TY  - JOUR
AU  - Panza, G.
AU  - Stöhr, J.
AU  - Birkmann, E.
AU  - Riesner, D.
AU  - Willbold, D.
AU  - Baba, O.
AU  - Terashima, T.
AU  - Dumpitak, C.
TI  - Aggregation and amyloid fibril formation of the prion protein is accelerated in presence of glycogen
JO  - Rejuvenation research
VL  - 11
SN  - 1549-1684
CY  - Larchmont, NY
PB  - Liebert
M1  - PreJuSER-62863
SP  - 365 - 369
PY  - 2008
N1  - Record converted from VDB: 12.11.2012
AB  - 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.
KW  - Amyloid: chemistry
KW  - Animals
KW  - Circular Dichroism
KW  - Cricetinae
KW  - Glycogen: pharmacology
KW  - Mesocricetus
KW  - Prions: chemistry
KW  - Prions: metabolism
KW  - Protein Structure, Quaternary
KW  - Recombinant Proteins: chemistry
KW  - Recombinant Proteins: metabolism
KW  - Amyloid (NLM Chemicals)
KW  - Prions (NLM Chemicals)
KW  - Recombinant Proteins (NLM Chemicals)
KW  - Glycogen (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:18341429
UR  - <Go to ISI:>//WOS:000255773200015
DO  - DOI:10.1089/rej.2008.0698
UR  - https://juser.fz-juelich.de/record/62863
ER  -