TY  - JOUR
AU  - Panza, G.
AU  - Stöhr, J.
AU  - Dumpitak, C.
AU  - Papathanassiou, D.
AU  - Weiss, J.
AU  - Riesner, D.
AU  - Willbold, D.
AU  - Birkmann, E.
TI  - Spontaneous and BSE-prion-seeded amyloid formation of full length recombinant bovine prion protein
JO  - Biochemical and biophysical research communications
VL  - 373
SN  - 0006-291X
CY  - Orlando, Fla.
PB  - Academic Press
M1  - PreJuSER-313
SP  - 493 - 497
PY  - 2008
N1  - Record converted from VDB: 12.11.2012
AB  - The conversion of the cellular isoform of the prion protein into the pathogenic isoform PrP(Sc) is the key event in prion diseases. The disease can occur spontaneously genetically or by infection. In earlier studies we presented an in vitro conversion system which simulates the structural transition in recPrP by varying low concentrations of SDS at constant NaCl. In the present study we adopted the conversion system from experimental Scrapie in hamster to bovine recPrP and generated amyloid fibrils. The intermediate state which is optimal for fibril formation is a soluble, beta-rich state. The system was extended using BSE-prions as seeds and led to an acceleration of fibril formation by orders of magnitude. This seeded amyloid formation assay avoids any PK-treatment, is therefore able to detect even PK-sensitive PrP(Sc) and does not require cellular components.
KW  - Amyloid: biosynthesis
KW  - Amyloid: chemistry
KW  - Animals
KW  - Cattle
KW  - Cricetinae
KW  - Encephalopathy, Bovine Spongiform: metabolism
KW  - Models, Molecular
KW  - PrPSc Proteins: chemistry
KW  - PrPSc Proteins: metabolism
KW  - Protein Conformation
KW  - Recombinant Proteins: chemistry
KW  - Recombinant Proteins: metabolism
KW  - Amyloid (NLM Chemicals)
KW  - PrPSc Proteins (NLM Chemicals)
KW  - Recombinant Proteins (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:18585368
UR  - <Go to ISI:>//WOS:000258208500008
DO  - DOI:10.1016/j.bbrc.2008.06.059
UR  - https://juser.fz-juelich.de/record/313
ER  -