Proteinase K-resistant aggregates of recombinant prion protein PrP-(23-98) are toxic to cultured cells.
Here, we show for the first time that non-fibrillar and spherical aggregates produced from PrP-(23-98) in the presence of NADPH plus copper ions are toxic to cultured cells and induce apoptotic signals. It is also confirmed that endogenous cellular PrP isoform is not required for toxicity to occur.
Shiraishi
Noriyuki
N
Department of Biochemistry, Wakayama Medical University, 811-1 Kimiidera, Wakayama 641-8509, Japan. nshirais@wakayama-med.ac.jp
Inai
Yoko
Y
Ihara
Yoshito
Y
D000818:Animals; D017209:Apoptosis / Q000187:drug effects*; D002460:Cell Line; D019286:Endopeptidase K / Q000378:metabolism*; D006624:Hippocampus / Q000187:drug effects; D051379:Mice; D010446:Peptide Fragments / Q000633:toxicity*; D011328:Prions / Q000633:toxicity*; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000633:toxicity*
D010446:Peptide Fragments; D011328:Prions; D011994:Recombinant Proteins; C538804:prion protein (23-98); D019286:Endopeptidase K