Elucidation of the prion pathogenic decision mechanism through a copper ion binding site of a prion protein

2014 Fiscal Year Final Research Report

• Project/Area Number: 25870479
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Neurology; Veterinary medical science
• Research Institution: The University of Tokushima
• Principal Investigator: HARA Hideyuki 徳島大学, 疾患酵素学研究センター, 助教 (40469953)
• Project Period (FY): 2013-04-01 – 2015-03-31
• Keywords: プリオン / 構造変換 / 銅イオン / オクタペプチドリピート

Outline of Final Research Achievements

Prion diseases are characterized by the replicative propagation of disease-associated forms of prion protein (PrPSc; PrP refers to prion protein). Structural conversion of the normal cellular isoform, designated PrPC, into PrPSc is a key event in prion propagation. However, the conversion mechanism remains unclear. In this study, we intracerebrally inoculated prions into tg(PrPΔOR)/Prnp0/0 mice, which express mouse PrP missing only the octapeptide repeat (OR) region on the PrP-null background. There are different incubation time in infected the prions. As a result, the mechanism of structural conversion was depending on the type of prions. Also we examined the effects of copper ions on the pathological progression of prion disease. However, copper ions didn't have any influence on the pathological progression.

Free Research Field

神経内科学