Search results for "isoenzymes"

showing 10 items of 244 documents

Ethanol cycle in an ethanologenic bacterium

2002

AbstractA novel redox cycle is suggested, performing interconversion between acetaldehyde and ethanol in aerobically growing ethanologenic bacterium Zymomonas mobilis. It is formed by the two alcohol dehydrogenase (ADH) isoenzymes simultaneously catalyzing opposite reactions. ADH I is catalyzing acetaldehyde reduction. The local reactant ratio at its active site probably is shifted towards ethanol synthesis due to direct channeling of NADH from glycolysis. ADH II is oxidizing ethanol. The net result of the cycle operation is NADH shuttling from glycolysis to the membrane respiratory chain, and ensuring flexible distribution of reducing equivalents between the ADH reaction and respiration.

NADH channelingBiophysicsRespiratory chainBiochemistryZymomonas mobilischemistry.chemical_compoundStructural BiologyGeneticsGlycolysisEthanol metabolismMolecular BiologyAlcohol dehydrogenaseZymomonasEthanolEthanolbiologyFutile cycleRespirationZymomonas mobilisAlcohol dehydrogenaseAcetaldehydeCell BiologyNADbiology.organism_classificationAerobiosisIsoenzymeschemistryBiochemistryFutile cycleChemostatbiology.proteinOxidation-Reductionhormones hormone substitutes and hormone antagonistsFEBS Letters
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Cycloamphilectenes, a new type of potent marine diterpenes: inhibition of nitric oxide production in murine macrophages.

2003

The inhibitory effect of a series of 6 cycloamphilectenes, novel marine diterpenes based on amphilectene skeletons and isolated from the Vanuatu sponge Axinella sp., on NO, PGE(2) and TNFalpha production in murine peritoneal macrophages was studied. These compounds reduced potently nitric oxide production in a concentration-dependent manner with IC(50) values in the submicromolar range (0.1-4.3 microM). Studies on intact cells and Western blot analysis showed that the more potent cycloamphilectenes reduced the expression of inducible nitric oxide synthase without affecting cyclo-oxygenase-2 expression. Among them cycloamphilectene 2, the unique compound bearing an exocyclic methylene group,…

NeutrophilsBlotting WesternNitric Oxide Synthase Type IIElectrophoretic Mobility Shift AssayIn Vitro TechniquesNitric OxideGeneral Biochemistry Genetics and Molecular BiologyDinoprostoneNitric oxidechemistry.chemical_compoundMiceStructure-Activity RelationshipWestern blotmedicineAnimalsEdemaHumansGeneral Pharmacology Toxicology and PharmaceuticsMethylenebiologymedicine.diagnostic_testPancreatic ElastaseTumor Necrosis Factor-alphaMacrophagesZymosanAnti-Inflammatory Agents Non-SteroidalAxinellaNF-kappa BMembrane ProteinsGeneral Medicinebiology.organism_classificationPoriferaNitric oxide synthaseIsoenzymesSpongechemistryBiochemistryCyclooxygenase 2Prostaglandin-Endoperoxide Synthasesbiology.proteinMacrophages PeritonealTumor necrosis factor alphaFemaleMarine ToxinsDiterpenesNitric Oxide SynthaseLife sciences
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Inhibition of 5-lipoxygenase activity by the natural anti-inflammatory compound aethiopinone

2001

Objetive and Design: We have investigated the mechanisms of action of aethiopinone, an anti-inflammatory compound from Salvia aethiopis L. roots.¶Material and Subjects: Human neutrophils from healthy volunteers and murine peritoneal macrophages. Swiss mice were randomly divided into groups of six animals.¶Treatment: Test compounds were applied topically in the mouse ear oedema test. In the air pouch, mice received aethiopinone (0.001-0.5 μmol/pouch or 12.5-50 mg/kg p.o.).¶Methods: LTB4 production was assayed in human neutrophils and COX-2 and iNOS activities in murine macrophages. Air pouches were induced subcutaneously in mice and injected with zymosan on the day six. Mouse ear oedema was …

Neutrophilsmedicine.drug_classImmunologyNitric Oxide Synthase Type IIPharmacologyLeukotriene B4DinoprostonePhospholipases AAnti-inflammatoryMicechemistry.chemical_compoundIn vivoAnimalsEdemaHumansMedicineLipoxygenase InhibitorsIC50InflammationPharmacologyArachidonic Acidbiologybusiness.industryAnti-Inflammatory Agents Non-SteroidalZymosanMembrane ProteinsEarbiology.organism_classificationIn vitroIsoenzymeschemistryCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesArachidonate 5-lipoxygenaseImmunologyCyclooxygenase 1Macrophages PeritonealSalvia aethiopisbiology.proteinArachidonic acidNitric Oxide SynthasebusinessNaphthoquinonesInflammation Research
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Dysidotronic acid, a new sesquiterpenoid, inhibits cytokine production and the expression of nitric oxide synthase.

2001

In a previous study, we reported a new bioactive sesquiterpenoid, named dysidotronic acid, to be a potent, selective human synovial phospholipase A(2) inhibitor. Dysidotronic acid is a novel, non-complex manoalide analogue lacking the pyranofuranone ring. We now investigate the effect of this compound on cytokine, nitric oxide and prostanoid generation on the mouse macrophage cell line RAW 264.7, where it showed a dose-dependent inhibition with inhibitory concentration 50% values in the micromolar range. This effect was also confirmed in the mouse air pouch injected with zymosan. Dysidotronic acid inhibited the production of tumor necrosis factor alpha and interleukin-1 beta as well as the …

Nitric oxide (NO)MouseLeukotriene B4NeutrophilsRAW 264.7Dysidotronic acidNitric Oxide Synthase Type IIDinoprostonePhospholipases ANitric oxideCell Linechemistry.chemical_compoundManoalideMicemedicineAnimalsHumansProstaglandin E2Enzyme InhibitorsCytokineNitritesPharmacologybiologyTumor Necrosis Factor-alphaMacrophagesZymosanZymosanMembrane ProteinsNitric oxide synthaseIsoenzymesAir pouchchemistryBiochemistryEnzyme inhibitorCyclooxygenase 2Prostaglandin-Endoperoxide Synthasesbiology.proteinCytokinesArachidonic acidDiterpenesNitric Oxide SynthaseSesquiterpenesmedicine.drugEuropean journal of pharmacology
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Effects of fenspiride on human bronchial cyclic nucleotide phosphodiesterase isoenzymes: functional and biochemical study.

1998

We have investigated the role of human bronchial cyclic nucleotide phosphodiesterases in the effects of fenspiride, a drug endowed with bronchodilator and anti-inflammatory properties. Functional studies on human isolated bronchi showed that fenspiride (10(-6)-3 x 10(-3) M, 30 min) induced a shift to the left of the concentration-response curves for isoprenaline and sodium nitroprusside with -logEC50 values of 4.1+/-0.1 (n = 7) and 3.5+/-0.2 (n = 8), respectively. Biochemical studies were carried out on three human bronchi in which separation of cyclic nucleotide phosphodiesterase isoenzymes was performed by ion exchange chromatography followed by determination of phosphodiesterase activity…

NitroprussideMuscle RelaxationVasodilator AgentsPhosphodiesterase 3FenspirideBronchimedicineHumansSpiro CompoundsPharmacologyCyclic nucleotide phosphodiesterasebiologyDose-Response Relationship DrugChemistryIsoproterenolPhosphodiesteraseBronchodilator AgentsIsoenzymesBiochemistryEnzyme inhibitor3'5'-Cyclic-AMP PhosphodiesterasescGMP-specific phosphodiesterase type 5biology.proteinPhosphodiesterase 2Sodium nitroprussidemedicine.drugMuscle ContractionEuropean journal of pharmacology
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Pharmacological and biochemical study on the effects of selective phosphodiesterase inhibitors on human term myometrium

1999

This study was aimed at evaluating the in vitro effects of phosphodiesterase inhibitors and beta2-adrenoceptor agonists on spontaneous contractions of human term myometrium. Rolipram, RP 73401 (3-cyclopentyloxy-N-(3,5(-dichloro-4-pyridil)-4-methoxybenzamide) and Ro 20-1724 (1-4-(3-butoxy-4-methoxybenzyl)-2-imidozolidinone) (phosphodiesterase 4 inhibitors) inhibited spontaneous myometrial contractions (Emax approximately 100%; pD2 of 6.80+/-0.28, 6.84+/-0.32 and 6.31+/-0.03, respectively). Salbutamol and formoterol were less effective (Emax=40+/-6% and 35+/-12%, respectively) than phosphodiesterase 4 inhibitors to reduce myometrial contractility. Inhibitors of phosphodiesterase 3 (milrinone …

Nitroprussidemedicine.medical_specialtyTocolytic agentPhosphodiesterase InhibitorsSiguazodanPhosphodiesterase 3In Vitro Techniqueschemistry.chemical_compoundPregnancyInternal medicinemedicineHumansDrug InteractionsRolipramPharmacologyChromatographyDose-Response Relationship DrugPhosphoric Diester HydrolasesPhosphodiesteraseGeneral MedicineAdrenergic beta-AgonistsIsoenzymesEndocrinologychemistryMyometriumMilrinoneFemaleSodium nitroprussideZaprinastmedicine.drugNaunyn-Schmiedeberg's Archives of Pharmacology
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Rat olfactory bulb and epithelium UDP-glucuronosyltransferase 2A1 (UGT2A1) expression: in situ mRNA localization and quantitative analysis.

2001

UDP-glucuronosyltransferases (UGTs) form a multigenic family of enzymes involved in the biotransformation and elimination of numerous endo- and xenobiotic compounds. Beside the diverse UGT isoforms present in the liver as well as in other tissues, the UGT2A1 isoform, also called olfactory UGT, was initially thought to be expressed in the nasal epithelium only. In this work, we demonstrate the UGT2A1 mRNA expression in the olfactory bulb, using in situ hybridization and quantitative reverse transcription-polymerase chain reaction (RT-PCR) techniques. Within the epithelium, UGT2A1 mRNA is mainly found in the sustentacular cells and to a lesser extent in Bowman's gland cells. Moreover, in situ…

Olfactory systemMaleCentral nervous systemNerve Tissue ProteinsIn situ hybridizationBiologyCellular and Molecular NeuroscienceMiceRapid amplification of cDNA endsOlfactory MucosaGene expressionmedicineAnimalsNeurons AfferentRNA MessengerGlucuronosyltransferaseRats WistarMolecular BiologyIn Situ HybridizationAir PollutantsMice Inbred BALB CSequence Homology Amino AcidReverse Transcriptase Polymerase Chain ReactionEpithelial CellsMolecular biologyOlfactory BulbEpitheliumOlfactory bulbRatsIsoenzymesmedicine.anatomical_structureInactivation MetabolicOlfactory epitheliumBrain research. Molecular brain research
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Immunoelectron microscopic localization of nitric oxide synthase III in the guinea pig organ of Corti

1998

Nitric oxide synthase III (NOS III) was identified in the guinea pig cochlea on an ultrastructural level using a post-embedding immunolabeling procedure. Ultrathin sections of London Resin (LR) White-embedded specimens were incubated with various concentrations of a commercially available antibody to NOS III and the immunoreactivity visualized by a gold-labeled secondary antibody. Analysis of ultrathin sections of the organ of Corti in the second turn of the cochlea showed that NOS III could be localized in the endothelial cells of the blood vessels under the basilar membrane, which was comparable to its location in similar cells types in various biological systems. Besides this, NOS III wa…

Pathologymedicine.medical_specialtyStereocilia (inner ear)Guinea PigsCuticular plateBiologyImmunolabelingHair Cells AuditorymedicineAnimalsMicroscopy ImmunoelectronOrgan of CortiCochleaLamina reticularisGeneral MedicineImmunohistochemistryBasilar MembraneCell biologyIsoenzymesmedicine.anatomical_structureOtorhinolaryngologyOrgan of CortiDeiters cellsEndothelium Vascularsense organsHair cellNitric Oxide SynthaseEuropean Archives of Oto-Rhino-Laryngology
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Nitric oxide synthase: expression and expressional control of the three isoforms.

1995

Three isozymes of nitric oxide synthase (NOS) have been identified. Their cDNA- and protein structures as well as their genomic DNA structures have been described. NOS I (ncNOS, originally discovered in neurons) and NOS III (ecNOS, originally discovered in endothelial cells) are low output, Ca(2+)-activated enzymes whose physiological function is signal transduction. NOS II (iNOS, originally discovered in cytokine-induced macrophages) is a high output enzyme which produces toxic amounts of NO that represent an important component of the antimicrobial, antiparasitic and antineoplastic activity of these cells. Depending on the species, NOS II activity is largely (human) or completely (mouse a…

PharmacologyGene isoformRegulation of gene expressionchemistry.chemical_classificationMessenger RNAbiologyChromosome MappingPromoterGeneral MedicineIsozymeMolecular biologyGene Expression Regulation EnzymologicRatsNitric oxide synthaseIsoenzymesMiceEnzymechemistryBiochemistrybiology.proteinTranscriptional regulationAnimalsHumansNitric Oxide SynthasePromoter Regions GeneticNaunyn-Schmiedeberg's archives of pharmacology
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Effect of nutritional imbalances on cytochrome P-450 isozymes in rat liver

1988

Male Sprague-Dawley rats were fed for six weeks either a control diet containing 22% casein (C) and 5% fat (F) or a low-protein diet (6% C, 5% F) or high-lipid diet (30% C, 30% F). A group of rats received a control diet containing 50 ppm of Phenoclor DP6. Three major forms of cytochrome P-450, UT 50, BP 3a and MC 2 were purified from livers of DP6-fed rats and only two forms, UT 50 and PB 3a, were purified from control and dietary groups. The amino acid composition and the catalytic activities towards all substrates tested were only significantly modified in the purified UT 50 P-450 isozyme from rats fed the low-protein diet. The N-terminal sequence analysis shows that cytochrome P-450 UT …

Pharmacologymedicine.medical_specialtyCytochromeSequence analysisCytochrome P450BiologyBiochemistryIsozymeRatsIsoenzymesPhenoclor DP6EndocrinologyCytochrome P-450 Enzyme SystemEnzyme InductionRat liverCaseinInternal medicineImmunologic TechniquesMicrosomes Liverbiology.proteinmedicineAnimalsAnimal Nutritional Physiological PhenomenaAmino AcidsEnzyme inducerBiochemical Pharmacology
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