1 and 2 (ERK1 and ERK2). The n-3 PUFA alone failed to induce phosphorylation of ERK1/ERK2. We stimulated the MAP kinase pathway with anti-CD3 antibodies and phorbol 12-myristate 13-acetate (PMA), which act upstream of the MAP kinase (MAPK)/ERK kinase (MEK) as U0126, an MEK inhibitor, abolished the actions of these two agents on MAP kinase activation. EPA and DHA diminished the PMA- and anti-CD3-induced phosphorylation of ERK1/ERK2 in Jurkat T cells. In the present study, PMA act…

MAPK/ERK pathwayCD3 ComplexDocosahexaenoic AcidsMAP Kinase Signaling SystemT-LymphocytesQD415-436Arachidonic AcidsLymphocyte Activationfatty acidsBiochemistryJurkat cellsAntibodiesJurkat Cellschemistry.chemical_compoundEndocrinologyHumansPhosphorylationProtein Kinase CProtein kinase CMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3MAP kinase kinase kinasebiologyKinaseIonomycinfood and beveragesCell BiologyCell biologyEnzyme ActivationBiochemistrychemistryMitogen-activated protein kinasebiology.proteinPhorbolTetradecanoylphorbol AcetatePhosphorylationlipids (amino acids peptides and proteins)T cell receptorMitogen-Activated Protein KinasesJournal of Lipid Research
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p42 MAPK phosphorylates 80 kDa MARCKS at Ser-113.

1996

Abstract It is demonstrated here that p42 MAPKinase (p42 MAPK) phosphorylates the M yristoylated A lanine- R ich C - K inase S ubstrate (MARCKS) at Ser-113. In permeabilised Swiss 3T3 cells activation of protein kinase C (PKC) leads to p42 MAPK activation, but only the protein kinase C sites in MARCKS become phosphorylated and not Ser-113. The mitogen platelet-derived growth factor (PDGF) elicits the same response. These results demonstrate that while Ser-113 is a substrate for p42 MAPK in vitro and can be phosphorylated in vivo as shown by Taniguchi et al. [(1994) J. Biol. Chem. 269, 18299–18302], its phosphorylation is not subject to acute regulation by p42 MAPK in Swiss 3T3 cells.

MAPK/ERK pathwayMARCKSmedicine.medical_treatmentMitogen-activated protein kinase kinaseBiochemistryenvironment and public healthSubstrate SpecificityMiceStructural BiologySerinep42MAPKinasePhosphorylationMyristoylated Alanine-Rich C Kinase SubstrateCells CulturedProtein Kinase CMitogen-Activated Protein Kinase 1Platelet-Derived Growth FactorbiologyChemistryIntracellular Signaling Peptides and Proteins3T3 CellsProtein-Tyrosine KinasesCell biologyBiochemistryMitogen-activated protein kinasePhosphorylationTetradecanoylphorbol Acetatebiological phenomena cell phenomena and immunityPlatelet-derived growth factor receptorhormones hormone substitutes and hormone antagonistsendocrine systemRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsGeneticsmedicineAnimalsAmino Acid SequenceMARCKSMolecular BiologyProtein kinase CGrowth factorMembrane ProteinsProteinsCell BiologyPeptide FragmentsEnzyme ActivationMolecular Weightenzymes and coenzymes (carbohydrates)Calcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedMitogensFEBS letters
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