Search results for "Biopterin"

showing 10 items of 25 documents

Nitric oxide synthase inhibition and oxidative stress in cardiovascular diseases: Possible therapeutic targets?

2013

International audience; Nitric oxide (• NO) is synthetized enzymatically from L-arginine (L-Arg) by three NO synthase isoforms, iNOS, eNOS and nNOS. The synthesis of NO is selectively inhibited by guanidino-substituted analogs of L-Arg or methylarginines such as asymmetric dimethylarginine (ADMA), which results from protein degradation in cells. Many disease states, including cardiovascular diseases and diabetes, are associated with increased plasma levels of ADMA. The N-terminal catalytic domain of these NOS isoforms binds the heme prosthetic group as well as the redox cofactor, tetrahydrobiopterin (BH 4) associated with a regulatory protein, calmodulin (CaM). The enzymatic activity of NOS…

NO inhibitorsfree radicals030204 cardiovascular system & hematologyProtein degradationPharmacologyNitric OxideNitric oxide03 medical and health scienceschemistry.chemical_compoundBH 40302 clinical medicine[SDV.MHEP.CSC]Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular systemcardiovascular diseaseEnosmedicineAnimalsHumansPharmacology (medical)Enzyme InhibitorsEndothelial dysfunctionReactive nitrogen species030304 developmental biologyPharmacologyNO synthases0303 health sciencesbiologyTetrahydrobiopterinbiology.organism_classificationmedicine.disease[SDV.MHEP.CSC] Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular system3. Good healthADMANitric oxide synthaseOxidative StresschemistryBiochemistryCardiovascular Diseasesbiology.proteinNitric Oxide SynthaseAsymmetric dimethylargininemedicine.drugPharmacology & Therapeutics
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Uncoupling of endothelial NO synthase in atherosclerosis and vascular disease.

2013

Nitric oxide (NO) produced by the endothelial NO synthase (eNOS) is an antihypertensive, antithrombotic and anti-atherosclerotic molecule. Hypercholesterolemia leads to a reduction in vascular NO bioavailability. This is attributed to a dysfunction of the eNOS enzyme and a reduced eNOS activity. NADPH oxidase-mediated oxidative stress leads to oxidation of tetrahydrobiopterin (BH4), the essential cofactor of eNOS. In BH4 deficiency, oxygen reduction uncouples from NO synthesis, thereby converting eNOS to a superoxide-producing enzyme. As a consequence of eNOS uncoupling, NO production is reduced and the pre-existing oxidative stress is enhanced, which contribute significantly to atherogenes…

Pharmacologymedicine.medical_specialtyAngiotensin II receptor type 1biologyNitric Oxide Synthase Type IIINitric Oxide Synthase Type IIITetrahydrobiopterinResveratrolbiology.organism_classificationmedicine.disease_causeNitric OxideNebivololNitric oxidechemistry.chemical_compoundEndocrinologychemistryEnosInternal medicineDrug DiscoverymedicineAnimalsHumansVascular DiseasesOxidative stressmedicine.drugCurrent opinion in pharmacology
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Regulation of pteridine biosynthesis and aromatic amino acid hydroxylation in Drosophila melanogaster

1989

The relationship between high dietary levels of aromatic amino acid and regulation of pteridines in Drosophila eyes was examined by measuring changes in pool levels of six pterins in the wild type and mutants and amino acid pool levels in flies that carry mutations for pteridine biosynthesis. The effect upon relative viability and developmental times was also analyzed; relative viability was affected by L-phenylalanine, L-tryptophan, and L-tyrosine in decreasing order and the D-amino acids had little or no effect. The changes in concentration of biopterin, dihydrobiopterin, pterin, sepiapterin, drosopterins, and isoxanthopterin showed a characteristic pattern of increased and/or decreased a…

PhenylalanineBiopterinPhenylalanineBiologyHydroxylationBiochemistrychemistry.chemical_compoundDihydrobiopterinGeneticsmedicineAromatic amino acidsAnimalsAmino AcidsPterinMolecular BiologyEcology Evolution Behavior and Systematicschemistry.chemical_classificationPteridinesTryptophanGeneral MedicineTetrahydrobiopterinAmino acidDrosophila melanogasterchemistryBiochemistryMutationTyrosinePteridinemedicine.drug
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Pharmacological prevention of eNOS uncoupling.

2013

Under physiological conditions, nitric oxide (NO) is produced in the vasculature mainly by the endothelial NO synthase (eNOS). This endothelium-derived NO is a protective molecule with antihypertensive, antithrombotic and anti-atherosclerotic properties. Cardiovascular risk factors such as hypertension, hypercholesterolemia, cigarette smoking and diabetes mellitus induce oxidative stress mostly by stimulation of the NADPH oxidase. Overproduction of reactive oxygen species leads to oxidation of tetrahydrobiopterin (BH4), the essential cofactor of eNOS. In BH4 deficiency, oxygen reduction uncouples from NO synthesis, thereby converting eNOS to a superoxide- producing enzyme. Consequently, NO …

SepiapterinNitric Oxide Synthase Type IIImedicine.drug_classPharmacologymedicine.disease_causeNitric OxideRenin inhibitorNitric oxidechemistry.chemical_compoundEnosDrug DiscoverymedicineHumansPharmacologyNADPH oxidasebiologyEndothelial CellsTetrahydrobiopterinAliskirenbiology.organism_classificationOxidative StresschemistryCardiovascular Diseasesbiology.proteinReactive Oxygen SpeciesOxidative stressmedicine.drugCurrent pharmaceutical design
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Sepiapterin reductase in cultured human cells.

1987

Sepiapterin reductase, an enzyme involved in the synthesis of tetrahydrobiopterin (the natural cofactor for phenylalanine, tyrosine and tryptophan hydroxylases), has been assayed in cultured human amniotic fibroblasts and in cultured mononuclear blood cells. In both cases, the Michaelis constants for sepiapterin and NADPH were essentially equal; 20 microM and 6 microM respectively for stimulated mononuclear blood cells and 22 microM and 5 microM respectively for amniotic fibroblasts. The inhibition by N-acetylserotonin was also similar in both cases. The concentration that produced 50% inhibition in stimulated mononuclear blood cells and in amniotic fibroblasts was 2 microM. The results str…

SepiapterinSerotoninBiophysicsPhenylalanineBiochemistryCofactorchemistry.chemical_compoundmedicineHumansAmnionTyrosineSepiapterin reductaseMolecular BiologyCells Culturedchemistry.chemical_classificationbiologyTryptophanCell BiologyTetrahydrobiopterinMolecular biologyAlcohol OxidoreductasesKineticsEnzymechemistryBiochemistrybiology.proteinLeukocytes Mononuclearmedicine.drugBiochemical and biophysical research communications
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Developmental and biochemical studies on the phenylalanine hydroxylation system in Drosophila melanogaster

1992

Abstract The enzyme phenylalanine hydroxylase, the substrate phenylalanine, the product of the reaction tyrosine, and the probable in vivo cofactors (6R)- l -erytro-5,6,7,8-tetrahydrobiopterin (H4Bip) and 5,6,7,8-tetrahydropterin (H4Ptr), have been measured during development in Drosophila. The developmental profile of phenylalanine hydroxylase activity shows two peaks. The larger occurs at the time of pupation, coiciding with an important accumulation of tyrosine in the insect. The minor peak appears at the time of adult emergence. The developmental profile of H4Bip shows also two peaks, coinciding with those of maximal phenylalanine hydroxylase activity. However, H4Ptr is only detectable …

chemistry.chemical_classificationDevelopmental profilebiologyPhenylalanine hydroxylasePhenylalanineTetrahydrobiopterinBiochemistryCofactorHydroxylationchemistry.chemical_compoundEnzymechemistryBiochemistryInsect Sciencebiology.proteinmedicineTyrosineMolecular Biologymedicine.drug
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Implication of eNOS Uncoupling in Cardiovascular Disease

2017

Under physiological conditions, nitric oxide (NO) is produced in the vasculature mainly by the endothelial nitric oxide synthase (eNOS). Endothelial NO relaxes blood vessels, inhibits platelet activity, and protects against atherosclerosis. Under pathological conditions such as hypertension, diabetes, and hypercholesterolemia, eNOS may become uncoupled. Uncoupled eNOS generates superoxide at the expense of NO and contributes substantially to oxidative stress and endothelial dysfunction. Major mechanisms of eNOS uncoupling include deficiency of the eNOS cofactor tetrahydrobiopterin, deficiency of the eNOS substrate L-arginine, and eNOS S-glutathionylation. Reversal of eNOS uncoupling may rep…

chemistry.chemical_classificationmedicine.medical_specialtyReactive oxygen speciesbiologybusiness.industrySuperoxideTetrahydrobiopterinbiology.organism_classificationmedicine.disease_causemedicine.diseaseNitric oxidechemistry.chemical_compoundEndocrinologychemistryEnosInternal medicinemedicinePlatelet activationEndothelial dysfunctionbusinessOxidative stressmedicine.drugReactive Oxygen Species
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Pigment patterns in mutants affecting the biosynthesis of pteridines and xanthommatin in Drosophila melanogaster.

1986

Eye-color mutants of Drosophila melanogaster have been analyzed for their pigment content and related metabolites. Xanthommatin and dihydroxanthommatin (pigments causing brown eye color) were measured after selective extraction in acidified butanol. Pteridines (pigments causing red eye color) were quantitated after separation of 28 spots by thin-layer chromatography, most of which are pteridines and a few of which are fluorescent metabolites from the xanthommatin pathway. Pigment patterns have been studied in 45 loci. The pteridine pathway ramifies into two double branches giving rise to isoxanthopterin, “drosopterins,” and biopterin as final products. The regulatory relationship among the …

genetic structuresMutantDihydroxanthommatinBiopterinBiochemistryPigmentchemistry.chemical_compoundBiosynthesisOxazinesGeneticsEye colormedicineAnimalsAmino AcidsMolecular BiologyEcology Evolution Behavior and SystematicsGeneticsbiologyEye ColorPteridinesGeneral MedicinePigments Biologicalbiology.organism_classificationDrosophila melanogasterBiochemistrychemistryXanthenesvisual_artMutationvisual_art.visual_art_mediumsense organsDrosophila melanogasterRetinal PigmentsPteridinemedicine.drugBiochemical genetics
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Arginine and nitric oxide synthase: regulatory mechanisms and cardiovascular aspects

2014

L-Arginine (L-Arg) is a conditionally essential amino acid in the human diet. The most common dietary sources of L-Arg are meat, poultry and fish. L-Arg is the precursor for the synthesis of nitric oxide (NO); a key signaling molecule via NO synthase (NOS). Endogenous NOS inhibitors such as asymmetric-dimethyl-L-Arg inhibit NO synthesis in vivo by competing with L-Arg at the active site of NOS. In addition, NOS possesses the ability to be "uncoupled" to produce superoxide anion instead of NO. Reduced NO bioavailability may play an essential role in cardiovascular pathologies and metabolic diseases. L-Arg deficiency syndromes in humans involve endothelial inflammation and immune dysfunctions…

medicine.medical_specialtyArgininemedicine.disease_causeArginineCardiovascular SystemNitric oxidechemistry.chemical_compoundImmune system[SDV.MHEP.CSC]Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular systemInternal medicinemedicineHumansComputingMilieux_MISCELLANEOUSbiologySuperoxideNitric oxide synthasecardiovascularBiological TransportTetrahydrobiopterinmedicine.diseaseBiopterinDiet3. Good health[SDV.MHEP.CSC] Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular systemNitric oxide synthaseEndocrinologyAdipose TissuechemistryCardiovascular DiseasesDietary Supplementsbiology.proteinCitrullineMetabolic syndrometherapeutic potentialOxidative stressFood ScienceBiotechnologymedicine.drug
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Cardiovascular and Endocrine Properties of L-Tryptophan in Combination with Various Diets

1991

Brain serotonin neurons are intimately involved in a number of relevant physiological functions such as cardiovascular regulation, neuroendocrine output from the anterior pituitary (e.g. ACTH, prolactin), regulation of behavior (e.g. agression, sleep, locomotor and sexual behavior), mood or appetite control (Fernstrom, 1983; Lehnert et al., 1987; Spring et al., 1987; Wurtman, 1987). The synthesis of brain serotonin is dependent on the availability of the large neutral amino acid L-tryptophan that is hydroxylated to 5-L-hydroxytryptophan and subsequently decarboxylated to yield serotonin. The rate-limiting enzyme tryptophan hydroxylase has a Michaelis constant of approximately 2–3 x 10−5 M w…

medicine.medical_specialtyChemistryTryptophanAdrenocorticotropic hormoneTetrahydrobiopterinTryptophan hydroxylaseProlactinmedicine.anatomical_structureEndocrinologyAnterior pituitaryInternal medicinemedicineSerotoninTyrosinemedicine.drug
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