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Fig. 1. The copper-stimulated endocytosis of PrPC is blocked by tyrphostin A23. (A) SH-SY5Y cells expressing PrPC were surface biotinylated and then either untreated or treated with tyrphostin A23 in the presence or absence of 100 µM Cu2+. Prior to lysis, the cells were incubated with trypsin to digest cell-surface PrPC. Cells were then lysed, and total PrPC was immunoprecipitated from the sample using antibody 3F4 and then subjected to western blot analysis. The biotin-labelled PrPC fraction was detected with peroxidase-conjugated streptavidin. (B) The same samples from (A) were also immunoprecipitated using an anti-transferrin receptor antibody. (C) Cells were treated with tyrphostin A63 and processed as in (A). (D) Biotin-labelled N2a cells were processed as described in (A), but PrPC was immunoprecipitated using the antibody SAF-32. Densitometric analysis (mean±s.e.m.) of multiple blots from three separate experiments is shown.





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