Search results for "Peripherin"

showing 5 items of 5 documents

Cytokeratin 20 Is a General Marker of Cutaneous Merkel Cells While Certain Neuronal Proteins Are Absent

1995

Merkel cells are difficult to identify in tissue sections. Previous studies have used cytokeratins (CK) 8, 18, and 19 as histologic markers of Merkel cells. However, these CKs are also expressed in some outer root sheath keratinocytes and some early fetal epidermal cells and thus are not truly specific of Merkel cells in general. Using selective antibodies against a newly described CK, number 20--originally found in intestinal epithelium and Merkel cell carcinomas--in comparison to a key protein of neuroendocrine cells, chromogranin A, we established CK 20 as a specific Merkel cell marker in skin of humans, pigs, and mice. CK 20 seems to be an even more general and sensitive Merkel cell mar…

AdultPathologymedicine.medical_specialtySwineCellHuman skinNerve Tissue ProteinsDermatologyKeratin-20BiologyOuter root sheathBiochemistryCytokeratinMiceFetusIntermediate Filament ProteinsmedicineAnimalsHumansMolecular BiologySkinintegumentary systemChromogranin APeripherinEpithelial CellsCell BiologyMolecular biologyImmunohistochemistrymedicine.anatomical_structurebiology.proteinMerkel cellNeuronal Cell Adhesion MoleculeBiomarkersHairJournal of Investigative Dermatology
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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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Peripherin-2 differentially interacts with cone opsins in outer segments of cone photoreceptors

2016

Peripherin-2 is a glycomembrane protein exclusively expressed in the light-sensing compartments of rod and cone photoreceptors designated as outer segments (OS). Mutations in peripherin-2 are associated with degenerative retinal diseases either affecting rod or cone photoreceptors. While peripherin-2 has been extensively studied in rods, there is only little information on its supramolecular organization and function in cones. Recently, we have demonstrated that peripherin-2 interacts with the light detector rhodopsin in OS of rods. It remains unclear, however, if peripherin-2 also binds to cone opsins. Here, using a combination of co-immunoprecipitation analyses, transmission electron micr…

0301 basic medicineRhodopsinOpsingenetic structuresmacromolecular substances030105 genetics & heredityBiologymedicine.disease_causeRetinaMice03 medical and health scienceschemistry.chemical_compoundImmunolabelingMicroscopy Electron TransmissionAntigens NeoplasmFluorescence Resonance Energy TransferGeneticsmedicineAnimalsHumansPeripherin 2Molecular BiologyGenetics (clinical)MutationRetinal DegenerationRetinalGeneral MedicineCone Opsinseye diseases030104 developmental biologyFörster resonance energy transfernervous systemchemistryRhodopsinMutationRetinal Cone Photoreceptor CellsBiophysicsbiology.proteinsense organsProtein BindingVisual phototransductionHuman Molecular Genetics
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Identification of KRT16 as a target of an autoantibody response in complex regional pain syndrome

2016

Abstract Objective Using a mouse model of complex regional pain syndrome (CRPS), our goal was to identify autoantigens in the skin of the affected limb. Methods A CRPS-like state was induced using the tibia fracture/cast immobilization model. Three weeks after fracture, hindpaw skin was homogenized, run on 2-d gels, and probed by sera from fracture and control mice. Spots of interest were analyzed by liquid chromatography-mass spectroscopy (LC-MS) and the list of targets validated by examining their abundance and subcellular localization. In order to measure the autoantigenicity of selected protein targets, we quantified the binding of IgM in control and fracture mice sera, as well as in co…

AdultMale0301 basic medicinePathologymedicine.medical_specialtyPeripherinsTibia FractureAutoantigensProtein citrullinationArticlelaw.inventionMiceYoung Adult03 medical and health sciencesPeptide Elongation Factor 10302 clinical medicineDevelopmental NeuroscienceENO3Downregulation and upregulationlawAnimalsHumansMedicineAnnexin A2Skinbusiness.industryKeratin-6AutoantibodyMiddle Agedmedicine.diseaseHindlimbUp-RegulationMice Inbred C57BLTibial FracturesDisease Models Animal030104 developmental biologyComplex regional pain syndromeNeurologyPhosphopyruvate HydrataseImmunologyRecombinant DNABiomarker (medicine)businessComplex Regional Pain Syndromes030217 neurology & neurosurgerySubcellular FractionsExperimental Neurology
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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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