Search results for "Retinitis"

showing 10 items of 92 documents

Molecular genetics of autosomal dominant retinitis pigmentosa (ADRP): a comprehensive study of 43 Italian families

2005

Retinitis pigmentosa is the most common form of retinal degeneration and is heterogeneous both clinically and genetically. The autosomal dominant forms ( ADRP) can be caused by mutations in 12 different genes. This report describes the first simultaneous mutation analysis of all the known ADRP genes in the same population, represented by 43 Italian families. This analysis allowed the identification of causative mutations in 12 of the families (28% of the total). Seven different mutations were identified, two of which are novel (458delC and 6901C --> T (P2301S), in the CRX and PRPF8 genes, respectively). Several novel polymorphisms leading to amino acid changes in the FSCN2, NRL, IMPDH1, and…

Retinal degenerationDNA Mutational Analysismedicine.disease_causeGene FrequencyPrevalenceAge of OnsetSPLICING-FACTOR GENESChildGenetics (clinical)Genes DominantGeneticsMutationeducation.field_of_studyRNA-Binding ProteinsMiddle AgedDNA-Binding ProteinsBasic-Leucine Zipper Transcription FactorsItalyChild PreschoolMESSENGER-RNAMicrotubule-Associated ProteinsRetinitis PigmentosaFORMAdultRhodopsinmedicine.medical_specialtycongenital hereditary and neonatal diseases and abnormalitiesAdolescentPopulationRHODOPSIN GENEBiologyMolecular geneticsRetinitis pigmentosaGeneticsmedicineHumansFamilyEye ProteinseducationGeneAllele frequencyHomeodomain ProteinsMUTATIONSmedicine.diseaseeye diseasesMutationTrans-ActivatorsMutation testingOnline Mutation ReportCarrier Proteins
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The mitotic spindle protein SPAG5/Astrin connects to the Usher protein network postmitotically

2011

Abstract Background Mutations in the gene for Usher syndrome 2A (USH2A) are causative for non-syndromic retinitis pigmentosa and Usher syndrome, a condition that is the most common cause of combined deaf-blindness. To gain insight into the molecular pathology underlying USH2A-associated retinal degeneration, we aimed to identify interacting proteins of USH2A isoform B (USH2AisoB) in the retina. Results We identified the centrosomal and microtubule-associated protein sperm-associated antigen (SPAG)5 in the retina. SPAG5 was also found to interact with another previously described USH2AisoB interaction partner: the centrosomal ninein-like protein NINLisoB. Using In situ hybridization, we foun…

Retinal degenerationGenetics and epigenetic pathways of disease [NCMLS 6]Usher syndromeBiologyPhotoreceptor cell03 medical and health sciences0302 clinical medicineMicrotubuleEvaluation of complex medical interventions Genomic disorders and inherited multi-system disorders [NCEBP 2]Retinitis pigmentosamedicineotorhinolaryngologic diseasesBasal bodylcsh:QH573-671Ganglion cell layer030304 developmental biologyGenetics0303 health sciencesRetinalcsh:CytologyResearchPathogenesis and modulation of inflammation Infection and autoimmunity [N4i 1]Cell Biologymedicine.diseaseGenetics and epigenetic pathways of disease Plasticity and memory [NCMLS 6]eye diseasesCell biologyGenetics and epigenetic pathways of disease DCN MP - Plasticity and memory [NCMLS 6]medicine.anatomical_structure030220 oncology & carcinogenesissense organs
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Disruption of the retinitis pigmentosa 28 gene Fam161a in mice affects photoreceptor ciliary structure and leads to progressive retinal degeneration.

2014

Mutations in the FAM161A gene were previously identified as the cause for autosomal-recessive retinitis pigmentosa 28. To study the effects of Fam161a dysfunction in vivo, we generated gene-trapped Fam161a(GT/GT) mice with a disruption of its C-terminal domain essential for protein-protein interactions. We confirmed the absence of the full-length Fam161a protein in the retina of Fam161a(GT/GT) mice using western blots and showed weak expression of a truncated Fam161a protein by immunohistochemistry. Histological analyses demonstrated that photoreceptor segments were disorganized in young Fam161a(GT/GT) mice and that the outer retina was completely lost at 6 months of age. Reactive microglia…

Retinal degenerationMaleOpsinGenotypeVision DisordersAction PotentialsGene ExpressionMice TransgenicRetinal Pigment EpitheliumBiologyRetinaMiceRetinitis pigmentosaGeneticsmedicineAnimalsHumansPhotoreceptor CellsPeripherin 2Eye ProteinsMolecular BiologyGenetics (clinical)Retinal regenerationRetinaGene therapy of the human retinaCiliumRetinal DegenerationGeneral Medicinemedicine.diseaseeye diseasesCell biologyProtein Transportmedicine.anatomical_structureGenetic LociGene TargetingMutationFemalesense organsMicrogliaCarrier ProteinsProtein BindingHuman molecular genetics
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A key role for cyclic nucleotide gated (CNG) channels in cGMP-related retinitis pigmentosa.

2011

The rd1 natural mutant is one of the first and probably the most commonly studied mouse model for retinitis pigmentosa (RP), a severe and frequently blinding human retinal degeneration. In several decades of research, the link between the increase in photoreceptor cGMP levels and the extremely rapid cell death gave rise to a number of hypotheses. Here, we provide clear evidence that the presence of cyclic nucleotide gated (CNG) channels in the outer segment membrane is the key to rod photoreceptor loss. In Cngb1(-/-) x rd1 double mutants devoid of regular CNG channels, cGMP levels are still pathologically high, but rod photoreceptor viability and outer segment morphology are greatly improve…

Retinal degenerationMaleProgrammed cell deathgenetic structuresMutantchemistry.chemical_elementCyclic Nucleotide-Gated Cation ChannelsNerve Tissue ProteinsCalciumBiologyCyclic nucleotidechemistry.chemical_compoundMiceRetinal Rod Photoreceptor CellsRetinitis pigmentosaGeneticsmedicineAnimalsHumansRod cellCyclic nucleotide-gated ion channelMolecular BiologyCyclic GMPGenetics (clinical)Mice KnockoutMice Inbred C3HGeneral MedicineAnatomymedicine.diseaseeye diseasesCell biologyMice Inbred C57BLDisease Models Animalmedicine.anatomical_structurechemistryCalciumFemalesense organsRetinitis PigmentosaHuman molecular genetics
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PRCD is concentrated at the base of photoreceptor outer segments and is involved in outer segment disc formation.

2019

Abstract Mutations of the PRCD gene are associated with rod-cone degeneration in both dogs and humans. Prcd is expressed in the mouse eye as early as embryonic day 14. In the adult mouse retina PRCD is expressed in the outer segments of both rod and cone photoreceptors. Immunoelectron microscopy revealed that PRCD is located at the outer segment rim, and that it is highly concentrated at the base of the outer segment. Prcd-knockout mice present with progressive retinal degeneration, starting at 20 weeks of age and onwards. This process is reflected by a significant and progressive reduction of both scotopic and photopic electroretinographic responses, and by thinning of the retina, and spec…

Retinal degenerationMalegenetic structuresImmunoelectron microscopyRetinal Pigment EpitheliumBiologyRetinachemistry.chemical_compoundMicePhagocytosisGeneticsmedicineAnimalsScotopic visionOuter nuclear layerEye ProteinsMolecular BiologyGenetics (clinical)Mice KnockoutRetinaRetinal DegenerationMembrane ProteinsRetinalGeneral Medicinemedicine.diseaseRod Cell Outer SegmentPhotoreceptor outer segmenteye diseasesCell biologyMice Inbred C57BLmedicine.anatomical_structurechemistryRetinal Cone Photoreceptor CellsFemalesense organsCone-Rod DystrophiesRetinitis PigmentosaPhotopic visionSignal TransductionHuman molecular genetics
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SANS (USH1G) expression in developing and mature mammalian retina

2008

AbstractThe human Usher syndrome (USH) is the most common form of combined deaf-blindness. Usher type I (USH1), the most severe form, is characterized by profound congenital deafness, constant vestibular dysfunction and prepubertal-onset of retinitis pigmentosa. Five corresponding genes of the six USH1 genes have been cloned so far. The USH1G gene encodes the SANS (scaffold protein containing ankyrin repeats and SAM domain) protein which consists of protein motifs known to mediate protein–protein interactions. Recent studies indicated SANS function as a scaffold protein in the protein interactome related to USH.Here, we generated specific antibodies for SANS protein expression analyses. Our…

Retinal degenerationScaffold proteinBlotting WesternNerve Tissue ProteinsBiologyRibbon synapseRats Inbred WKYPhotoreceptor cellRetinaMiceXenopus laevisAntibody SpecificityCiliogenesisConnecting ciliumRetinitis pigmentosamedicineAnimalsCiliaEye ProteinsCentrosomeRetinaCiliogenesisPhotoreceptor cellsCiliumImmune SeraCiliary BodyFibroblastsmedicine.diseaseSynapseSensory SystemsCell biologyRatsMice Inbred C57BLOphthalmologymedicine.anatomical_structureSynapsesRetinal developmentsense organsUsher SyndromesUsher syndromePhotoreceptor Cells VertebrateSynaptosomesVision Research
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Retinal Sensibility to Drugs in Normal Rats and Carriers of Inherited Retinal Degeneration

1972

Secondary retinitis pigmentosa of pseudo-retinitis pigmentosa can be brought about by certain diseases, especially exanthematic or viral ones.

Retinal degenerationcongenital hereditary and neonatal diseases and abnormalitiesmedicine.medical_specialtygenetic structuresmedicine.diagnostic_testbusiness.industryRetinalmedicine.diseaseeye diseaseschemistry.chemical_compoundchemistryOphthalmologyRetinitis pigmentosaotorhinolaryngologic diseasesMedicinesense organsbusinessElectroretinography
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Phosphodiesterase inhibition induces retinal degeneration, oxidative stress and inflammation in cone-enriched cultures of porcine retina.

2013

nherited retinal degenerations affecting both rod and cone photoreceptors constitute one of the causes 74 of incurable blindness in the developed world. Cyclic guanosine monophosphate (cGMP) is crucial in the 75 phototransduction and, mutations in genes related to its metabolism are responsible for different retinal 76 dystrophies. cGMP-degrading phosphodiesterase 6 (PDE6) mutations cause around 4e5% of the retinitis 77 pigmentosa, a rare form of retinal degeneration. The aim of this study was to evaluate whether phar- 78 macological PDE6 inhibition induced retinal degeneration in cone-enriched cultures of porcine retina 79 similar to that found in murine models. PDE6 inhibition was induced…

Retinal degenerationgenetic structuresPurinonesPhosphodiesterase InhibitorsSwineEstrès oxidatiuApoptosisBiologyRetinaCellular and Molecular Neurosciencechemistry.chemical_compoundOrgan Culture TechniquesRetinitis pigmentosamedicineIn Situ Nick-End LabelingAnimalsNeurociènciesCyclic GMPRetinaCalpainCaspase 3Retinal DegenerationPhosphodiesteraseRetinalmedicine.diseaseMolecular biologySensory SystemsOphthalmologyOxidative Stressmedicine.anatomical_structurechemistryBiochemistryRetinal Cone Photoreceptor CellsSwine Miniaturesense organsZaprinastRetinal DystrophiesRetinitis PigmentosaVisual phototransduction
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Rhodopsin transport in the membrane of the connecting cilium of mammalian photoreceptor cells

2000

The transport of the photopigment rhodopsin from the inner segment to the photosensitive outer segment of vertebrate photoreceptor cells has been one of the main remaining mysteries in photoreceptor cell biology. Because of the lack of any direct evidence for the pathway through the photoreceptor cilium, alternative extracellular pathways have been proposed. Our primary aim in the present study was to resolve rhodopsin trafficking from the inner to the outer segment. We demonstrate, predominantly by high-sensitive immunoelectron microscopy, that rhodopsin is also densely packed in the membrane of the photoreceptor connecting cilium. Present prominent labeling of rhodopsin in the ciliary mem…

RhodopsinOpsingenetic structuresPhotoreceptor Connecting CiliumImmunoblottingMolecular Sequence Datamacromolecular substancesMyosinsBiologyPhotoreceptor cellRats Sprague-DawleyMiceRetinal Rod Photoreceptor CellsStructural BiologymedicineAnimalsHumansPhotopigmentAmino Acid SequenceCiliaMicroscopy ImmunoelectronCiliary membraneCiliumRod OpsinsAntibodies MonoclonalDyneinsBiological TransportCell BiologyMiddle AgedRod Cell Outer SegmentActin cytoskeletonImmunohistochemistryActinseye diseasesRatsCell biologyMice Inbred C57BLmedicine.anatomical_structureRhodopsinMyosin VIIabiology.proteinCattleFemalesense organsRetinitis PigmentosaCell Motility and the Cytoskeleton
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Peripherin-2 couples rhodopsin to the CNG channel in outer segments of rod photoreceptors.

2014

Outer segments (OS) of rod photoreceptors are cellular compartments specialized in the conversion of light into electrical signals. This process relies on the light-triggered change in the intracellular levels of cyclic guanosine monophosphate (cGMP), which in turn controls the activity of cyclic nucleotide-gated (CNG) channels in the rod OS plasma membrane. The rod CNG channel is a macromolecular complex that in its core harbors the ion-conducting CNGA1 and CNGB1a subunits. To identify additional proteins of the complex that interact with the CNGB1a core subunit we applied affinity purification of mouse retinal proteins followed by mass spectrometry. In combination with in vitro and in viv…

Rhodopsingenetic structuresImmunoelectron microscopyProtein subunitPeripherinsCyclic Nucleotide-Gated Cation ChannelsNerve Tissue ProteinsBiologyRetinaCell membraneMiceRetinal Rod Photoreceptor CellsRetinitis pigmentosaGeneticsmedicineAnimalsHumansPeripherin 2Molecular BiologyGenetics (clinical)General MedicineAnatomyRetinal Photoreceptor Cell Outer Segmentmedicine.diseaseProtein Structure TertiaryTransmembrane domainmedicine.anatomical_structureFörster resonance energy transferRhodopsinbiology.proteinBiophysicssense organsRetinitis PigmentosaProtein Binding
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