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- W1585403709 abstract "Suramin induces misfolding of the cellular prion protein (PrP C ) and interferes with the propagation of infectious scrapie prions. A mechanistic analysis of this effect revealed that suramin‐induced misfolding occurs at the plasma membrane and is dependent on the proximal region of the C‐ terminal domain (aa 90–158) of PrP C . The conformational transition induces rapid internalization, mediated by the unstructured N‐ terminal domain, and subsequent intracellular degradation of PrP C . As a consequence, PrPΔN adopts a misfolded conformation at the plasma membrane; however, internalization is significantly delayed. We also found that misfolding and intracellular retention of PrP C can be induced by copper and that, moreover, copper interferes with the propagation of the pathogenic prion protein (PrP Sc ) in scrapie‐infected N2a cells. Our study revealed a quality control pathway for aberrant PrP conformers present at the plasma membrane and identified distinct PrP domains involved." @default.
- W1585403709 created "2016-06-24" @default.
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- W1585403709 date "2004-04-29" @default.
- W1585403709 modified "2023-10-16" @default.
- W1585403709 title "Misfolding of the Prion Protein at the Plasma Membrane Induces Endocytosis, Intracellular Retention and Degradation" @default.
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- W1585403709 doi "https://doi.org/10.1111/j.1398-9219.2004.00185.x" @default.
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