Search results for " Outer"

showing 10 items of 129 documents

Mutation Analysis Identifies GUCY2D as the Major Gene Responsible for Autosomal Dominant Progressive Cone Degeneration

2008

PURPOSE. Heterozygous mutations in the GUCY2D gene, which encodes the membrane-bound retinal guanylyl cyclase-1 protein (RetGC-1), have been shown to cause autosomal dominant inherited cone degeneration and cone–rod degeneration (adCD, adCRD). The present study was a comprehensive screening of the GUCY2D gene in 27 adCD and adCRD unrelated families of these rare disorders. METHODS. Mutation analysis was performed by direct sequencing as well as PCR and subsequent restriction length polymorphism analysis (PCR/RFLP). Haplotype analysis was performed in selected patients by using microsatellite markers. RESULTS. GUCY2D gene mutations were identified in 11 (40%) of 27 patients, and all mutation…

Retinal degenerationMaleDNA Mutational AnalysisReceptors Cell SurfaceBiologyPolymerase Chain ReactionArticlemedicineElectroretinographyMissense mutationHumansGenetic Predisposition to DiseaseCodonGeneGeneticsHaplotypeRetinal DegenerationDNAmedicine.diseasePrognosisRod Cell Outer SegmentMajor geneMolecular biologyPedigreeHaplotypesGuanylate CyclaseMutationMutation testingDisease ProgressionGUCY2DFemaleRestriction fragment length polymorphism
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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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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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Differential expression and interaction with the visual G-protein transducin of centrin isoforms in mammalian photoreceptor cells.

2004

Photoisomerization of rhodopsin activates a heterotrimeric G-protein cascade leading to closure of cGMP-gated channels and hyperpolarization of photoreceptor cells. Massive translocation of the visual G-protein transducin, Gt, between subcellular compartments contributes to long term adaptation of photoreceptor cells. Ca(2+)-triggered assembly of a centrin-transducin complex in the connecting cilium of photoreceptor cells may regulate these transducin translocations. Here we demonstrate expression of all four known, closely related centrin isoforms in the mammalian retina. Interaction assays revealed binding potential of the four centrin isoforms to Gtbetagamma heterodimers. High affinity b…

Rhodopsingenetic structuresLightBlotting WesternBiologyBiochemistryRetinaRats Sprague-DawleyMiceCalcium-binding proteinHeterotrimeric G proteinmedicineAnimalsProtein IsoformsScattering RadiationCiliaTransducinMicroscopy ImmunoelectronMolecular BiologyCyclic GMPGlutathione TransferaseCentrosomeRetinaChromatographyDose-Response Relationship DrugReverse Transcriptase Polymerase Chain ReactionCiliumCalcium-Binding ProteinsCell BiologySequence Analysis DNARod Cell Outer SegmentRecombinant ProteinsCell biologyRatsMice Inbred C57BLKineticsProtein Transportmedicine.anatomical_structureMicroscopy FluorescenceRhodopsinCentrosomeCentrinbiology.proteinCalciumCattleElectrophoresis Polyacrylamide Gelsense organsTransducinProtein BindingThe Journal of biological chemistry
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Siderophore production by environmental strains ofSalmonellaspecies

1989

Iron uptake mechanisms were investigated in different species of Salmonella isolated from environmental waters. All strains examined were able to grow in the presence of high concentrations (10 mM) of the iron chelator EDDA. All strains excreted phenolate and hydroxamate siderophores, as assessed by bioassays and chemical tests. Bioassays with different indicator strains showed that all Salmonella strains can cross-feed other Enterobacteria, as well as mutants of Salmonella typhimurium deficient in the Enterobactin system, suggesting that this siderophore may be produced by the environmental Salmonella strains. The siderophore aerobactin may also be produced by one of the strains, according…

SalmonellaSiderophoreBiologybiology.organism_classificationmedicine.disease_causeMicrobiologyEnterobacteriaceaeMicrobiologychemistry.chemical_compoundEnterobactinBiochemistrychemistryGeneticsmedicineAerobactinBioassayBacterial outer membraneMolecular BiologyBacteriaFEMS Microbiology Letters
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Host glycoprotein Gp96 and scavenger receptor SREC interact with PorB of disseminating Neisseria gonorrhoeae in an epithelial invasion pathway.

2007

Neisseria gonorrhoeae expresses numerous surface proteins that mediate bacterial adherence and invasion during infection. Gonococci expressing serotype A of the major outer membrane porin PorB (PorB(IA)) are frequently isolated from patients with severe disseminating infections. PorB(IA) triggers efficient adherence and invasion under low phosphate conditions mimicking systemic bloodstream infections. Here, we identify the human heat shock glycoprotein Gp96 and the scavenger receptor SREC as PorB(IA)-specific receptors. Gonococci expressing PorB(IA), but not those expressing PorB serotype B instead, bind to purified native or recombinant Gp96. Depletion of Gp96 from host cells prevented adh…

SerotypeCancer ResearchMICROBIO2405 ParasitologyPorinsBiologymedicine.disease_causeEndoplasmic ReticulumMicrobiologyBacterial Adhesionlaw.inventionMicrobiologyGonorrhealawVirologyImmunology and Microbiology(all)medicineAnimalsHumansScavenger receptorReceptorMolecular BiologyCells Culturedchemistry.chemical_classificationMembrane Glycoproteins10061 Institute of Molecular Cancer Research2404 MicrobiologyEpithelial CellsNeisseria gonorrhoeaeScavenger Receptors Class FchemistryPorin2406 VirologyRecombinant DNANeisseria gonorrhoeae570 Life sciences; biologyParasitologyGlycoproteinBacterial outer membraneProtein BindingCell hostmicrobe
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Phenotypic characterization of Vibrio vulnificus biotype 2, a lipopolysaccharide-based homogeneous O serogroup within Vibrio vulnificus.

1996

In this study, we have reevaluated the taxonomic position of biotype 2 of Vibrio vulnificus. For this purpose, we have biochemically and serologically characterized 83 biotype 2 strains from diseased eels, comparing them with 17 biotype 1 strains from different sources. Selected strains were also molecularly analyzed and tested for eel and mouse pathogenicity. Results have shown that biotype 2 (i) is biochemically homogeneous, indole production being the main trait that distinguishes it from biotype 1, (ii) presents small variations in DNA restriction profiles and outer membrane protein patterns, some proteins being immunologically related to outer membrane proteins from biotype 1, (iii) ex…

SerotypeEelsEcologybiologyImmunoblottingO AntigensVibrio vulnificusbiology.organism_classificationApplied Microbiology and BiotechnologyVibrioMicrobiologyPlasmidPhenotypeMembrane proteinVibrionaceaeAnimalsSerotypingBacterial outer membraneWater MicrobiologyBacteriaFood ScienceBiotechnologyResearch ArticlePlasmidsVibrio
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Electrophoretic analysis of heterogeneous lipopolysaccharides from various strains of Vibrio vulnificus biotypes 1 and 2 by silver staining and immun…

1992

Lipopolysaccharides (LPS) of 11 strains of Vibrio vulnificus biotypes 1 and 2, isolated from an eel farm, and of 10 reference strains, were examined by SDS-polyacrylamide gel electrophoresis coupled with silver staining and immunoblotting. LPS samples were obtained from whole-cell lysates, outer membrane fragments, and extracellular products. By silver staining, only a diffuse band of low-molecular weight could be visualized in all cases except for a biotype 1 strain isolated from water. However, immunoblotting with antisera obtained against strains of biotypes 1 and 2 from eels allowed visualization of multiple O-polysaccharide chains. All biotype 2 strains, independently of their origins,…

SerotypeLipopolysaccharidesSilver StainingBlotting WesternVibrio vulnificusApplied Microbiology and BiotechnologyMicrobiologyMicrobiologySilver stainSpecies SpecificityVibrionaceaeAgglutination TestsAnimalsVibrioGel electrophoresisAntiserumEelsbiologyPolysaccharides BacterialO AntigensGeneral Medicinebiology.organism_classificationMolecular biologyAntibodies BacterialElectrophoresis Polyacrylamide GelRabbitsBacterial outer membraneBacteriaCurrent microbiology
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Immunogenic antigens of the eel pathogen Vibrio vulnificus serovar E.

2003

Abstract The immunogenic antigens of Vibrio vulnificus serovar E were investigated in the eel. Fish were vaccinated by immersion with Vulnivaccine (V), revaccinated 2 years later by intraperitoneal injection (RV) and bath infected 15 days post-revaccination (RVI). The specific immune response in serum was followed in all groups, and selected sera were used for immunostaining of surface (SA) and extracellular antigens (ECA). Bacteria were grown in iron-rich (TSB and MSWYE) and iron-poor media (TSB and MSWYE plus human transferrin (TSB-T and MSWYE-T)) as well as eel serum (ES), and their SA and ECA were extracted and electrophoretically analysed. Cells grown in MSWYE-T and ES presented the sa…

SerotypeLipopolysaccharidesTime FactorsLipopolysaccharideIronImmunoblottingEnzyme-Linked Immunosorbent AssayVibrio vulnificusAquatic ScienceMicrobiologychemistry.chemical_compoundAntigenEnvironmental ChemistryAnimalsPathogenVibrio vulnificuschemistry.chemical_classificationAntigens BacterialbiologyImmune SeraGeneral Medicinebiology.organism_classificationAnguillachemistryTransferrinAntibody FormationBacterial VaccinesElectrophoresis Polyacrylamide GelBacterial outer membraneBacteriaBacterial Outer Membrane ProteinsFishshellfish immunology
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