title: Calreticulin inhibits prion protein PrP-(23-98) aggregation in vitro.
abstract: Because prion protein PrP-(23-98) was recently found to polymerize into amyloid-like and proteinase K-resistant spherical aggregates in the presence of NADPH plus copper ions, we tested to determine whether calreticulin (CRT) inhibits PrP-(23-98) aggregation in vitro. The results indicated that CRT suppressed PrP-(23-98) aggregation, and that CRT-mediated solubilization occurred in the aggregates.
authors.affiliation: Department of Nutrition, Tokai Gakuen University, Nagoya, Japan. shiraish@tokaigakuen-u.ac.jp
authors.forename: Noriyuki
authors.initials: N
authors.lastname: Shiraishi
authors.forename: Yoko
authors.initials: Y
authors.lastname: Inai
authors.forename: Yoshiaki
authors.initials: Y
authors.lastname: Hirano
authors.forename: Yoshito
authors.initials: Y
authors.lastname: Ihara
mesh_terms: D000682:Amyloid / Q000378:metabolism; D037282:Calreticulin / Q000494:pharmacology / Q000627:therapeutic use*; D003300:Copper / Q000009:adverse effects / Q000037:antagonists & inhibitors* / Q000494:pharmacology; D004305:Dose-Response Relationship, Drug; D019286:Endopeptidase K / Q000378:metabolism; D006801:Humans; D009249:NADP / Q000009:adverse effects / Q000037:antagonists & inhibitors* / Q000494:pharmacology; D010446:Peptide Fragments / Q000378:metabolism*; D058225:Plaque, Amyloid / Q000378:metabolism / Q000517:prevention & control*; D017096:Prion Diseases / Q000188:drug therapy / Q000473:pathology; D011328:Prions / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects*; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism*; D012996:Solutions; D013053:Spectrophotometry
chemical_list: D000682:Amyloid; D037282:Calreticulin; D010446:Peptide Fragments; D011328:Prions; D011994:Recombinant Proteins; D012996:Solutions; C538804:prion protein (23-98); D009249:NADP; D003300:Copper; D019286:Endopeptidase K