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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