Search results for "arginine"

showing 10 items of 389 documents

Potential Functional Significance of Brain-Type and Muscle-Type Nitric Oxide Synthase I Expressed in Adventitia and Media of Rat Aorta

1999

Abstract —Skeletal muscle and myocardium express μNOS I, an elongated splice variant of neuronal-type nitric oxide (NO) synthase (NOS I), and NOS III, endothelial-type NO synthase, respectively. This study was designed to elucidate whether vascular smooth muscle also contains a constitutively expressed NO synthase isoform. In the rat, μNOS I contains an insert of 102 nucleotides after nucleotide 2865 of the cDNA, yielding a protein of 164 kd. Reverse transcription-polymerase chain reaction with primers flanking this insert and with insert-specific primers indicated that endothelium-denuded rat aorta expresses both brain-type NOS I and μNOS I. RNase protection analyses with an antisense RNA…

Gene isoformPathologymedicine.medical_specialtyDNA ComplementaryVascular smooth muscleNitric Oxide Synthase Type IIIBlotting WesternAorta ThoracicNitric Oxide Synthase Type INitroarginineGene Expression Regulation EnzymologicMuscle Smooth VascularMembrane PotentialsPotassium ChlorideNitric oxideImmunoenzyme TechniquesRats Sprague-DawleyNorepinephrinechemistry.chemical_compoundmedicine.arteryAdventitiamedicineAnimalsVasoconstrictor AgentsAorta AbdominalRNA MessengerMuscle SkeletalMessenger RNAAortabiologyBrainSkeletal muscleMolecular biologyRatsNitric oxide synthaseAntisense Elements (Genetics)medicine.anatomical_structurechemistryVasoconstrictionbiology.proteinCalciumFemaleNitric Oxide SynthaseTunica MediaCardiology and Cardiovascular MedicineArteriosclerosis, Thrombosis, and Vascular Biology
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Nitric oxide synthase isozymes. Characterization, purification, molecular cloning, and functions.

1994

Three isozymes of nitric oxide (NO) synthase (EC 1.14.13.39) have been identified and the cDNAs for these enzymes isolated. In humans, isozymes I (in neuronal and epithelial cells), II (in cytokine-induced cells), and III (in endothelial cells) are encoded for by three different genes located on chromosomes 12, 17, and 7, respectively. The deduced amino acid sequences of the human isozymes show less than 59% identity. Across species, amino acid sequences for each isoform are well conserved (> 90% for isoforms I and III, > 80% for isoform II). All isoforms use L-arginine and molecular oxygen as substrates and require the cofactors NADPH, 6(R)-5,6,7,8-tetrahydrobiopterin, flavin adenine…

Gene isoformVascular smooth muscleCalmodulinbiologyATP synthaseArginineMolecular biologyIsozymeNitric oxideIsoenzymesNitric oxide synthasechemistry.chemical_compoundchemistryInternal Medicinebiology.proteinAnimalsHumansTissue DistributionAmino Acid OxidoreductasesCloning MolecularNitric Oxide SynthaseHemeHypertension
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Analysis of tombusvirus revertants to identify essential amino acid residues within RNA-dependent RNA polymerase motifs

2005

The RNA-dependent RNA polymerase (RdRp) of Tomato bushy stunt virus (TBSV) contains an arginine- and proline-rich (RPR) motif. This motif functions as an RNA-binding domain and is essential for tombusvirus replication. A mutant carrying three arginine substitutions in this motif rendered the virus unable to replicate in Nicotiana benthamiana plants and protoplasts. When the replicase function was provided in trans, by expressing the TBSV RdRp in N. benthamiana plants, an infectious variant could be isolated. Sequence analysis showed that only the substituted glycine residue (position 216) had reverted to arginine; all other substitutions remained unchanged. This finding suggested that stron…

GeneticsTombusvirusArginineSequence analysisvirusesfungifood and beveragesRNA-dependent RNA polymeraseNicotiana benthamianaBiologyRNA-Dependent RNA Polymerasebiology.organism_classificationVirologyTombusviruschemistry.chemical_compoundTombusviridaechemistryVirologyRNA polymeraseRNA ViralAmino AcidsTomato bushy stunt virusJournal of General Virology
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Amino acid activation in Ciona ovary and developing egg

1964

E stata studiata la attivazione di alcuni amini acidi negli ovociti nell'uovo vergine e nell'uovo fecondato diCiona intestinalis. L'andamento della attivazione della glicina e stato seguito sino alla neurulazione. Il quantitativo di amino acidi attivati e minimo nell'uovo vergine, esso aumenta rapidamente dopo la fecondazione. Durante la gastrulazione la attivazione della glicina raggiunge i valori maggiori.

GlycineOvaryIn Vitro TechniquesBiologyArginineCellular and Molecular NeuroscienceChordata NonvertebrateLeucinemedicineAnimalsHistidineMolecular BiologyOvumPharmacologyAmino acid activationAlanineOvaryCell Biologybiology.organism_classificationMolecular biologyCionamedicine.anatomical_structureBiochemistryProtein BiosynthesisTyrosineMolecular MedicineFemaleExperientia
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ARGININE, HISTIDINE AND TRYPTOPHAN IN PEPTIDE SYNTHESIS. THE INDOLE FUNCTION OF TRYPTOPHAN

1990

Indole testchemistry.chemical_compoundArginineBiochemistryChemistryOrganic ChemistryTryptophanPeptide synthesisHistidineFunction (biology)Organic Preparations and Procedures International
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ChemInform Abstract: Arginine, Histidine, and Tryptophan in Peptide Synthesis. The Indole Function of Tryptophan

2010

Indole testchemistry.chemical_compoundArginineBiochemistryChemistryStereochemistryTryptophanPeptide synthesisGeneral MedicineHistidineFunction (biology)ChemInform
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Fluvastatin stabilizes the blood–brain barrier in vitro by nitric oxide-dependent dephosphorylation of myosin light chains

2006

Inhibition of the 3-hydroxy-3-methylglutaryl-coenzyme-A reductase and the downstream mevalonate pathway is in part responsible for the beneficial effects that statins exert on the cardiovascular system. In this study we aimed at analysing the stabilizing effects of fluvastatin on the blood-brain barrier (BBB) integrity, using an in vitro co-culture model of ECV304 and C6, or primary bovine endothelial cells and rat astrocytes. Fluvastatin dose-dependently (1-25 micromol/l) increased barrier integrity as analysed by measurements of transendothelial electrical resistance (TEER). This effect (117.4+/-2.6% at 25 micromol/l) was significantly reduced by the nitric oxide (NO) synthase inhibitor L…

IndolesMyosin Light ChainsMyosin light-chain kinaseGeranylgeranyl pyrophosphatePhosphataseFarnesyl pyrophosphateBiologyNitric OxideBlood–brain barrierAntioxidantsCapillary PermeabilityFatty Acids MonounsaturatedDephosphorylationMiceCellular and Molecular Neurosciencechemistry.chemical_compoundElectric ImpedancemedicineAnimalsDrug InteractionsEnzyme InhibitorsFluvastatinCells CulturedPharmacologyAnalysis of VarianceMicroscopy Confocalomega-N-MethylarginineDose-Response Relationship DrugEndothelial CellsBiological TransportMolecular biologyCoculture TechniquesRatsmedicine.anatomical_structurechemistryBiochemistryBlood-Brain BarrierAstrocytesModels AnimalCattleMevalonate pathwayFluvastatinmedicine.drugNeuropharmacology
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Arginine-Rich Peptidomimetic Ampicillin/Gentamicin Conjugate To Tackle Nosocomial Biofilms: A Promising Strategy To Repurpose First-Line Antibiotics

2023

: Combined therapy with penicillins and aminoglycosides has been proved beneficial to address many persistent bacterial infections with possible synergistic effects. However, the different pharmacokinetic profiles of these two antibiotic classes may not guarantee a concerted spatio-temporal delivery at the site of action, decreasing the efficacy of this combination and promoting resistance. Herein, we propose a multifunctional antibiotic-polymer conjugate, designed to colocalize ampicillin and gentamicin to tackle persistent biofilm infections. The two antibacterial molecules were grafted along with the amino acid l-arginine to a biocompatible polymer backbone with peptidomimetic hydrophili…

Infectious DiseasesantibiofilmSettore CHIM/09 - Farmaceutico Tecnologico Applicativopeptidomimeticsdrug deliveryampicillinargininegentamicinSettore MED/42 - Igiene Generale E ApplicataACS Infectious Diseases
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Gliadin-mediated production of polyamines by RAW264.7 macrophages modulates intestinal epithelial permeability in vitro

2015

AbstractCeliac disease (CD) is an immune-mediated enteropathy sustained by dietary gluten in susceptible individuals, and characterized by a complex interplay between adaptive and innate responses against gluten peptides (PTG). In a recent contribution we have demonstrated that the treatment with PTG induces the expression and activity of arginase in both murine macrophages and human monocytes from healthy subjects, thus suggesting a role for arginine and its metabolites in gluten-triggered response of these cells. Here we further explore this field, by addressing the effects of PTG on polyamine synthesis and release in murine RAW264.7 macrophages, and how they affect epithelial permeabilit…

Intestinal permeabilityArginineArginaseInflammationBiologyIntestinal permeabilitymedicine.diseaseIn vitroGliadinCell biologyArginasechemistry.chemical_compoundBiochemistrychemistrymedicinePutrescinebiology.proteinPolyaminesMolecular MedicineCeliac diseaseSecretionmedicine.symptomGliadinMolecular BiologyBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
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Role of Neutral Amino Acid Transport and Protein Breakdown for Substrate Supply of Nitric Oxide Synthase in Human Endothelial Cells

2003

Endothelial dysfunction is often associated with a relative substrate deficiency of the endothelial nitric oxide synthase (eNOS) in spite of apparently high intracellular arginine concentrations. For a better understanding of the underlying pathophysiological mechanisms, we aimed to characterize the intracellular arginine sources of eNOS. Our previous studies in human endothelial EA.hy926 cells suggested the existence of two arginine pools: pool I can be depleted by extracellular lysine, whereas pool II is not freely exchangeable with the extracellular space, but accessible to eNOS. In this study, we demonstrate that the eNOS accessible pool II is also present in human umbilical vein endoth…

Intracellular FluidUmbilical VeinsNitric Oxide Synthase Type IIIArginineEndotheliumPhysiologyGlutamineArginineTransfectionSubstrate Specificitychemistry.chemical_compoundEnosNeutral amino acid transportCitrullinemedicineAnimalsHumansAmino AcidsCells CulturedbiologyCarcinomaMembrane Transport ProteinsProteinsNitric Oxide Synthase Type IIIBiological Transportbiology.organism_classificationRatsEndothelial stem cellNitric oxide synthaseAmino Acid Transport Systems NeutralAmino Acids Neutralmedicine.anatomical_structureUrinary Bladder NeoplasmsBiochemistrychemistrybiology.proteinCitrullineEndothelium VascularNitric Oxide SynthaseCardiology and Cardiovascular MedicineCirculation Research
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