Journal Article

PreJuSER-62863

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Aggregation and amyloid fibril formation of the prion protein is accelerated in presence of glycogen

Panza, G. ; Stöhr, J. ; Birkmann, E.FZJ* ; Riesner, D. ; Willbold, D.FZJ* ; Baba, O. ; Terashima, T. ; Dumpitak, C.FZJ*

2008
Liebert Larchmont, NY

This record in other databases:    

Please use a persistent id in citations: doi:10.1089/rej.2008.0698

Abstract: Prion diseases like Creutzfeldt-Jakob disease in humans or scrapie in sheep and goats are infectious neurodegenerative diseases. Their infectious agent, called prion, is composed mainly of aggregated and misfolded prion protein and non-proteinaceous components. An example of such a common non-proteinaceous secondary component of natural prions is the polysaccharide scaffold. We studied the influence of such a polysaccharide on the conformational transition of PrP applying an in vitro conversion system. Here we report that glycogen supports and accelerates PrP amorphous aggregation similar to seeded aggregation and leads to co-aggregates. Furthermore, PrP fibril formation was highly accelerated in the presence of glycogen.

Keyword(s): Amyloid: chemistry (MeSH) ; Animals (MeSH) ; Circular Dichroism (MeSH) ; Cricetinae (MeSH) ; Glycogen: pharmacology (MeSH) ; Mesocricetus (MeSH) ; Prions: chemistry (MeSH) ; Prions: metabolism (MeSH) ; Protein Structure, Quaternary (MeSH) ; Recombinant Proteins: chemistry (MeSH) ; Recombinant Proteins: metabolism (MeSH) ; Amyloid ; Prions ; Recombinant Proteins ; Glycogen ; J

Note: Record converted from VDB: 12.11.2012

---

Contributing Institute(s):

1. Molekulare Biophysik (INB-2)

Research Program(s):

1. Funktion und Dysfunktion des Nervensystems (P33)

Appears in the scientific report 2008

---