Search results for "Nerve Tissue Protein"

showing 10 items of 345 documents

optomotor-blind suppresses instability at the A/P compartment boundary of the Drosophila wing.

2008

Formation and function of the A/P compartment boundary of the Drosophila wing have been studied intensely. The boundary prevents mingling of A and P cells, is characterized by an expression discontinuity of several genes like engrailed, Cubitus interruptus, hedgehog and decapentaplegic and is essential for patterning the wing. Compared with segmental or compartmental boundaries in several other systems which generally manifest as folds or clefts, the wing A/P boundary is morphologically inconspicuous in both the larval and adult stage. We show here that the Drosophila wing A/P boundary, too, is susceptible to fold and cleft formation and that these processes are suppressed by the T-box tran…

GeneticsEmbryologyanimal structuresWingDecapentaplegicMorphogenesisGene Expression Regulation DevelopmentalNerve Tissue ProteinsBiologyMicrotubulesengrailedCell biologyAdherens junctionCompartment (development)AnimalsDrosophila ProteinsWings AnimalDrosophilaEnhancerT-Box Domain ProteinsHedgehogDevelopmental BiologyBody PatterningSequence DeletionMechanisms of development
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Spatial discontinuity of Optomotor-blind expression in the Drosophila wing imaginal disc disrupts epithelial architecture and promotes cell sorting

2010

Abstract Background Decapentaplegic (Dpp) is one of the best characterized morphogens, required for dorso-ventral patterning of the Drosophila embryo and for anterior-posterior (A/P) patterning of the wing imaginal disc. In the larval wing pouch, the Dpp target gene optomotor-blind (omb) is generally assumed to be expressed in a step function above a certain threshold of Dpp signaling activity. Results We show that the transcription factor Omb forms, in fact, a symmetrical gradient on both sides of the A/P compartment boundary. Disruptions of the Omb gradient lead to a re-organization of the epithelial cytoskeleton and to a retraction of cells toward the basal membrane suggesting that the O…

GeneticsWinganimal structuresbiologyDecapentaplegicMorphogenesisNerve Tissue ProteinsCell sortingbiology.organism_classificationCell biologyImaginal discDrosophila melanogasterlcsh:Biology (General)Research articleAnimalsDrosophila ProteinsWings AnimalCompartment (development)Drosophila melanogasterT-Box Domain Proteinslcsh:QH301-705.5Drosophila ProteinSignal TransductionDevelopmental BiologyBMC Developmental Biology
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Genome-wide association analysis on normal hearing function identifies PCDH20 and SLC28A3 as candidates for hearing function and loss.

2015

Hearing loss and individual differences in normal hearing both have a substantial genetic basis. Although many new genes contributing to deafness have been identified, very little is known about genes/variants modulating the normal range of hearing ability. To fill this gap, we performed a two-stage meta-analysis on hearing thresholds (tested at 0.25, 0.5, 1, 2, 4, 8 kHz) and on pure-tone averages (low-, medium-and high-frequency thresholds grouped) in several isolated populations from Italy and Central Asia (total N = 2636). Here, we detected two genome-wide significant loci close to PCDH20 and SLC28A3 (top hits: rs78043697, P = 4.71E-10 and rs7032430, P = 2.39E-09, respectively). For both…

Genome-wide association studieLOCICOMMON DISEASESNerve Tissue ProteinsVARIANTSSUSCEPTIBILITYDeafnessGenome-wide association studiesMiceHearingGenome-wide association studies; normal hearing function; PCDH20; SLC28A3PCDH20SLC28A3otorhinolaryngologic diseasesAnimalsHumansGenetic Predisposition to DiseaseMETAANALYSISHair Cells Auditory InnerSequence Analysis RNAAssociation Studies ArticlesMembrane Transport ProteinsLOCALIZATIONCadherinsTRANSPORTER-3ProtocadherinsGENOTYPEMYOSIN-VIIAItalyAsia Centralnormal hearing function3111 BiomedicineGenome-Wide Association StudyHuman molecular genetics
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Taste, movement, and death: varying effects of new prospero mutants during Drosophila development

2003

0022-3034 (Print) Comparative Study Journal Article Research Support, Non-U.S. Gov't; The PGal4 transposon inserted upstream of the pan-neural gene prospero (pros) causes several neural and behavioral defects in the Voila(1) strain. The precise excision of the transposon simultaneously rescued all these defects whereas its unprecise excision created new pros(V) alleles, including the null allele pros(V17). Here, we describe the relationship between the genetic structure of pros locus, larval locomotion, and larval gustatory response. These two behaviors showed varying degrees of variation depending upon the pros allele. We also found a good relation between behavioral alteration, the level …

GenotypeNerve Tissue Proteins/*genetics/metabolismeducationLethalMovement/*physiologyTaste/*geneticsDrosophila melanogaster/embryology/genetics/growth & developmentReaction TimeAnimalsDrosophila ProteinsNeuromuscular Junction/genetics/growth & development/metabolismSouthernLarva/genetics/*growth & developmentAllelesNonmammalianNuclear Proteins/*genetics/metabolismBlottingDevelopmental/physiologyImmunohistochemistryhumanitiesGenomics/methodsDeathInvertebrate/chemistryGene Expression RegulationGenesEmbryoMutationDNA Transposable ElementsGangliaInsectTranscription Factors
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Zebrafish Reveals Different and Conserved Features of Vertebrate Neuroglobin Gene Structure, Expression Pattern, and Ligand Binding

2004

Neuroglobin has been identified as a respiratory protein that is primarily expressed in the mammalian nervous system. Here we present the first detailed analysis of neuroglobin from a non-mammalian vertebrate, the zebrafish Danio rerio. The zebrafish neuroglobin gene reveals a mammalian-type exon-intron pattern in the coding region (B12.2, E11.0, and G7.0), plus an additional 5'-non-coding exon. Similar to the mammalian neuroglobin, the zebrafish protein displays a hexacoordinate deoxy-binding scheme. Flash photolysis kinetics show the competitive binding on the millisecond timescale of external ligands and the distal histidine, resulting in an oxygen affinity of 1 torr. Western blotting, i…

GillsDNA Complementaryanimal structuresBlotting WesternDanioNeuroglobinNerve Tissue ProteinsIn situ hybridizationBiologyLigandsBinding CompetitiveBiochemistryRetinaDiffusionExonChloridesAnimalsCoding regionHistidineRNA MessengerCloning MolecularMolecular BiologyZebrafishConserved SequenceIn Situ HybridizationZebrafishMessenger RNAModels GeneticExonsOlfactory PathwaysCell Biologybiology.organism_classificationMolecular biologyIntronsRecombinant ProteinsGlobinsMitochondriaCell biologyOxygenRespiratory proteinKineticsGene Expression RegulationMicroscopy FluorescenceSpectrophotometryNeuroglobinJournal of Biological Chemistry
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Screening of the USH1G gene among Spanish patients with Usher syndrome. Lack of mutations and evidence of a minor role in the pathogenesis of the syn…

2007

The Usher syndrome (USH) is an autosomal recessive hereditary disorder characterized by the association of sensorineural hearing loss, retinitis pigmentosa (RP) and, in some cases, vestibular dysfunction. The USH1G gene, encoding SANS, has been found to cause both Usher syndrome type I and atypical Usher syndrome. 109 Spanish unrelated patients suffering from Usher syndrome type I, type II, type III and unclassified Usher syndrome were screened for mutations in this gene, but only eight different changes without a clear pathogenic effect have been detected. Based on these results as well as previous studies in other populations where mutational analysis of this gene has been carried out, on…

Hearing lossUsher syndromeDNA Mutational AnalysisMolecular Sequence DataNerve Tissue ProteinsPathogenesisRetinitis pigmentosaotorhinolaryngologic diseasesmedicineHumansAmino Acid SequenceGenetic TestingGeneGenetics (clinical)Geneticsbusiness.industrymedicine.diseaseeye diseasesMutational analysisOphthalmologySpainPediatrics Perinatology and Child HealthMutationSensorineural hearing lossmedicine.symptombusinessUsher SyndromesUSH1G GENEOphthalmic genetics
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Cyanide binding and heme cavity conformational transitions in **Drosophila melanogaster** hexacoordinate hemoglobin

2006

The reason for the presence of hemoglobin-like molecules in insects, such as Drosophila melanogaster, that live in fully aerobic environments has yet to be determined. Heme endogenous hexacoordination (where HisE7 and HisF8 axial ligands to the heme Fe atom are both provided by the protein) is a recently discovered mechanism proposed to modulate O-2 affinity in hemoglobins from different species. Previous results have shown that D. melanogaster hemoglobin 1 (product of the glob1 gene) displays heme endogenous hexacoordination in both the ferrous and ferric states. Here we present kinetic data characterizing the exogenous cyanide ligand binding process, and the three-dimensional structure (a…

HemeproteinStereochemistryProtein ConformationCyanideMolecular Sequence DataNeuroglobinNerve Tissue ProteinsHemeCrystallography X-RayLigandsBiochemistrychemistry.chemical_compoundHemoglobinsMiceSequence Analysis ProteinMelanogasterAnimalsDrosophila ProteinsHumansCRYSTAL-STRUCTUREHistidineHemeBinding SitesCyanidesbiologyCytoglobinCytoglobinHexacoordinatebiology.organism_classificationGlobinsFERRIC APLYSIAKineticsDrosophila melanogasterchemistryHUMAN NEUROGLOBINAPLYSIA-LIMACINA MYOGLOBINX-RAYHemoglobinDrosophila melanogaster
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Neuroglobin and cytoglobin in search of their role in the vertebrate globin family

2004

Neuroglobin and cytoglobin are two recent additions to the family of heme-containing respiratory proteins of man and other vertebrates. Here, we review the present state of knowledge of the structures, ligand binding kinetics, evolution and expression patterns of these two proteins. These data provide a first glimpse into the possible physiological roles of these globins in the animal's metabolism. Both, neuroglobin and cytoglobin are structurally similar to myoglobin, although they contain distinct cavities that may be instrumental in ligand binding. Kinetic and structural studies show that neuroglobin and cytoglobin belong to the class of hexa-coordinated globins with a biphasic ligand-bi…

HemeproteinsModels MolecularCell typeProtein ConformationMolecular Sequence DataNeuroglobinNerve Tissue ProteinsBiochemistryInorganic Chemistrychemistry.chemical_compoundOxygen homeostasisAnimalsHumansGlobinAmino Acid SequencePhylogenyRegulation of gene expressionChemistryCytoglobinCytoglobinMolecular biologyCell biologyGlobinsMyoglobinGene Expression RegulationNeuroglobinSequence AlignmentFunction (biology)
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AAV Vector–mediated RNAi of Mutant Huntingtin Expression Is Neuroprotective in a Novel Genetic Rat Model of Huntington's Disease

2008

We report the characterization of a new rapid-onset model of Huntington's disease (HD) generated by adeno-associated virus (AAV) vector–mediated gene transfer of N-terminal huntingtin (htt) constructs into the rat striatum. Expression of exon 1 of mutant htt containing 70 CAG repeats rapidly led to neuropathological features associated with HD. In addition, we report novel data relating to neuronal transduction of AAV vectors that modulated the phenotype observed in this model. Quantitative reverse transcriptase–polymerase chain reaction (RT–PCR) revealed that AAV vector–mediated expression in the striatum increased by >100-fold as compared to the endogenous htt level. Moreover, AAV vectors…

HuntingtinvirusesGenetic VectorsNerve Tissue ProteinsSubstantia nigraBiologyArticleViral vectorHuntington's diseaseRNA interferenceDrug DiscoverymedicineHuntingtin ProteinGeneticsAnimalsHumansMolecular BiologyNeuronsPharmacologyHuntingtin ProteinGene knockdownReverse Transcriptase Polymerase Chain ReactionNeurodegenerationNuclear ProteinsExonsGenetic TherapyDependovirusmedicine.diseaseMolecular biologyCorpus StriatumRatsHuntington DiseaseNeuroprotective AgentsPhenotypenervous systemMolecular MedicineRNA InterferenceMolecular Therapy
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Post-translational modifications in the survival motor neuron protein

2004

Spinal muscular atrophy (SMA) is an autosomal recessive disease characterized by a progressive loss of the spinal motoneurons. The SMA-determining gene has been termed survival motor neuron (SMN) and is deleted or mutated in over 98% of patients. The encoded gene product is a protein expressed as different isoforms. In particular, we showed that the rat SMN cDNA produces two isoforms with Mr of 32 and 35 kDa, both localized in nuclear coiled bodies, but the 32 kDa form is also cytoplasmic, whereas the 35 kDa form is also microsomal. To determine the molecular relationship between these two isoforms and potential post-translational modifications, we performed transfection experiments with a …

INVOLVEMENTFORMSPRODUCTBiochemistryMiceChlorocebus aethiopsProtein IsoformsPhosphorylationCyclic AMP Response Element-Binding ProteinSMN PROTEINCells CulturedMotor NeuronsSPINAL MUSCULAR-ATROPHYRNA-Binding ProteinsSMN Complex Proteins3T3 CellsTransfectionmedicine.anatomical_structureSpinal CordCOS CellsSUBCELLULAR-LOCALIZATIONEXPRESSIONGene isoformRecombinant Fusion ProteinsBiophysicsNerve Tissue ProteinsBiologyMuscular Atrophy SpinalGene productSMN Complex ProteinsComplementary DNAmedicineAnimalsHumansMolecular BiologyCell BiologySpinal muscular atrophyMotor neuronmedicine.diseaseSurvival of Motor Neuron 1 ProteinMolecular biologyRatsnervous system diseasesMolecular WeightSEVERITYnervous systemBODIESProtein Processing Post-TranslationalDETERMINING GENEImmunostainingBiochemical and Biophysical Research Communications
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