English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Zendy Plus

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Zendy Tools

Zendy Open

The conversion of cellular prion protein (PrP C ) into its pathological isoform (PrP Sc ) conveys an increase in hydrophobicity and induces a partial resistance to proteinase K (PK). Interestingly, co-incubation with high copper ion concentrations also modifies the solubility of PrP C  and induces a partial PK resistance which was reminiscent of PrP Sc . However, concerns were raised whether this effect was not due to a copper-induced inhibition of the PK itself. We have therefore analyzed the kinetics of the formation of PK-resistant PrP C  and excluded possible interference effects by removing unbound copper ions prior to the addition of PK by methanol precipitation or immobilization of PrP C  followed by washing steps. We found that preincubation of PrP C  with copper ions at concentrations as low as 50 µM indeed rendered these proteins completely PK resistant, while control substrates were proteolyzed. No other divalent cations induced a similar effect. However, in addition to this specific stabilizing effect on PrP C , higher copper ion concentrations insolution (&gt; 200 µM) directly blocked the enzymatic activity of PK, possibly by replacing the Ca 2+  ions in the active center of the enzyme. Therefore, as a result of this inhibition the proteolytic degradation of PrP C  as well as PrP Sc  molecules was suppressed.

Cellular prion protein acquires resistance to proteolytic degradation following copper ion binding