Search results for "Peripherins"

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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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