Search results for "Prostacyclin synthase"

showing 7 items of 7 documents

Extracellular histones disarrange vasoactive mediators reléase through COX-NOS interaction in human endothelial cells

2017

Abstract Extracellular histones are mediators of inflammation, tissue injury and organ dysfunction. Interactions between circulating histones and vascular endothelial cells are key events in histone‐mediated pathologies. Our aim was to investigate the implication of extracellular histones in the production of the major vasoactive compounds released by human endothelial cells (HUVECs), prostanoids and nitric oxide (NO). HUVEC exposed to increasing concentrations of histones (0.001 to 100 μg/ml) for 4 hrs induced prostacyclin (PGI2) production in a dose‐dependent manner and decreased thromboxane A2 (TXA2) release at 100 μg/ml. Extracellular histones raised cyclooxygenase‐2 (COX‐2) and prostac…

0301 basic medicineProstacyclinHistoneschemistry.chemical_compoundThromboxane A2Cytochrome P-450 Enzyme SystemSuperoxidesEnosvascular mediatorsGenètica humanabiologySuperoxideendothelial cellsIntramolecular OxidoreductasesEndothelial stem cellMolecular MedicineOriginal ArticleThromboxane-A SynthaseSignal Transductionmedicine.drugmedicine.medical_specialtyNitric Oxide Synthase Type IIIPrimary Cell CultureNitric OxideProstacyclin synthaseNitric oxideCyclic N-OxidesThromboxane A203 medical and health sciencesInternal medicineHuman Umbilical Vein Endothelial CellsmedicineExtracellularHumansRNA MessengerprostanoidsDose-Response Relationship DrugOriginal ArticlesCell Biologybiology.organism_classificationEpoprostenolÒxid nítric030104 developmental biologyEndocrinologyGene Expression RegulationchemistryCelecoxibCyclooxygenase 2Cyclooxygenase 1biology.proteinSpin LabelsProteïnesextracellular histones
researchProduct

Mitochondrial aldehyde dehydrogenase (ALDH-2)--maker of and marker for nitrate tolerance in response to nitroglycerin treatment.

2008

The hemodynamic and anti-ischemic effects of nitroglycerin (GTN) are rapidly blunted as a result of the development of nitrate tolerance. Long-term nitrate treatment also is associated with decreased vascular responsiveness caused by changes in intrinsic mechanisms of the tolerant vasculature itself. According to the oxidative stress concept, increased vascular superoxide and peroxynitrite production as well as an increased sensitivity to vasoconstrictors secondary to activation of protein kinase C as well as vascular NADPH oxidases contribute to the development of tolerance. Recent experimental work has defined new tolerance mechanisms, including inhibition of the enzyme that bioactivates …

Aldehyde dehydrogenasePharmacologyToxicologymedicine.disease_causeProstacyclin synthasechemistry.chemical_compoundNitroglycerinDrug tolerancemedicineHumansEndothelial dysfunctionchemistry.chemical_classificationReactive oxygen speciesNitratesbiologyAldehyde Dehydrogenase MitochondrialGeneral MedicineDrug ToleranceAldehyde Dehydrogenasemedicine.diseaseMitochondriaOxidative StresschemistryBiochemistrycardiovascular systembiology.proteinSoluble guanylyl cyclasePeroxynitriteOxidative stresscirculatory and respiratory physiologyChemico-biological interactions
researchProduct

Increased Circulating Levels of 3-Nitrotyrosine Autoantibodies

2012

3-nitrotyrosine formation is an oxidative protein modification that was first discovered in vivo in the early 1990s by Beckman and colleagues.1,2 The biological relevance of this process was extensively investigated in the subsequent years and further facilitated by the development of 3-nitrotyrosine–specific antibodies.3 Protein tyrosine nitration is mainly mediated by 3 biochemical processes (Figure): (1) by peroxynitrite (ONOO−) formation,4–6 the reaction product of nitric oxide (•NO) and superoxide (•O2−); (2) by a (myelo)peroxidase-catalyzed nitrogen dioxide radical (•NO2) formation from hydrogen peroxide and nitrite;7,8 and (3) by a nonspecific formation of the nitrogen dioxide radica…

MaleImmunoglobulinsProstacyclinCoronary Artery DiseasePharmacologyArticleProstacyclin synthaseNitric oxideEpitopeschemistry.chemical_compoundPhysiology (medical)medicineHumansbiologySuperoxidebusiness.industryNitric Oxide Synthase Type IIIPeroxynitrous acidchemistryBiochemistryMyeloperoxidasebiology.proteinTyrosineFemaleCardiology and Cardiovascular MedicinebusinessPeroxynitritemedicine.drugCirculation
researchProduct

Characterization of monoclonal antibodies generated against bovine and porcine prostacyclin synthase and quantitation of bovine prostacyclin synthase

1994

AbstractMonoclonal antibodies were raised against prostacyclin synthases purified from bovine and porcine aortae, respectively. Two monoclonal antibodies, RS1 and RS2, were purified and characterized. As shown by enzyme activity precipitation and Western blot analysis, in solubilized bovine and porcine aortae microsomes the monoclonal antibodies reacted only with prostacyclin synthase. The monoclonal antibody RS1 cross-reacts with partially purified prostacyclin synthase from human umbilical veins in an ELISA-based assay. None of the antibodies inhibited the enzyme activity. By combination of the monoclonal antibody RS2 with a polyclonal antibody we established an enzyme-linked immunosorben…

Monoclonal antibodyUmbilical VeinsSwinemedicine.drug_classProstaglandinBlotting WesternBiophysicsProstaglandinEnzyme-Linked Immunosorbent AssayProstacyclinMonoclonal antibodySensitivity and SpecificityBiochemistryProstacyclin synthasechemistry.chemical_compoundCytochrome P-450 Enzyme SystemWestern blotAntibody SpecificityStructural BiologyMicrosomesGeneticsmedicineAnimalsHumansTissue DistributionIsomerasesMolecular BiologyAortaImmunosorbent Techniquesbiologymedicine.diagnostic_testAntibodies MonoclonalCell BiologyMolecular biologyImmunohistochemistryIntramolecular OxidoreductasesBiochemistrychemistryPolyclonal antibodiesImmunoquantitationProstacyclin synthasebiology.proteinImmunohistochemistryCattleAntibodymedicine.drugFEBS Letters
researchProduct

Explaining the phenomenon of nitrate tolerance.

2005

During the last century, nitroglycerin has been the most commonly used antiischemic and antianginal agent. Unfortunately, after continuous application, its therapeutic efficacy rapidly vanishes. Neurohormonal activation of vasoconstrictor signals and intravascular volume expansion constitute early counter-regulatory responses (pseudotolerance), whereas long-term treatment induces intrinsic vascular changes, eg, a loss of nitrovasodilator-responsiveness (vascular tolerance). This is caused by increased vascular superoxide production and a supersensitivity to vasoconstrictors secondary to a tonic activation of protein kinase C. NADPH oxidase(s) and uncoupled endothelial nitric oxide synthase …

PhysiologyVasodilator AgentsPharmacologymedicine.disease_causeNitric OxideProstacyclin synthaseNitric oxidechemistry.chemical_compoundNitroglycerinSuperoxidesPeroxynitrous AcidmedicineCyclic GMP-Dependent Protein KinasesAnimalsHumansBiotransformationchemistry.chemical_classificationReactive oxygen speciesNADPH oxidasebiologyChemistrySuperoxidePhosphoric Diester HydrolasesAldehyde Dehydrogenase MitochondrialDrug ToleranceAldehyde DehydrogenaseCyclic Nucleotide Phosphodiesterases Type 1VasodilationOxidative StressBiochemistryVasoconstrictioncardiovascular systembiology.proteinEndothelium VascularCardiology and Cardiovascular MedicineSoluble guanylyl cyclaseReactive Oxygen SpeciesPeroxynitriteOxidative stressSignal TransductionCirculation research
researchProduct

Progestogens reduce thromboxane production by cultured human endothelial cells.

2011

Objectives Progestogens have been poorly studied concerning their roles in endothelial physiology. Prostanoids are vasoactive compounds, such as thromboxane A2, a potent vasoconstrictor, and prostacyclin, a vasodilator. We examined the effects of two progestogens used clinically, progesterone and medroxyprogesterone acetate, on thromboxane A2 production by cultured human umbilical vein endothelial cells (HUVEC) and investigated the role of progesterone receptors and the enzymes involved in production of thromboxane A2 and prostacyclin. Methods Cells were exposed to 1‐100 nmol/l of either progesterone or medroxyprogesterone acetate, and thromboxane A2 production was measured in culture mediu…

medicine.medical_specialtyUmbilical VeinsAntineoplastic Agents HormonalThromboxaneBlotting WesternGene ExpressionProstacyclinMedroxyprogesterone AcetatePolymerase Chain ReactionProstacyclin synthaseThromboxane receptorThromboxane ProductionThromboxane A2chemistry.chemical_compoundThromboxane A2Hormone AntagonistsCytochrome P-450 Enzyme SystemInternal medicineProgesterone receptorMedicineHumansCyclooxygenase InhibitorsRNA MessengerCells CulturedProgesteronebiologyDose-Response Relationship Drugbusiness.industryObstetrics and GynecologyEndothelial CellsGeneral MedicineIntramolecular OxidoreductasesThromboxane B2MifepristoneEndocrinologychemistrycardiovascular systembiology.proteinPyrazolesThromboxane-A synthaseThromboxane-A SynthaseProgestinsbusinessmedicine.drugClimacteric : the journal of the International Menopause Society
researchProduct

Protein tyrosine nitration and thiol oxidation by peroxynitrite-strategies to prevent these oxidative modifications.

2013

The reaction product of nitric oxide and superoxide, peroxynitrite, is a potent biological oxidant. The most important oxidative protein modifications described for peroxynitrite are cysteine-thiol oxidation and tyrosine nitration. We have previously demonstrated that intrinsic heme-thiolate (P450)-dependent enzymatic catalysis increases the nitration of tyrosine 430 in prostacyclin synthase and results in loss of activity which contributes to endothelial dysfunction. We here report the sensitive peroxynitrite-dependent nitration of an over-expressed and partially purified human prostacyclin synthase (3.3 μM) with an EC50 value of 5 μM. Microsomal thiols in these preparations effectively co…

thiol oxidationprotein tyrosine nitrationlcsh:Chemistrychemistry.chemical_compoundCytochrome P-450 Enzyme SystemSf9 CellsTyrosinelcsh:QH301-705.5Spectroscopychemistry.chemical_classification0303 health sciencesbiologySuperoxide030302 biochemistry & molecular biologyGeneral MedicineComputer Science ApplicationsIntramolecular OxidoreductasesBiochemistryThiolprostacyclin synthasesuperoxideOxidation-ReductionPeroxynitriteOxidative phosphorylationSpodopteraCatalysisArticleperoxynitriteNitric oxideProstacyclin synthaseInorganic Chemistry03 medical and health sciencesnitric oxideddc:570NitrationPeroxynitrous AcidAnimalsHumansSulfhydryl CompoundsPhysical and Theoretical ChemistryMolecular Biology030304 developmental biologyOrganic Chemistrynitric oxide; superoxide; peroxynitrite; protein tyrosine nitration; thiol oxidation; peroxynitrite scavengers; prostacyclin synthasechemistrylcsh:Biology (General)lcsh:QD1-999biology.proteinTyrosineCattleperoxynitrite scavengersProtein Processing Post-TranslationalInternational journal of molecular sciences
researchProduct