Search results for "Photoreceptor Cells"

showing 10 items of 99 documents

Different roles for KIF17 and kinesin II in photoreceptor development and maintenance.

2009

Kinesin 2 family members are involved in transport along ciliary microtubules. In Caenorhabditis elegans channel cilia, kinesin II and OSM-3 cooperate along microtubule doublets of the axoneme middle segment, whereas OSM-3 alone works on microtubule singlets to elongate the distal segment. Among sensory cilia, vertebrate photoreceptors share a similar axonemal structure with C. elegans channel cilia, and deficiency in either kinesin II or KIF17, the homologue of OSM-3, results in disruption of photoreceptor organization. However, direct comparison of the two effects is confounded by the use of different species and knockdown strategies in prior studies. Here, we directly compare the effects…

AxonemeEmbryo NonmammalianBlotting WesternKinesinsBiologyArticleMiceMicroscopy Electron TransmissionMicrotubuleCiliogenesisAnimalsImmunoprecipitationKinesin 8Microscopy ImmunoelectronZebrafishZebrafishKIF17CiliumfungiZebrafish Proteinsbiology.organism_classificationImmunohistochemistryCell biologyRetinal Cone Photoreceptor CellsKinesinsense organsDevelopmental BiologyDevelopmental dynamics : an official publication of the American Association of Anatomists
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A novel function of Huntingtin in the cilium and retinal ciliopathy in Huntington's disease mice

2015

Huntington's disease (HD) is a neurodegenerative disorder caused by the toxic expansion of polyglutamine in the Huntingtin (HTT) protein. The pathomechanism is complex and not fully understood. Increasing evidence indicates that the loss of normal protein function also contributes to the pathogenesis, pointing out the importance of understanding the physiological roles of HTT. We provide evidence for a novel function of HTT in the cilium. HTT localizes in diverse types of cilia — including 9 + 0 non-motile sensory cilia of neurons and 9 + 2 motile multicilia of trachea and ependymal cells — which exert various functions during tissue development and homeostasis. In the photoreceptor cilium,…

AxonemeMalecongenital hereditary and neonatal diseases and abnormalitiesHuntingtinCentrioleMice TransgenicNerve Tissue ProteinsBiologyMicrotubulesPhotoreceptor cellRetinalcsh:RC321-571MiceHuntington's diseaseIntraflagellar transportmental disordersmedicineAnimalsHumansPhotoreceptor CellsHuntingtinCilialcsh:Neurosciences. Biological psychiatry. NeuropsychiatryComputingMilieux_MISCELLANEOUSHuntingtin ProteinPhotoreceptorCiliumNuclear ProteinsHuntington's diseasemedicine.diseaseCell biologyCiliopathyDisease Models Animalmedicine.anatomical_structureHEK293 CellsHuntington DiseaseNeurologyFemale[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]sense organs
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Early adaptive response of the retina to a pro-diabetogenic diet: Impairment of cone response and gene expression changes in high-fructose fed rats

2015

The lack of plasticity of neurons to respond to dietary changes, such as high fat and high fructose diets, by modulating gene and protein expression has been associated with functional and behavioral impairments that can have detrimental consequences. The inhibition of high fat-induced rewiring of hypothalamic neurons induced obesity. Feeding rodents with high fructose is a recognized and widely used model to trigger obesity and metabolic syndrome. However the adaptive response of the retina to short term feeding with high fructose is poorly documented. We therefore aimed to characterize both the functional and gene expression changes in the neurosensory retina of Brown Norway rats fed duri…

Blood GlucoseLeptinMalemedicine.medical_specialtyretinamedicine.medical_treatment[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionEukaryotic Initiation Factor-2BiologyDiabetes Mellitus ExperimentalfructoseCellular and Molecular Neurosciencechemistry.chemical_compoundDownregulation and upregulationInternal medicineGene expressionDietary CarbohydratesmedicineAnimalsInsulin[SDV.MHEP.OS]Life Sciences [q-bio]/Human health and pathology/Sensory Organs2. Zero hungerRetinamedicine.diagnostic_testGene Expression ProfilingLeptinInsulinFructoseEndoplasmic Reticulum Stressmedicine.diseaseCrystallinsSensory SystemsRatsOphthalmologyCholesterolmedicine.anatomical_structureEndocrinologyGene Expression Regulationchemistry[ SDV.MHEP.OS ] Life Sciences [q-bio]/Human health and pathology/Sensory OrgansFructosamineRetinal Cone Photoreceptor Cellsgene expressionsense organsMetabolic syndromeelectroretinographydiet[SDV.AEN]Life Sciences [q-bio]/Food and NutritionElectroretinography
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The translocation of signaling molecules in dark adapting mammalian rod photoreceptor cells is dependent on the cytoskeleton.

2008

In vertebrate rod photoreceptor cells, arrestin and the visual G-protein transducin move between the inner segment and outer segment in response to changes in light. This stimulus dependent translocation of signalling molecules is assumed to participate in long term light adaptation of photoreceptors. So far the cellular basis for the transport mechanisms underlying these intracellular movements remains largely elusive. Here we investigated the dependency of these movements on actin filaments and the microtubule cytoskeleton of photoreceptor cells. Co-cultures of mouse retina and retinal pigment epithelium were incubated with drugs stabilizing and destabilizing the cytoskeleton. The actin a…

Cell signalingCytochalasin Dgenetic structuresLightPaclitaxelPhalloidineDark AdaptationBiologyHeterocyclic Compounds 4 or More RingsMicrotubulesRetinaMiceStructural BiologyMicrotubuleRetinal Rod Photoreceptor CellsCytoskeletal drugsThiabendazolemedicineArrestinAnimalsTransducinCytoskeletonMicroscopy ImmunoelectronActinCytoskeletonVision OcularMice KnockoutRetinal pigment epitheliumArrestinHomozygoteCell BiologyDarknessRod Cell Outer Segmenteye diseasesActinsCell biologyMice Inbred C57BLActin CytoskeletonProtein Transportmedicine.anatomical_structureMicroscopy Fluorescencesense organsTransducinCell Migration AssaysSignal TransductionCell motility and the cytoskeleton
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Characterisation, analysis of expression and localisation of the opsin gene repertoire from the perspective of photoperiodism in the aphid Acyrthosip…

2017

Organisms exhibit a wide range of seasonal responses as adaptions to predictable annual changes in their environment. These changes are originally caused by the effect of the Earth's cycles around the sun and its axial tilt. Examples of seasonal responses include floration, migration, reproduction and diapause. In temperate climate zones, the most robust variable to predict seasons is the length of the day (i.e. the photoperiod). The first step to trigger photoperiodic driven responses involves measuring the duration of the light-dark phases, but the molecular clockwork performing this task is poorly characterized. Photopigments such as opsins are known to participate in light perception, b…

Central Nervous SystemNymph0301 basic medicineOpsinPhysiologyPhotoperiodGene ExpressionDiapauseBiologyPolymerase Chain Reaction03 medical and health sciences0302 clinical medicineAnimalsPhotopigmentAmino Acid SequencePhylogenyphotoperiodismAphidOpsinsGene Expression Profilingfood and beveragesAphididaebiology.organism_classificationHemipteraAcyrthosiphon pisum030104 developmental biologyEvolutionary biologyAphidsInsect ScienceInsect ProteinsFemalePhotoreceptor Cells InvertebrateSequence Alignment030217 neurology & neurosurgeryJournal of Insect Physiology
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The muscleblind gene participates in the organization of Z-bands and epidermal attachments of Drosophila muscles and is regulated by Dmef2.

1998

We report the embryonic phenotype of muscleblind (mbl), a recently described Drosophila gene involved in terminal differentiation of adult ommatidia. mbl is a nuclear protein expressed late in the embryo in pharyngeal, visceral, and somatic muscles, the ventral nerve cord, and the larval photoreceptor system. All three mbl alleles studied exhibit a lethal phenotype and die as stage 17 embryos or first instar larvae. These larvae are partially paralyzed, show a characteristically contracted abdomen, and lack striation of muscles. Our analysis of the somatic musculature shows that the pattern of muscles is established correctly, and they form morphologically normal synapses. Ultrastructural a…

Central Nervous SystemSomatic cellMuscle Fibers SkeletalNeuromuscular JunctionMuscle ProteinsGenes InsectBiologymuscle attachmentsmuscleblindMesodermTendonsEctodermAnimalsDrosophila ProteinsConnectinRNA MessengerNuclear proteinMuscle SkeletalMolecular BiologyZ-bandsCell NucleusEpidermis (botany)MyogenesisMEF2 Transcription FactorsDrosophila.Gene Expression Regulation DevelopmentalNuclear ProteinsEmbryoCell DifferentiationCell BiologyAnatomybacterial infections and mycosesEmbryonic stem cellPhenotypeCell biologyDNA-Binding ProteinsMyogenic Regulatory FactorsVentral nerve cordMutationInsect ProteinsDrosophilaPhotoreceptor Cells InvertebratemyogenesisDevelopmental BiologyTranscription FactorsDevelopmental biology
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The retinitis pigmentosa 28 protein FAM161A is a novel ciliary protein involved in intermolecular protein interaction and microtubule association

2012

Loss-of-function mutations in the gene encoding FAM161A were recently discovered as the cause for RP28, an autosomal recessive form of retinitis pigmentosa. To initiate the characterization of the cellular role of FAM161A in the retina, we focused on its subcellular localization and conducted in vitro studies to identify FAM161A-interacting proteins and associated cellular structures. Immunohistochemistry revealed the presence of mouse FAM161A in the photoreceptor inner segments, the synaptic regions of the outer and inner plexiform layers and the ganglion cells. In mouse and human retinal sections from unfixed eyes, FAM161A localized to the ciliary region linking photoreceptor outer and in…

CentrioleImmunoelectron microscopyBiologyMicrotubulesRetinaMice03 medical and health sciences0302 clinical medicineMicrotubuleRetinitis pigmentosaGeneticsmedicineAnimalsHumansBasal bodyPhotoreceptor CellsEye ProteinsMolecular BiologyGenetics (clinical)030304 developmental biologyCentrosome0303 health sciencesRetinaCiliumGeneral Medicinemedicine.diseaseCell biologymedicine.anatomical_structureCentrosomeMutationsense organsRetinitis Pigmentosa030217 neurology & neurosurgeryHuman Molecular Genetics
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The retinitis pigmentosa protein RP2 links pericentriolar vesicle transport between the Golgi and the primary cilium.

2010

Photoreceptors are complex ciliated sensory neurons. The basal body and periciliary ridge of photoreceptors function in association with the Golgi complex to regulate the export of proteins from the inner segment to the outer segment sensory axoneme. Here, we show that the retinitis pigmentosa protein RP2, which is a GTPase activating protein (GAP) for Arl3, localizes to the ciliary apparatus, namely the basal body and the associated centriole at the base of the photoreceptor cilium. Targeting to the ciliary base was dependent on N-terminal myristoylation. RP2 also localized to the Golgi and periciliary ridge of photoreceptors, which suggested a role for RP2 in regulating vesicle traffic an…

CentriolePhotoreceptor Connecting CiliumGolgi ApparatusBiologysymbols.namesakeMiceIntraflagellar transportGTP-Binding ProteinsGeneticsBasal bodyAnimalsHumansKIF3APhotoreceptor CellsCiliaEye ProteinsTransport VesiclesMolecular BiologyGenetics (clinical)Cells CulturedCentriolesADP-Ribosylation FactorsCiliumCiliary BodyIntracellular Signaling Peptides and ProteinsMembrane ProteinsBiological TransportGeneral MedicineGolgi apparatusCell biologysymbolssense organsCiliary baseRetinitis PigmentosaHuman molecular genetics
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Chlamydomonas reinhardtii in the landscape of pigments.

2004

▪ Abstract  This review focuses on the biosynthesis of pigments in the unicellular alga Chlamydomonas reinhardtii and their physiological and regulatory functions in the context of information gathered from studies of other photosynthetic organisms. C. reinhardtii is serving as an important model organism for studies of photosynthesis and the pigments associated with the photosynthetic apparatus. Despite extensive information pertaining to the biosynthetic pathways critical for making chlorophylls and carotenoids, we are just beginning to understand the control of these pathways, the coordination between pigment and apoprotein synthesis, and the interactions between the activities of these…

ChlorophyllRhodopsinNuclear geneChloroplastsved/biology.organism_classification_rank.speciesLight-Harvesting Protein ComplexesProtozoan ProteinsChlamydomonas reinhardtiiPhotosynthesisModels Biologicalchemistry.chemical_compoundHemiterpenesLycopeneBiosynthesisIsomerismPentanesBotanyGeneticsButadienesAnimalsPhotosynthesisModel organismCarotenoidPlant Proteinschemistry.chemical_classificationCell Nucleusbiologyved/biologyPigments Biologicalbiology.organism_classificationCarotenoidsChloroplastOxygenCytochrome b6f ComplexchemistryBiochemistryXanthophyllPhotoreceptor Cells InvertebrateChlamydomonas reinhardtiiAnnual review of genetics
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Light-Dependent Translocation of Arrestin in Rod Photoreceptors is Signaled through a Phospholipase C Cascade and Requires ATP

2009

Light adaptation of rod photoreceptors induces translocation of arrestin from inner segments (IS) to outer segments (OS). Our study suggests that components of the G-protein linked phosphoinositide pathway play a role in signaling the initiating events of arrestin translocation. We show that arrestin translocation can be stimulated by activators of phospholipase C (PLC) and protein kinase C (PKC) in the absence of light. Conversely, arrestin translocation to the OS is significantly slowed by inhibitors of PLC and PKC.In the second part of this study, we investigated the mechanism by which arrestin translocates in response to light. Other investigators have suggested that arrestin translocat…

Cholera ToxinLightgenetic structuresG proteinBiophysicsXenopusChromosomal translocationBiologyPhosphatidylinositolsArticleMiceXenopus laevisAdenosine TriphosphateRetinal Rod Photoreceptor CellsArrestinAnimalsEnzyme InhibitorsPotassium CyanideCells CulturedProtein Kinase CProtein kinase CArrestinPhosphoinositide PathwayPhospholipase CChemistryCell Biologybiology.organism_classificationeye diseasesCell biologyRhodopsinType C Phospholipasesbiology.proteinPhosphorylationArrestin beta 2Arrestin beta 1sense organsSignal transductionSignal TransductionBiophysical Journal
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