The prion protein is required for normal responses to light stimuli by photoreceptors and bipolar cells.

Autor:	Striebel JF; Laboratory of Neurological Infections and Immunity, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA., Carroll JA; Laboratory of Neurological Infections and Immunity, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA., Race B; Laboratory of Neurological Infections and Immunity, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA., Leung JM; Research Technologies Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA., Schwartz C; Research Technologies Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA., Reese ED; McLaughlin Research Institute, Great Falls, MT 59405, USA., Bowes Rickman C; Department of Ophthalmology, Duke University School of Medicine, Durham, NC 27710, USA.; Department of Cell Biology, Duke University School of Medicine, Durham, NC 27710, USA., Chesebro B; Laboratory of Neurological Infections and Immunity, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA., Klingeborn M; Department of Ophthalmology, Duke University School of Medicine, Durham, NC 27710, USA.; McLaughlin Research Institute, Great Falls, MT 59405, USA.
Jazyk:	angličtina
Zdroj:	IScience [iScience] 2024 Sep 13; Vol. 27 (10), pp. 110954. Date of Electronic Publication: 2024 Sep 13 (Print Publication: 2024).
DOI:	10.1016/j.isci.2024.110954
Abstrakt:	The prion protein, PrP C , is well known as an essential susceptibility factor for neurodegenerative prion diseases, yet its function in normal, healthy cells remains uncertain. A role in synaptic function has been proposed for PrP C , supported by its cell surface expression in neurons and glia. Here, in mouse retina, we localized PrP C to the junctions between photoreceptors and bipolar cells using synaptic proteins EAAT5, CtBP2, and PSD-95. PrP C localized most densely with bipolar cell dendrites synapsing with cone photoreceptors. In two coisogenic mouse strains, deletion of the gene encoding PrP C , Prnp , significantly altered the scotopic and/or photopic electroretinographic (ERG) responses of photoreceptors and bipolar cells. Cone-dominant pathways showed the most significant ERG changes. Retinal thickness, quantitated by high-resolution optical coherence tomography (OCT), and ribbon synapse morphology were not altered upon deletion of PrP C , suggesting that the ERG changes were driven by functional rather than structural alterations. Competing Interests: The authors declare no competing interests.
Databáze:	MEDLINE
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