<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Chaudhary S</submitter><funding>NINDS NIH HHS</funding><funding>National Institutes of Health</funding><pagination>108787</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8608713</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>212</volume><pubmed_abstract>Recently, we reported β-cleavage of the prion protein (PrP&lt;sup>C&lt;/sup>) in human ocular tissues. Here, we explored whether this is unique to the human eye, and its functional implications. A comparison of the cleavage pattern of PrP&lt;sup>C&lt;/sup> in human ocular tissues with common nocturnal and diurnal animals revealed mainly β-cleavage in humans, and mostly full-length PrP&lt;sup>C&lt;/sup> in animal retinas. Soluble FL PrP&lt;sup>C&lt;/sup> and N-terminal fragment (N2) released from β-cleavage was observed in the aqueous and vitreous humor (AH &amp; VH). Expression of human PrP&lt;sup>C&lt;/sup> in ARPE-19 cells, a human retinal pigmented epithelial cell line, also showed β-cleaved PrP&lt;sup>C&lt;/sup>. Surprisingly, β-cleavage was not altered by a variety of insults, including oxidative stress, suggesting a unique</pubmed_abstract><journal>Experimental eye research</journal><pubmed_title>β-Cleavage of the prion protein in the human eye: Implications for the spread of infectious prions and human ocular disorders.</pubmed_title><pmcid>PMC8608713</pmcid><funding_grant_id>R01 NS092145</funding_grant_id><pubmed_authors>Lindner E</pubmed_authors><pubmed_authors>Wise AS</pubmed_authors><pubmed_authors>Chaudhary S</pubmed_authors><pubmed_authors>Singh N</pubmed_authors><pubmed_authors>Kritikos AE</pubmed_authors><pubmed_authors>Ashok A</pubmed_authors><pubmed_authors>Rana NA</pubmed_authors></additional><is_claimable>false</is_claimable><name>β-Cleavage of the prion protein in the human eye: Implications for the spread of infectious prions and human ocular disorders.</name><description>Recently, we reported β-cleavage of the prion protein (PrP&lt;sup>C&lt;/sup>) in human ocular tissues. Here, we explored whether this is unique to the human eye, and its functional implications. A comparison of the cleavage pattern of PrP&lt;sup>C&lt;/sup> in human ocular tissues with common nocturnal and diurnal animals revealed mainly β-cleavage in humans, and mostly full-length PrP&lt;sup>C&lt;/sup> in animal retinas. Soluble FL PrP&lt;sup>C&lt;/sup> and N-terminal fragment (N2) released from β-cleavage was observed in the aqueous and vitreous humor (AH &amp; VH). Expression of human PrP&lt;sup>C&lt;/sup> in ARPE-19 cells, a human retinal pigmented epithelial cell line, also showed β-cleaved PrP&lt;sup>C&lt;/sup>. Surprisingly, β-cleavage was not altered by a variety of insults, including oxidative stress, suggesting a unique</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Nov</publication><modification>2025-04-05T11:27:28.061Z</modification><creation>2025-04-05T11:27:28.061Z</creation></dates><accession>S-EPMC8608713</accession><cross_references><pubmed>34624335</pubmed><doi>10.1016/j.exer.2021.108787</doi></cross_references></HashMap>