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- W3204127007 endingPage "108787" @default.
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- W3204127007 abstract "Recently, we reported β-cleavage of the prion protein (PrPC) 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 PrPC in human ocular tissues with common nocturnal and diurnal animals revealed mainly β-cleavage in humans, and mostly full-length PrPC in animal retinas. Soluble FL PrPC and N-terminal fragment (N2) released from β-cleavage was observed in the aqueous and vitreous humor (AH & VH). Expression of human PrPC in ARPE-19 cells, a human retinal pigmented epithelial cell line, also showed β-cleaved PrPC. Surprisingly, β-cleavage was not altered by a variety of insults, including oxidative stress, suggesting a unique role of this cleavage in the human eye. It is likely that β-cleaved C- or N-terminal fragments of PrPC protect from various insults unique to the human eye. On the contrary, β-cleaved C-terminus of PrPC is susceptible to conversion to the pathological PrP-scrapie form, and includes the binding sites for β1-integrin and amyloid-β, molecules implicated in several ocular disorders. Considering the species and tissue-specific cleavage of PrPC, our data suggest re-evaluation of prion infectivity and other ocular disorders of the human eye conducted in mouse models." @default.
- W3204127007 created "2021-10-11" @default.
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- W3204127007 date "2021-11-01" @default.
- W3204127007 modified "2023-10-15" @default.
- W3204127007 title "β-Cleavage of the prion protein in the human eye: Implications for the spread of infectious prions and human ocular disorders" @default.
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- W3204127007 doi "https://doi.org/10.1016/j.exer.2021.108787" @default.
- W3204127007 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8608713" @default.
- W3204127007 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34624335" @default.
- W3204127007 hasPublicationYear "2021" @default.
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