title: Effect of Chaperones on Prion Protein PrP23-98 Aggregation In Vitro.
abstract: Recent studies have indicated that PrP23-98, an N-terminal portion of PrP, polymerizes into amyloid-like and proteinase K (PK)-resistant aggregates in the presence of NADPH with copper ions [19], and then that CRT suppressed aggregation of PrP23-98 and also promoted solubilization of the aggregates [18]. As it is interesting to find out whether other chaperones can inhibit aggregation of PrP23-98 in vitro similar to CRT, this study was conducted to determine whether BiP, Grp94, PDI Grp58 and heat shock cognate protein70 (Hsc70) can inhibit aggregation of PrP23-98 in vitro. The present results indicated that Grp94 suppressed aggregation of PrP23-98, but that Grp94 could not mediate solubilization occurred in the aggregates in contrast to CRT. Other chaperons induced aggregation of PrP23-98 in the absence of NADPH.
authors.affiliation: Department of Nutrition, Tokai Gakuen University, 2-901 Nakahira, Nagoya 468-8514, Japan.
authors.forename: Noriyuki
authors.initials: N
authors.lastname: Shiraishi
authors.forename: Yoshiaki
authors.initials: Y
authors.lastname: Hirano
mesh_terms: D000091342:Endoplasmic Reticulum Chaperone BiP; D050883:HSC70 Heat-Shock Proteins / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism*; D009249:NADP / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism; D000072002:Prion Proteins / Q000378:metabolism*; D066329:Protein Aggregates / Q000502:physiology*; D011485:Protein Binding; D019704:Protein Disulfide-Isomerases / Q000378:metabolism*
chemical_list: D000091342:Endoplasmic Reticulum Chaperone BiP; D050883:HSC70 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D008565:Membrane Proteins; D018832:Molecular Chaperones; D010446:Peptide Fragments; D000072002:Prion Proteins; D066329:Protein Aggregates; C018551:glucose-regulated proteins; D009249:NADP; D019704:Protein Disulfide-Isomerases; C085868:PDIA3 protein, human