Search results for "Nerve Tissue Protein"

showing 10 items of 345 documents

Mildronate and its neuroregulatory mechanisms: targeting the mitochondria, neuroinflammation, and protein expression.

2013

This review for the first time summarizes the data obtained in the neuropharmacological studies of mildronate, a drug previously known as a cardioprotective agent. In different animal models of neurotoxicity and neurodegenerative diseases, we demonstrated its neuroprotecting activity. By the use of immunohistochemical methods and Western blot analysis, as well as some selected behavioral tests, the new mechanisms of mildronate have been demonstrated: a regulatory effect on mitochondrial processes and on the expression of nerve cell proteins, which are involved in cell survival, functioning, and inflammation processes. Particular attention is paid to the capability of mildronate to stimulate…

Neurotoxicity SyndromeNerve Tissue ProteinsMitochondrionNeuroprotectionMiceAdjuvants ImmunologicNeuritismedicineAnimalsHumansLearningNeuroinflammationNeuronsbusiness.industryNeurogenesisNeurodegenerationNeurotoxicityParkinson DiseaseGeneral Medicinemedicine.diseaseMitochondriaNerve RegenerationRatsDisease Models AnimalNeuroprotective AgentsSynaptic plasticityNeurotoxicity SyndromesbusinessNeuroscienceMethylhydrazinesMedicina (Kaunas, Lithuania)
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UDP-glucuronosyltransferases (UGTs) in neuro-olfactory tissues: expression, regulation, and function.

2010

International audience; This work aims to review uridine diphosphate (UDP)-glucuronosyltransferase (UGT) expression and activities along different neuronal structures involved in the common physiological process of olfaction: olfactory epithelium, olfactory bulb, and olfactory cortex. For the first time, using high-throughput in situ hybridization data generated by the Allen Brain Atlas (ABA), we present quantitative analysis of spatial distribution of UGT genes in the mouse brain. The olfactory area is a central nervous system site with the highest expression of UGTs, including UGT isoforms not previously identified in the brain. Since there is evidence of the transfer of xenobiotics to th…

Olfactory systemMESH : RNA Messenger[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionMESH: GlucuronosyltransferaseMESH : Blood-Brain BarrierMESH: Blood-Brain Barrierchemistry.chemical_compound0302 clinical medicineMESH: SmellPharmacology (medical)MESH: AnimalsMESH: Uridine DiphosphateMESH: Nerve Tissue ProteinsGlucuronosyltransferaseGeneral Pharmacology Toxicology and PharmaceuticsMESH : Olfactory BulbMESH : Nerve Tissue Proteins0303 health sciencesMESH: Gene Expression Regulation EnzymologicOlfactory PathwaysOlfactory BulbMESH : OdorsCell biologySmellmedicine.anatomical_structureBlood-Brain BarrierMESH: Olfactory Bulbmedicine.medical_specialtyCentral nervous systemNerve Tissue ProteinsIn situ hybridizationOlfactionBiologydigestive systemGene Expression Regulation EnzymologicOlfactory Receptor NeuronsUridine DiphosphateMESH : Gene Expression Regulation Enzymologic03 medical and health sciencesInternal medicinemedicineAnimalsRNA MessengerMESH : Uridine Diphosphate030304 developmental biologyMESH: RNA MessengerMESH: OdorsMESH : Olfactory PathwaysMESH : GlucuronosyltransferaseMESH: Olfactory Receptor NeuronsOlfactory bulbUridine diphosphateEndocrinologychemistryOdorantsMESH : SmellMESH : Olfactory Receptor NeuronsMESH : AnimalsOlfactory epithelium[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition030217 neurology & neurosurgeryFunction (biology)MESH: Olfactory Pathways
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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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Distribution of the A3 subunit of the cyclic nucleotide-gated ion channels in the main olfactory bulb of the rat.

2008

Previous data suggest that cyclic GMP (cGMP) signaling can play key roles in the circuitry of the olfactory bulb (OB). Therefore, the expression of cGMP-selective subunits of the cyclic nucleotide-gated ion channels (CNGs) can be expected in this brain region. In the present study, we demonstrate a widespread expression of the cGMP-selective A3 subunit of the cyclic nucleotide-gated ion channels (CNGA3) in the rat OB. CNGA3 appears in principal cells, including mitral cells and internal, medium and external tufted cells. Moreover, it appears in two populations of interneurons, including a subset of periglomerular cells and a group of deep short-axon cells. In addition to neurons, CNGA3-immu…

Olfactory systemMaleDoublecortin ProteinRostral migratory streamPeriglomerular cellPopulationCyclic Nucleotide-Gated Cation ChannelsNerve Tissue ProteinsOlfactionBiologyOlfactory nervemedicineAnimalsRats Wistareducationgamma-Aminobutyric Acideducation.field_of_studyGeneral NeuroscienceOlfactory BulbCell biologyOlfactory bulbRatsmedicine.anatomical_structurenervous systemMicroscopy FluorescenceNeurogliaNeuroscienceNeuroscience
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Synaptogenesis in the mouse olfactory bulb during glomerulus development

2008

Synaptogenesis is essential for the development of neuronal networks in the brain. In the olfactory bulb (OB) glomeruli, numerous synapses must form between sensory olfactory neurons and the dendrites of mitral/tufted and periglomerular cells. Glomeruli develop from E13 to E16 in the mouse, coincident with an increment of the neuropil in the border between the external plexiform (EPL) and olfactory nerve layers (ONL), coupled to an extensive labelling of phalloidin and GAP-43 from the ONL to EPL. We have tracked synaptogenesis in the OB during this period by electron microscopy (EM) and immunolabelling of the transmembrane synaptic vesicle glycoprotein SV-2. No SV-2 labelling or synapses we…

Olfactory systemNeuropilTime FactorsPhalloidineSynaptic MembranesSynaptogenesisGAP-43Nerve Tissue ProteinsBiologymitral cellsSynaptic TransmissionOlfactory Receptor NeuronsMiceGAP-43 ProteinOlfactory MucosaOlfactory nerveolfactory sensory neuronsNeuropilmedicineAnimalsGlomerulus (olfaction)Membrane GlycoproteinsGeneral NeuroscienceSV-2Cell DifferentiationDendritesOlfactory BulbOlfactory bulbmedicine.anatomical_structureSynapsesembryonic structuresSynaptic VesiclesOlfactory ensheathing gliaolfactory epitheliumsense organsNeuroscienceOlfactory epitheliumBiomarkers
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New neurons follow the flow of cerebrospinal fluid in the adult brain

2006

Autores: Sawamoto, K. et al. .- PMID:16410488

Olfactory systemRecombinant Fusion ProteinsSubventricular zoneNerve Tissue ProteinsBiologyCerebral VentriclesLateral ventriclesMiceCerebrospinal fluidNeuroblastCell MovementNeuroblast migrationEpendymamedicineAnimalsBrain Tissue TransplantationCiliaCerebrospinal FluidNeuronsMultidisciplinaryCell PolarityEpithelial CellsAnatomyOlfactory BulbOlfactory bulbmedicine.anatomical_structurenervous systemChoroid PlexusIntercellular Signaling Peptides and ProteinsNeuronNeuroscience
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Ataxin-1 and ataxin-2 intermediate-length PolyQ expansions in amyotrophic lateral sclerosis.

2012

ABSTRACT Objective: Recent evidence suggests that intermediate-length polyglutamine (PolyQ) expansions in the ataxin-2 ( ATXN-2 ) gene are a risk factor for amyotrophic lateral sclerosis (ALS). This work was undertaken with the aim to investigate the frequency of ataxin-1 ( ATXN-1 ) and ATXN-2 PolyQ expansions in a cohort of patients with sporadic ALS (sALS) and patients with familial ALS (fALS) from southern Italy. Methods: We assessed the PolyQ lengths of ATXN-1 and ATXN-2 in 405 patients with sALS, 13 patients with fALS, and 296 unrelated controls without history of neurodegenerative disorders. Results: We found significantly higher intermediate PolyQ expansions ≥32 for ATXN-1 alleles an…

OncologyAdultMalemedicine.medical_specialtyGenotypeALS; ATXN-1; ATXN-2Ataxin 1Nerve Tissue ProteinsRisk FactorsInternal medicinemedicineHumansIn patientGenetic Predisposition to DiseaseAmyotrophic lateral sclerosisAlleleRisk factorAge of OnsetATXN-2ATXN-1AllelesAtaxin-1AgedAged 80 and overbiologybusiness.industryAmyotrophic Lateral SclerosisAge FactorsNuclear ProteinsMiddle Agedmedicine.diseaseIncreased riskPOLYGLUTAMINE EXPANSIONS; HEXANUCLEOTIDE REPEAT; ALS; TYPE-1; NEURODEGENERATION; PHENOTYPE; GENETICS; PROTEIN; C9ORF72; RISKAtaxinsItalyAtaxinCohortbiology.proteinFemaleSettore MED/26 - NeurologiaNeurology (clinical)ALSbusinessPeptidesTrinucleotide Repeat Expansion
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Neuroglobin and cytoglobin overexpression protects human SH-SY5Y neuroblastoma cells against oxidative stress-induced cell death

2006

Although reactive oxygen species (ROS) at physiological concentrations are required for normal cell function, excessive production of ROS is detrimental to cells. Neuroglobin and cytoglobin are two globins, whose functions are still a matter of debate. A potential role in the detoxification of ROS is suggested. The influence of neuroglobin and cytoglobin on cell death after oxidative stress in human neuroblastoma SH-SY5Y cells was evaluated. Exposure of SH-SY5Y cells to paraquat or H(2)O(2) resulted in a concentration- and time-dependent induction of apoptotic and necrotic cell death. H(2)O(2) was 16 times more potent to induce cell death as compared to paraquat. SH-SY5Y cells transfected w…

ParaquatProgrammed cell deathTime FactorsBlotting WesternGene ExpressionNeuroglobinNerve Tissue ProteinsBiologymedicine.disease_causeNeuroblastomaCell Line TumormedicineHumansGlobinCell DeathDose-Response Relationship DrugHerbicidesGeneral NeuroscienceCytoglobinCytoglobinHydrogen PeroxideTransfectionFlow CytometryOxidantsMolecular biologyGlobinsOxidative StressApoptosisCell cultureNeuroglobinOxidative stressNeuroscience letters
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Drosophila DJ-1 mutants are sensitive to oxidative stress and show reduced lifespan and motor deficits.

2007

Parkinson's disease (PD) is a progressive movement disorder caused by the selective and massive loss of dopaminergic neurons (DA) in the substantia nigra pars compacta (SNc). DJ-1 loss-of-function mutations are involved in inherited early-onset PD forms and result in dysfunction of the oxidative stress response. In mice models, DJ-1 loss provokes sensitivity to oxidative insults but does not produce neurodegeneration. Similar results have been found when analyzing Drosophila mutants for the DJ-1 orthologous genes, DJ-1alpha and DJ-1beta. Here, we report the analysis of two new mutations for the Drosophila DJ-1 genes. Both ubiquitous induction of DJ-1alpha knockdown by RNAi and loss of funct…

Parkinson's diseaseDopamineProtein Deglycase DJ-1Substantia nigraNerve Tissue ProteinsBiologyMotor Activitymedicine.disease_causeLife ExpectancyGeneticsmedicineAnimalsDrosophila ProteinsLoss functionNeuronsGene knockdownPars compactaNeurodegenerationAge FactorsGeneral MedicineAnatomymedicine.diseaseCell biologyOxidative Stressmedicine.anatomical_structureMutationRNA InterferenceNeuronOxidative stressGene
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The expression level of the orphan nuclear receptor GCNF (germ cell nuclear factor) is critical for neuronal differentiation.

2004

The germ cell nuclear factor (GCNF) is essential for normal embryonic development and gametogenesis. To test the prediction that GCNF is additionally required for neuronal differentiation, we used the mouse embryonal carcinoma cell line PCC7-Mz1, which represents an advantageous model to study neuronal cells from the stage of fate choice until the acquirement of functional competence. We generated stable transfectants that express gcnf sense or antisense RNA under the control of a tetracycline-regulated promoter. After retinoic acid-induced withdrawal from the cell cycle, sense clones developed a neuron network with changed properties, and the time course of neuron maturation was shortened.…

Patch-Clamp TechniquesGerm cell nuclear factorSynaptophysinDown-RegulationGene ExpressionReceptors Cytoplasmic and NuclearNerve Tissue ProteinsTretinoinBiologyNestinMiceEndocrinologyGAP-43 ProteinIntermediate Filament ProteinsNuclear Receptor Subfamily 6 Group A Member 1AnimalsRNA AntisenseMolecular BiologyNeuronsCell CycleCell PolarityCell DifferentiationGeneral MedicineCell cycleNestinCell biologyUp-RegulationNeuroepithelial cellDNA-Binding Proteinsnervous systemNeuron maturationSynaptophysinbiology.proteinNeuron differentiationStem cellMicrotubule-Associated ProteinsMolecular endocrinology (Baltimore, Md.)
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