Effect of Chaperones on Prion Protein PrP23-98 Aggregation In Vitro

Title:Effect of Chaperones on Prion Protein PrP23-98 Aggregation In Vitro

Volume: 23 Issue: 11

Author(s): Noriyuki Shiraishi and Yoshiaki Hirano

Affiliation:

Keywords: Prion protein, PrP23-98, aggregates, chaperon.

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.

Cite this article as:

Shiraishi Noriyuki and Hirano Yoshiaki, Effect of Chaperones on Prion Protein PrP23-98 Aggregation In Vitro, Protein & Peptide Letters 2016; 23 (11) . https://dx.doi.org/10.2174/0929866523666160909160422