Search results for "Eye"

showing 10 items of 2511 documents

Diagnostic morphology of human eye-related storage disorders

1989

While retina and other ocular tissues are involved clinically and morphologically in a variety of lysosomal disorders, it is only the conjunctiva that is accessible by biopsy to morphological, i.e., electron microscopic recognition of the patient's individual lysosomal disease. However, this procedure is not utilized by many. Instead, skin and circulating lymphocytes are the most frequently obtained tissues for diagnostic investigation, as skin contains an abundance of diversified cell types for morphological examination and simultaneously fibroblasts to be cultured for biochemical investigation. It is the tissue most suitable for identifying lysosomal disorders and parallels in diagnostic …

Cell typePathologymedicine.medical_specialtyConjunctivaEye DiseasesDiseaseBiologyRetinaBiopsymedicineHumansPeripheral NervesElectron microscopicGenetics (clinical)SkinRetinaBlood Cellsmedicine.diagnostic_testMusclesNeuropathologistBrainSkeletal muscleOphthalmologymedicine.anatomical_structureLiverPediatrics Perinatology and Child HealthKidney DiseasesMetabolism Inborn ErrorsOphthalmic Paediatrics and Genetics
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Multiple signal transduction pathways regulate clusterin (gp 80) gene expression in MDCK cells

1996

ABSTRACT Clusterin (gp 80, apolipoprotein J, TRPM-2) is a widely expressed multifunctional glycoprotein. Its demonstrated and proposed functions include the transport of lipids and membrane fragments, the inhibition of the cytolytic action of the terminal complement complex and the modulation of cell—cell interactions. The expression of the gene is enhanced during tissue injury and remodelling and by hormone-withdrawal-induced apoptosis of prostate and mammary cells. We show here that, in the kidney-derived epithelial cell line MDCK, clusterin mRNA is repressed by glucocorticoids and by progesterone. Treatment with epidermal growth factor also represses clusterin gene expression in MDCK cel…

Cell typeTranscription GeneticKidneyDexamethasoneEpitheliumCell LineAlkaloidsDogsEndocrinologyEpidermal growth factor1-Methyl-3-isobutylxanthineGene expressionCyclic AMPAnimalsRNA MessengerEnzyme InhibitorsAldosteroneMolecular BiologyProgesteroneProtein Kinase CProtein kinase CGlycoproteinsBenzophenanthridinesMessenger RNAEpidermal Growth FactorClusterinbiologyChemistryMolecular biologyeye diseasesPhenanthridinesCell biologyKineticsClusterinCell culturebiology.proteinTetradecanoylphorbol Acetatesense organsSignal transductionMolecular ChaperonesSignal TransductionJournal of Molecular Endocrinology
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Oxysterols: Influence on plasma membrane rafts microdomains and development of ocular diseases

2015

Oxidation of cholesterol into oxysterols is a major way of elimination of cholesterol from the liver and extrahepatic tissues, including the brain and the retina. Oxysterols are involved in various cellular processes. Numerous links have been established between oxysterols and several disorders such as neurodegenerative pathologies, retinopathies and atherosclerosis. Different components of the lipid layer such as sphingolipids, sterols and proteins participate to membrane fluidity and forme lipid rafts microdomains. Few data are available on the links between lipids rafts and oxysterols. The purpose of this review is to suggest the potential role of lipid rafts microdomains in the developm…

Cell type[SDV.BIO]Life Sciences [q-bio]/BiotechnologyEye DiseasesOxysterol[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionClinical BiochemistryModels BiologicalBiochemistrychemistry.chemical_compoundMembrane MicrodomainsEndocrinologyretinopathyMembrane fluiditypolycyclic compoundsAnimalsHumanscyp46a1[SDV.MHEP.OS]Life Sciences [q-bio]/Human health and pathology/Sensory OrgansLipid bilayerMolecular BiologyLipid raftPharmacologylipid raftsCholesterolOrganic Chemistry[ SDV.BIO ] Life Sciences [q-bio]/BiotechnologycholesterolSphingolipidCell biologySterolsMembranechemistryBiochemistry[ SDV.MHEP.OS ] Life Sciences [q-bio]/Human health and pathology/Sensory Organsoxysterolslipids (amino acids peptides and proteins)[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition
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Induction of identified mesodermal cells by CNS midline progenitors in Drosophila.

1997

ABSTRACT The Drosophila ventral midline cells generate a discrete set of CNS lineages, required for proper patterning of the ventral ectoderm. Here we provide the first evidence that the CNS midline cells also exert inductive effects on the mesoderm. Mesodermal progenitors adjacent to the midline progenitor cells give rise to ventral somatic mucles and a pair of unique cells that come to lie dorsomedially on top of the ventral nerve cord, the so-called DM cells. Cell ablation as well as cell transplantation experiments indicate that formation of the DM cells is induced by midline progenitors in the early embryo. These results are corroborated by genetic analyses. Mutant single minded embryo…

Central Nervous SystemMesodermanimal structuresSomatic cellCellEctodermNerve Tissue ProteinsBiologyMesodermCell MovementProto-Oncogene ProteinsmedicineMorphogenesisAnimalsDrosophila ProteinsProgenitor cellEye ProteinsMolecular BiologyEmbryonic InductionEpidermal Growth FactorCell growthGene Expression Regulation DevelopmentalMembrane ProteinsEmbryoAnatomyCell biologyDNA-Binding Proteinsmedicine.anatomical_structureDrosophila melanogasterVentral nerve cordembryonic structuresDevelopmental BiologySignal TransductionTranscription FactorsDevelopment (Cambridge, England)
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Color Doppler ultrasonography of the eye and orbit

1993

Color Doppler imaging is the recent development in ultrasonography that allows simultaneous two-dimensional structural imaging in Doppler evaluation of blood flow. With this technique, it is possible for the first time to indirectly display the fine orbital vessels such as the ophthalmic artery and its branches, the central retinal artery, the posterior ciliary artery, and the lacrimal artery. Also, the display of venous structures such as the superior ophthalmic vein, the vortex vein, and the central retinal vein is possible. In addition to the qualitative display of those vessels, the hemodynamics in those vessels can be quantitatively assessed by looking at the Doppler spectrum and deter…

Central retinal arterymedicine.medical_specialtyCentral retinal veinEyechemistry.chemical_compoundRetinal DiseasesCentral retinal vein occlusionmedicine.arteryOphthalmologyOrbital DiseasesmedicineHumansUltrasonographyEquipment Safetybusiness.industryEye NeoplasmsRetinalGeneral Medicinemedicine.diseaseOphthalmologymedicine.anatomical_structurechemistryOphthalmic arterycardiovascular systemLacrimal arteryCentral retinal artery occlusionbusinessOrbitSuperior ophthalmic veinBlood Flow VelocityCurrent Opinion in ophthalmology
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Ozone Therapy as treatment for severe cases without good evolution in ophthalmology [abstract]

2019

PURPOSE: In ophthalmology many diseases lead to irreversible blindness, something that implies millions of dollars in care because people with these difficulties loose their autonomy, becoming dependent in all their everyday activities.
 This presentation will focus on clinical cases of the following pathologies treated with Ozone Therapy because all these were already being treated in a conventional way without signs of improvement. They are primary open-angle glaucoma, age-related macular degeneration, diabetic retinopathy, occlusion of the central retinal artery, facial paralysis and herpetic polyneuropathy associated with orbital apex syndrome.
 
 CASE PRESENTATION: As an…

Central retinal arterymedicine.medical_specialtyVisual acuitygenetic structuresbusiness.industryGlaucomaDiabetic retinopathyMacular degenerationmedicine.diseaseOzone therapyeye diseasesFacial paralysismedicine.arteryOphthalmologyMedicinemedicine.symptombusinessPolyneuropathyJournal of Ozone Therapy
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RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal bodies and interacts with nucleophosmin

2005

The ORF15 isoform of RPGR (RPGR(ORF15)) and RPGR interacting protein 1 (RPGRIP1) are mutated in a variety of retinal dystrophies but their functions are poorly understood. Here, we show that in cultured mammalian cells both RPGR(ORF15) and RPGRIP1 localize to centrioles. These localizations are resistant to the microtubule destabilizing drug nocodazole and persist throughout the cell cycle. RPGR and RPGRIP1 also co-localize at basal bodies in cells with primary cilia. The C-terminal (C2) domain of RPGR(ORF15) (ORF15(C2)) is highly conserved across 13 mammalian species, suggesting that it is a functionally important domain. Using matrix-assisted laser desorption ionization time-of-flight mas…

CentrioleFluorescent Antibody TechniqueMicechemistry.chemical_compoundChlorocebus aethiopsGuanine Nucleotide Exchange FactorsProtein IsoformsBasal bodyConserved SequenceGenetics (clinical)CentriolesGlutathione Transferaseintegumentary systemNuclear ProteinsExonsGeneral MedicineRetinitis pigmentosa GTPase regulatorImmunohistochemistryNocodazoleCOS CellsNucleophosminCell NucleolusRecombinant Fusion ProteinsMolecular Sequence DataBiologyOpen Reading FramesMicrotubuleTwo-Hybrid System TechniquesGeneticsAnimalsHumansAmino Acid SequenceEye ProteinsMolecular BiologyNucleophosminSequence Homology Amino AcidProteinsPrecipitin TestsMolecular biologyeye diseasesProtein Structure TertiaryMice Inbred C57BLCytoskeletal ProteinschemistryCentrosomeCytoplasmSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationMutationCattleHeLa CellsHuman Molecular Genetics
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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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Interpositus nucleus inactivation reduces unconditioned response amplitude after paired but not explicitly unpaired treatment in rabbit eyeblink cond…

2001

The amplitude of unconditioned responses (URs) in unconditioned stimulus (US) alone presentations were measured in six rabbits during explicitly unpaired and classical conditioning treatments. After both phases of the experiment, the interpositus nucleus (IPN) was reversibly inactivated by a cold probe. URs after unpaired treatment were unaffected by inactivation but after acquisition of a robust level of conditioned responses (CRs), URs in US-alone test trials were reduced in amplitude compared with URs immediately before and after inactivation. The results suggest that the IPN has a role in CR-related reflex modification.

CerebellumBlinkingChemistryGeneral NeuroscienceConditioning ClassicalClassical conditioningUnconditioned responseUnconditioned stimulusConditioning EyelidCold TemperatureAmplitudemedicine.anatomical_structureEyeblink conditioningCerebellar NucleiBiophysicsmedicineReflexAnimalsRabbitsNeuroscienceNucleusNeuroscience letters
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