Search results for "Nerve Tissue Protein"

showing 10 items of 345 documents

Circadian gene expression patterns of melanopsin and pinopsin in the chick pineal gland

2004

The directly light-sensitive chick pineal gland contains at least two photopigments. Pinopsin seems to mediate the acute inhibitory effect of light on melatonin synthesis, whereas melanopsin may act by phase-shifting the intrapineal circadian clock. In the present study we have investigated, by means of quantitative RT-PCR, the daily rhythm of photopigment gene expression as monitored by mRNA levels. Under a 12-h light/12-h dark cycle, the mRNA levels of both pigments were 5-fold higher in the transitional phase from light to dark than at night, both in vivo and in vitro. Under constant darkness in vivo and in vitro, the peak of pinopsin mRNA levels was attenuated, whereas that of melanopsi…

Melanopsinmedicine.medical_specialtyLightPhotoperiodCircadian clockBiophysicsNerve Tissue ProteinsBiologyPineal GlandBiochemistryAvian ProteinsPineal glandInternal medicineGene expressionmedicineAnimalsPhotopigmentCircadian rhythmMolecular BiologyCells CulturedRegulation of gene expressionAdaptation OcularRod OpsinsCell BiologyCircadian Rhythmmedicine.anatomical_structureEndocrinologyAnimals NewbornGene Expression RegulationLight effects on circadian rhythmsense organsChickensBiochemical and Biophysical Research Communications
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Atrial natriuretic peptide and CD34 overexpression in human idiopathic dilated cardiomyopathies.

2007

Idiopathic dilated cardiomyopathy (IDCM) is a primary myocardial disease of unknown cause characterized by ventricular chamber enlargement with impaired contractile function. In familial forms of IDCM, mutations of genes coding for cytoskeletal proteins related to force transmission, such as dystrophin, cardiac actin, desmin, and delta-sarcoglycan, have been identified. Here, we report the data of a retrospective investigation carried out to evaluate the expression of atrial natriuretic peptide (ANP), CD34, troponin T and nestin in the myocardium of patients affected with IDCM. Formalin-fixed and paraffin-embedded consecutive tissue sections from the ventricular wall of 10 human normal hear…

Microbiology (medical)ventricular myocytesCardiomyopathy Dilatedmedicine.medical_specialtyHeart VentriclesCardiomyopathyAntigens CD34Nerve Tissue ProteinsANP; CD34; nestin; troponin T; endothelial cells; ventricular myocytesPathology and Forensic MedicineNestinAtrial natriuretic peptideIntermediate Filament ProteinsTroponin TAntigens CDReference ValuesInternal medicineIdiopathic dilated cardiomyopathymedicineImmunology and AllergyHumansTroponin Tbiologybusiness.industryDilated cardiomyopathyGeneral MedicineNestinmedicine.diseaseTroponinImmunohistochemistryCardiologybiology.proteinendothelial cellDesminCD34AutopsybusinessANPAtrial Natriuretic FactorBiomarkersAPMIS : acta pathologica, microbiologica, et immunologica Scandinavica
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Lack of GDAP1 induces neuronal calcium and mitochondrial defects in a knockout mouse model of Charcot-Marie-tooth neuropathy

2015

27 páginas, 9 figuras.

Mitochondrial proteinCancer Researchlcsh:QH426-470Nerve Tissue ProteinsBiologyMitochondrionCharcot-Marie-Tooth diseaseGDAP1 geneMiceGeneticsAutophagyAnimalsCalcium SignalingMolecular BiologyGenetics (clinical)Ecology Evolution Behavior and SystematicsCytoskeletonCalcium signalingGeneticsVoltage-dependent calcium channelEndoplasmic reticulumAutophagyBiología y Biomedicina / BiologíaAxonsCell biologyMitochondriaMitochondrialMice Inbred C57BLAlpha tubulinlcsh:Geneticsmitochondrial fusionKnockout mouseMitochondrial fissionCalcium ChannelsAnimal cellGene DeletionResearch Article
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The Protein Structure Context of PolyQ Regions.

2016

Proteins containing glutamine repeats (polyQ) are known to be structurally unstable. Abnormal expansion of polyQ in some proteins exceeding a certain threshold leads to neurodegenerative disease, a symptom of which are protein aggregates. This has led to extensive research of the structure of polyQ stretches. However, the accumulation of contradictory results suggests that protein context might be of importance. Here we aimed to evaluate the structural context of polyQ regions in proteins by analysing the secondary structure of polyQ proteins and their homologs. The results revealed that the secondary structure in polyQ vicinity is predominantly random coil or helix. Importantly, the region…

Models MolecularProtein Conformation alpha-HelicalProtein Structure ComparisonProtein StructureSaccharomyces cerevisiae ProteinsGlutaminelcsh:MedicineNerve Tissue ProteinsSaccharomyces cerevisiaePlant ScienceResearch and Analysis MethodsBiochemistryPlant Roots570 Life sciencesDatabase and Informatics MethodsProtein Structure DatabasesMacromolecular Structure AnalysisHumansProtein Interaction Domains and MotifsAmino AcidsDatabases ProteinProtein Interactionslcsh:ScienceMolecular BiologyMediator ComplexOrganic CompoundsPlant AnatomyAcidic Amino AcidsOrganic Chemistrylcsh:RChemical CompoundsBiology and Life SciencesProteinsRoot StructureChemistryBiological DatabasesProtein-Protein InteractionsPhysical Scienceslcsh:QStructural ProteinsProtein Structure DeterminationPeptidesResearch Article570 BiowissenschaftenPLoS ONE
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The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin.

2003

Neuroglobin and cytoglobin reversibly bind oxygen in competition with the distal histidine, and the observed oxygen affinity therefore depends on the properties of both ligands. In the absence of an external ligand, the iron atom of these globins is hexacoordinated. There are three cysteine residues in human neuroglobin; those at positions CD7 and D5 are sufficiently close to form an internal disulfide bond. Both cysteine residues in cytoglobin, although localized in other positions than in human neuroglobin, may form a disulfide bond as well. The existence and position of these disulfide bonds was demonstrated by mass spectrometry and thiol accessibility studies. Mutation of the cysteines …

Models MolecularSpectrometry Mass Electrospray IonizationStereochemistryNeuroglobinNerve Tissue ProteinsLigandsBiochemistryRedoxHumansHistidineCysteineDisulfidesGlobinMolecular BiologyHistidineChemistryCytoglobinCytoglobinCell BiologyLigand (biochemistry)Recombinant ProteinsGlobinsOxygenKineticsNeuroglobinOxidation-ReductionOxygen bindingProtein BindingCysteine
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High Pressure Enhances Hexacoordination in Neuroglobin and Other Globins

2005

The techniques of high applied pressure and flash photolysis have been combined to study ligand rebinding to neuroglobin (Ngb) and tomato Hb, globins that may display a His-Fe-His hexacoordination in the absence of external ligands. High pressure induces a moderate decrease in the His association rate and a large decrease in His dissociation rate, thus leading to an enhancement of the overall His affinity. The overall structural difference between penta- and hexacoordinated globins may be rather small and can be overcome by external modifications such as high pressure. Over the pressure range 0.1-700 MPa (7 kbar), the globins may show a loss of over a factor of 100 in the amplitude of the b…

Models MolecularSteric effectsProtein ConformationStereochemistryIronNeuroglobinchemistry.chemical_elementNerve Tissue ProteinsHemeLigandsBiochemistryOxygenHemoglobinschemistry.chemical_compoundSolanum lycopersicumPressureAnimalsHumansHistidineHorsesGlobinMolecular BiologyHemeBinding SitesPhotolysisMyoglobinChemistryPhotodissociationHeartCell BiologyLigand (biochemistry)GlobinsOxygenKineticsNeuroglobinBiophysicsFlash photolysisProtein BindingJournal of Biological Chemistry
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Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family.

2001

Neuroglobin is a recently discovered member of the globin superfamily that is suggested to enhance the O(2) supply of the vertebrate brain. Spectral measurements with human and mouse recombinant neuroglobin provide evidence for a hexacoordinated deoxy ferrous (Fe(2+)) form, indicating a His-Fe(2+)-His binding scheme. O(2) or CO can displace the endogenous protein ligand, which is identified as the distal histidine by mutagenesis. The ferric (Fe(3+)) form of neuroglobin is also hexacoordinated with the protein ligand E7-His and does not exhibit pH dependence. Flash photolysis studies show a high recombination rate (k(on)) and a slow dissociation rate (k(off)) for both O(2) and CO, indicating…

Models MolecularTime FactorsLightStereochemistryIronNeuroglobinNerve Tissue ProteinsPlasma protein bindingLigandsBiochemistryMiceAnimalsHumansHistidineGlobinCloning MolecularMolecular BiologyHistidineChromatography High Pressure LiquidCarbon MonoxideChemistryCytoglobinTemperatureCell BiologyHydrogen-Ion ConcentrationLigand (biochemistry)Recombinant ProteinsGlobin foldGlobinsOxygenKineticsNeuroglobinOxidation-ReductionUltracentrifugationProtein ligandProtein BindingThe Journal of biological chemistry
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Redistribution of aquaporin-4 in human glioblastoma correlates with loss of agrin immunoreactivity from brain capillary basal laminae

2003

Vasogenic edema is one of the most serious clinical problems in brain tumors and tightly connected to water shifts between the different fluid compartments in the brain. Aquaporin water channels have been recognized to have an important impact on the development of edematous swelling in the brain. Astrocytes, which are believed to induce or at least maintain the blood-brain barrier in the brain capillary endothelial cells, express the aquaporin isoform AQP4. Normally, AQP4 is highly concentrated in the glial membrane where astrocytes contact mesenchymal space, such as perivascular or brain superficial regions. Parenchymal membranes do not show any immunocytochemical AQP4-specific signal. We…

Models NeurologicalSynucleinsAquaporinNerve Tissue ProteinsBiologyAquaporinsBlood–brain barrierBasement MembranePathology and Forensic MedicineCellular and Molecular NeuroscienceGliomaUtrophinmedicineExtracellularAnimalsHumansAgrinDystroglycansAquaporin 4Membrane GlycoproteinsAgrinBrain NeoplasmsEndothelial Cellsmedicine.diseaseImmunohistochemistryRatsCell biologyCytoskeletal Proteinsmedicine.anatomical_structureAquaporin 4Immunologysense organsNeurology (clinical)GlioblastomaAstrocyteActa Neuropathologica
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Interspecies comparison of neuroglobin, cytoglobin and myoglobin: Sequence evolution and candidate regulatory elements

2003

Neuroglobin and cytoglobin are two novel members of the vertebrate globin family. Their physiological role is poorly understood, although both proteins bind oxygen reversibly and may be involved in cellular oxygen homeostasis. Here we investigate the selective constraints on coding and non-coding sequences of the neuroglobin and cytoglobin genes in human, mouse, rat and fish. Neuroglobin and cytoglobin are highly conserved, displaying very low levels of non-synonymous nucleotide substitutions. An oxygen supply function predicts distinct modes of gene regulation, involving hypoxia-responsive transcription factors. To detect conserved candidate regulatory elements, we compared the neuroglobin…

Molecular Sequence DataNeuroglobinNerve Tissue ProteinsSequence alignmentRegulatory Sequences Nucleic AcidBiologyMiceSpecies SpecificityGeneticsAnimalsHumansGlobinMolecular BiologyGeneGenetics (clinical)MammalsGeneticsRegulation of gene expressionBinding SitesBase SequenceMyoglobinCytoglobinFishesDNAMRNA stabilizationBiological EvolutionGlobinsRatsOxygenGene Expression RegulationRegulatory sequenceNeuroglobinSequence AlignmentTranscription FactorsCytogenetic and Genome Research
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Genetic dissection of plexin signaling in vivo

2014

Mammalian plexins constitute a family of transmembrane receptors for semaphorins and represent critical regulators of various processes during development of the nervous, cardiovascular, skeletal, and renal system. In vitro studies have shown that plexins exert their effects via an intracellular R-Ras/M-Ras GTPase-activating protein (GAP) domain or by activation of RhoA through interaction with Rho guanine nucleotide exchange factor proteins. However, which of these signaling pathways are relevant for plexin functions in vivo is largely unknown. Using an allelic series of transgenic mice, we show that the GAP domain of plexins constitutes their key signaling module during development. Mice …

MultidisciplinaryRHOAanimal structuresbiologyTransgenePlexinMutantMice TransgenicNerve Tissue ProteinsBiological SciencesPhenotypeCell biologyMiceSemaphorinembryonic structuresbiology.proteinAnimalsGuanine nucleotide exchange factorSignal transductionSignal Transduction
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