Search results for "messenger"

showing 10 items of 1493 documents

Expressional control of the ‘constitutive’ isoforms of nitric oxide synthase (NOS I and NOS III)

1998

Nitric oxide synthase (NOS) exists in three established isoforms. NOS I (NOS1, ncNOS) was originally discovered in neurons. This enzyme and splice variants thereof have since been found in many other cells and tissues. NOS II (NOS2, iNOS) was first identified in murine macrophages, but can also be induced in many other cell types. NOS III (NOS3, ecNOS) is expressed mainly in endothelial cells. Whereas NOS II is a transcriptionally regulated enzyme, NOS I and NOS III are considered constitutively expressed proteins. However, evidence generated in recent years indicates that these two isoforms are also subject to expressional regulation. In view of the important biological functions of these …

LipopolysaccharidesGene isoformNitric Oxide Synthase Type IIITranscription GeneticNOS1Nitric Oxide Synthase Type IBiochemistryTranscription (biology)GeneticsTranscriptional regulationAnimalsHumansRNA MessengerGrowth SubstancesMolecular BiologyTranscription factorRegulation of gene expressionPolymorphism GeneticbiologyChemistryChromosome MappingLysophosphatidylcholinesNitric Oxide Synthase Type IIIEstrogensExonsCell biologyIsoenzymesLipoproteins LDLOxygenNitric oxide synthaseGene Expression Regulationbiology.proteinCytokinesNitric Oxide SynthaseGene DeletionBiotechnologyThe FASEB Journal
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Cloning and expression of a novel component of the CAP superfamily enhanced in the inflammatory response to LPS of the ascidian Ciona intestinalis.

2010

The CAP superfamily is a group of proteins that have been linked to several biological functions such as reproduction, cancer, and immune defense. A differential screening between lipopolysaccharide (LPS)-challenged and naive Ciona intestinalis has been performed to identify LPS-induced genes. This strategy has allowed the isolation of a full-length 1471-bp cDNA encoding for a 413-amino-acid protein (CiCAP). In silico analysis has shown that this polypeptide displays a modular structure with similarities to vertebrate CAP-superfamily proteins and to a collagen-binding adhesin of Streptococcus mutans. Domain organization analysis and alignment of CiCAP to other vertebrate CAP proteins have r…

LipopolysaccharidesHistologyHemocytesSequence analysisIn silicoMolecular Sequence DataSettore BIO/05 - ZoologiaSequence alignmentPolymerase Chain ReactionPathology and Forensic MedicineComplementary DNAAnimalsCiona intestinalisAmino Acid SequenceRNA MessengerCloning MolecularGenePeptide sequenceIn Situ HybridizationPhylogenyInflammationMessenger RNAbiologyBase SequenceSequence Homology Amino AcidProteinsCell BiologySequence Analysis DNAbiology.organism_classificationMolecular biologyCiona intestinalisInnate immune system differential display CAP protein molecular biology ciona intestinalis (Tunicata)Sequence AlignmentCell and tissue research
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Inability of rat alveolar macrophages to recycle l-citrulline to l-arginine despite induction of argininosuccinate synthetase mRNA and protein, and i…

1998

In the present study it was tested whether rat alveolar macrophages (AMphi) convert L-citrulline to L-arginine to maintain nitric oxide (NO) synthesis under conditions of limited availability of L-arginine. Rat AMphi (0.5 x 10(6) cells/well, cultured for 20 h in the absence or presence of 1 microg/ml lipopolysaccharides, LPS), were incubated for 6 h in amino acid-free Krebs solution and nitrite accumulation was determined as a measure of NO synthesis. After culture in the absence of LPS, nitrite in the incubation media was at the detection limit, independent of the addition of L-arginine or L-citrulline. AMphi, cultured in the presence of LPS, produced about 4 nmol per 10(6) cells and 6 h n…

LipopolysaccharidesMaleArginineBlotting WesternArgininosuccinate synthaseIn Vitro TechniquesArginineNitric OxideNitric oxidechemistry.chemical_compoundWestern blotMacrophages AlveolarmedicineAnimalsRNA MessengerNitriteIncubationCells CulturedPharmacologyDose-Response Relationship Drugbiologymedicine.diagnostic_testGeneral MedicineMetabolismL-citrullineArgininosuccinate LyaseRatschemistryBiochemistrybiology.proteinCitrullineFemaleNaunyn-Schmiedeberg's Archives of Pharmacology
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Neuronal activity triggers uptake of hematopoietic extracellular vesicles in vivo

2019

Communication with the hematopoietic system is a vital component of regulating brain function in health and disease. Traditionally, the major routes considered for this neuroimmune communication are by individual molecules such as cytokines carried by blood, by neural transmission, or, in more severe pathologies, by the entry of peripheral immune cells into the brain. In addition, functional mRNA from peripheral blood can be directly transferred to neurons via extracellular vesicles (EVs), but the parameters that determine their uptake are unknown. Using varied animal models that stimulate neuronal activity by peripheral inflammation, optogenetics, and selective proteasome inhibition of dop…

LipopolysaccharidesMaleGene ExpressionStimulationHippocampusBiochemistryStereotaxic Techniques0302 clinical medicineShort ReportsAnimal CellsMedicine and Health SciencesPremovement neuronal activityBiology (General)Routes of AdministrationNeurons0303 health sciencesBrain MappingKainic AcidBrainAnimal ModelsPeripheralCell biologyHaematopoiesisBioassays and Physiological AnalysisExperimental Organism SystemsHippocampus ; Yellow flourescent protein ; Intravenous injections ; Marker genes ; Gene expression ; Neurons ; Microglial cells ; OptogeneticsFemaleCellular TypesSignal TransductionProteasome Endopeptidase ComplexQH301-705.5Yellow Fluorescent ProteinMice TransgenicGlial CellsMouse ModelsStimulus (physiology)BiologyResearch and Analysis Methods03 medical and health sciencesExtracellular VesiclesImmune systemModel OrganismsIn vivoIntravenous InjectionsGeneticsAnimalsddc:610Molecular Biology TechniquesMolecular BiologyMicroglial Cells030304 developmental biologyInflammationPharmacologyMessenger RNABlood CellsUbiquitinDopaminergic NeuronsBiology and Life SciencesProteinsMarker GenesCell BiologyNeurophysiological AnalysisOptogeneticsLuminescent ProteinsCellular NeuroscienceAnimal Studies030217 neurology & neurosurgeryNeuroscience
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Expressional downregulation of neuronal-type NO synthase I in guinea pig skeletal muscle in response to bacterial lipopolysaccharide

1997

AbstractWe have investigated the expression of neuronal-type NO synthase I (NOS I) and inducible-type NOS II in guinea pig skeletal muscle (diaphragm). Expression of NOS I mRNA and protein was highest in muscle of specific pathogen-free animals, lower in normally bred animals, and lowest in lipopolysaccharide (LPS)-treated animals. NOS II mRNA and protein levels were highest in muscle of LPS-treated animals. Elevated NOS activity in muscle from LPS-treated animals was less susceptible to the NOS I-selective inhibitor NG-nitro-l-arginine. Expressional downregulation of NOS I in sepsis may have implications for contractile function of skeletal muscle.

LipopolysaccharidesMaleLipopolysaccharideGuinea PigsBiophysicsDown-RegulationAnti-NO synthase antibodiesBiochemistryNitric oxideGuinea pigchemistry.chemical_compoundDownregulation and upregulationStructural BiologyChapsGeneticsmedicineAnimalsNO synthase mRNAMuscle SkeletalMolecular BiologyNO synthase activityNeuronsMessenger RNAbiologySkeletal muscleCell BiologyMolecular biologyNitric oxide synthasemedicine.anatomical_structurechemistrybiology.proteinNitric Oxide SynthaseNG-nitro-l-arginineFEBS Letters
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Responses of retinal arterioles and ciliary arteries in pigs with acute respiratory distress syndrome (ARDS)

2019

Abstract Acute respiratory distress syndrome (ARDS) is a clinical syndrome of acute lung failure in critically sick patients, which severely compromises the function of multiple organs, including the brain. Although, the optic nerve and the retina are a part of the central nervous system, the effects of ARDS on these ocular structures are completely unknown. Thus, the major goal of this study was to test the hypothesis that ARDS affects vascular function in the eye. ARDS was induced in anesthetized pigs by intratracheal injection of lipopolysaccharide (LPS). Sham-treated animals served as controls. Pigs were monitored for 8 h and then sacrificed. Subsequently, retinal arterioles and short p…

LipopolysaccharidesMalePathologymedicine.medical_specialtyARDSEndotheliumRetinal ArterySwineNitric Oxide Synthase Type IIEnzyme-Linked Immunosorbent AssayVasodilationReal-Time Polymerase Chain ReactionCiliary ArteriesCellular and Molecular Neurosciencechemistry.chemical_compoundGlutathione Peroxidase GPX1medicine.arterymedicineAnimalsRNA MessengerEndothelial dysfunctionGlutathione PeroxidaseRespiratory Distress SyndromeRetinaMicroscopy Videobusiness.industryInterleukinsRetinalShort posterior ciliary arteriesCatalasemedicine.diseaseSensory SystemsCiliary arteriesArteriolesDisease Models AnimalOphthalmologymedicine.anatomical_structurechemistryEndothelium VascularHypoxia-Inducible Factor 1Reactive Oxygen SpeciesbusinessExperimental Eye Research
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Transcriptional up-regulation of nNOS in the dorsal vagal complex during low endotoxemia

2005

The present study analyses the expression and distribution of neuronal nitric oxide synthase (nNOS) in the brainstem of animals pre-treated with Escherichia coli or Helicobacter pylori LPS, at doses that modulate gastric motor function. Systemic administration of H. pylori LPS prevented in a dose-dependent manner (5, 40 and 100 microg kg(-1), i.v.) the increase in intragastric pressure induced by 2-deoxy-D-glucose (200 mg kg(-1), i.v.) in urethane-anaesthetized rats. Quantitative analysis showed a significant increase in the amount of nNOS mRNA induced by E. coli or H. pylori LPS (2 h later), in a segment of the brainstem containing the dorsal vagal complex (DVC). Immunohistochemical studie…

LipopolysaccharidesMalemedicine.medical_specialtyNerve Tissue ProteinsNitric Oxide Synthase Type Imedicine.disease_causeGeneral Biochemistry Genetics and Molecular BiologyRats Sprague-DawleyDownregulation and upregulationInternal medicineEscherichia coliPressuremedicineAnimalsGeneral Pharmacology Toxicology and PharmaceuticsEscherichia coliMessenger RNAbiologyStomachVagus NerveGeneral MedicineHelicobacter pyloribiology.organism_classificationEndotoxemiaRatsUp-RegulationEndocrinologyDorsal motor nucleusAnesthesiaSystemic administrationImmunohistochemistryBrainstemNitric Oxide SynthaseBrain StemLife Sciences
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Ciona intestinalis peroxinectin is a novel component of the peroxidase–cyclooxygenase gene superfamily upregulated by LPS

2013

Peroxinectins function as hemoperoxidase and cell adhesion factor involved in invertebrate immune reaction. In this study, the ascidian (Ciona intestinalis) peroxinectin gene (CiPxt) and its expression during the inflammatory response have been examined. CiPxt is a new member of the peroxidase-cyclooxygenase gene superfamily that contains both the peroxidase domain and the integrin KGD (Lys-Gly-Asp) binding motif. A phylogenetic tree showed that CiPxt is very close to the chordate group and appears to be the outgroup of mammalian MPO, EPO and TPO clades. The CiPxt molecular structure model resulted superimposable to the human myeloperoxidase. The CiPxt mRNA expression is upregulated by LPS …

LipopolysaccharidesModels MolecularHemocytesLPSAmino Acid MotifsMolecular Sequence DataPeroxinectinImmunologyIntegrinSettore BIO/05 - ZoologiaChordatePeroxinectin;Peroxidase;Inflammation;LPS;Ciona intestinalisAnimalsCiona intestinalisAmino Acid SequenceRNA MessengerCell adhesionPhylogenyPeroxidaseInflammationRegulation of gene expressionSequence Homology Amino AcidbiologyCell adhesion moleculeAnimal Structuresbiology.organism_classificationMolecular biologyImmunity InnateProtein Structure TertiaryCiona intestinalisGene Expression RegulationPeroxidasesOrgan SpecificityMyeloperoxidaseembryonic structuresImmunologybiology.proteinCell Adhesion MoleculesDevelopmental BiologyEndostyleDevelopmental & Comparative Immunology
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LTB4 is present in exudative pleural effusions and contributes actively to neutrophil recruitment in the inflamed pleural space

2004

SUMMARY The pleural space is a virtual compartment between the lung and chest wall that becomes filled with fluid and inflammatory cells during a variety of respiratory diseases. Here, we study the potential role of the eicosanoid metabolite leukotriene B4 (LTB4) in disparate diseases leading to acute (pneumonia) or chronic (tuberculosis, cancer) inflammation of the pleural space. LTB4 concentrations were significantly higher in pleural fluid due to pneumonia, tuberculosis and cancer with respect to congestive heart failure and correlated with neutrophil elastase, which is used as an indication of state of activation of neutrophils in the pleural space. Moreover, pleural LTB4 was biological…

LipopolysaccharidesPathologyHot TemperatureNeutrophilsLeukotriene B4Gene ExpressionEpitheliumchemistry.chemical_compoundNeoplasmsClinical StudiesImmunology and AllergyMedicineRespiratory systemPancreatic ElastasebiologyNeutrophilMiddle Agedrespiratory systemChemotaxis Leukocytemedicine.anatomical_structureNeutrophil InfiltrationNeutrophil elastaseLTB4Pleuralipids (amino acids peptides and proteins)medicine.symptomAdultmedicine.medical_specialtyImmunologyInflammationGranulocyteLeukotriene B4HumansRNA MessengerTuberculosis PulmonaryAgedArachidonate 5-LipoxygenaseLungbusiness.industryPneumoniaMacrophage Activationmedicine.diseaserespiratory tract diseasesPleural EffusionPneumoniaEicosanoidchemistryImmunologybiology.proteinbusinessClinical and Experimental Immunology
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Colocalization but differential regulation of neuronal NO synthase and nicotinic acetylcholine receptor in C2C12 myotubes.

2003

In mammalian skeletal muscle, neuronal-type nitric oxide synthase (nNOS) is found to be enriched at neuromuscular endplates. Here we demonstrate the colocalization of the nicotinic acetylcholine receptor (nAChR, stained with α-bungarotoxin) and nNOS (stained with a specific antibody) in murine C2C12myotubes. However, coimmunoprecipitation experiments demonstrated no evidence for a direct protein-protein association between the nAChR and nNOS in C2C12myotubes. An antibody to the α1-subunit of the nAChR did not coprecipitate nNOS, and an nNOS-specific antibody did not precipitate the α1-subunit of the nAChR. Treatment of mice with bacterial LPS downregulated the expression of nNOS in skeletal…

LipopolysaccharidesPhysiologyMuscle Fibers SkeletalNitric Oxide Synthase Type IReceptors NicotinicCell LineInterferon-gammaMicemedicineAnimalsProtein IsoformsTissue DistributionRNA MessengerMuscle SkeletalMice Inbred C3HbiologyMyogenesisSkeletal muscleColocalizationCell BiologyMolecular biologyNitric oxide synthaseNicotinic acetylcholine receptormedicine.anatomical_structureNicotinic agonistnervous systembiology.proteinNitric Oxide SynthaseC2C12Acetylcholinemedicine.drugAmerican journal of physiology. Cell physiology
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