TY  - JOUR
AU  - Lüers, L.
AU  - Panza, G.
AU  - Henke, F.
AU  - Aygenim, T.
AU  - Weiß, J.
AU  - Willbold, D.
AU  - Birkmann, E.
TI  - Amyloid formation: Age-related mechanism in Creutzfeldt-Jakob disease?
JO  - Rejuvenation research
VL  - 13
SN  - 1549-1684
CY  - Larchmont, NY
PB  - Liebert
M1  - PreJuSER-9742
PY  - 2010
N1  - Record converted from VDB: 12.11.2012
AB  - Protein aggregation occurs in many age-related neurodegenerative diseases, where it can lead to deposits of naturally occurring proteins in the brain. In case of Creutzfeldt-Jakob disease (CJD), these deposits consist of prion protein (PrP). CJD has three etiologies: spontaneous, genetic, or caused by infection. A polymorphism within the PrP gene is associated with susceptibility of infection. The main event in prion diseases is the conversion of PrP from its naturally occurring isoform to its disease-associated isoform. Here, we present the adaption of a previously reported in vitro conversion system based on hamster recombinant PrP to analyze amyloid fibril formation of human recombinant PrP. We further compare the aggregation characteristics of the human PrP according to the polymorphism variants M129 and V129.
KW  - Aging: metabolism
KW  - Aging: physiology
KW  - Amyloid: metabolism
KW  - Circular Dichroism
KW  - Congo Red: pharmacology
KW  - Creutzfeldt-Jakob Syndrome: etiology
KW  - Creutzfeldt-Jakob Syndrome: metabolism
KW  - Creutzfeldt-Jakob Syndrome: pathology
KW  - Humans
KW  - Microscopy, Electron, Transmission
KW  - Models, Biological
KW  - PrPSc Proteins: chemistry
KW  - PrPSc Proteins: metabolism
KW  - Recombinant Proteins: analysis
KW  - Recombinant Proteins: chemistry
KW  - Recombinant Proteins: metabolism
KW  - Staining and Labeling
KW  - Thiazoles: pharmacology
KW  - Amyloid (NLM Chemicals)
KW  - PrPSc Proteins (NLM Chemicals)
KW  - Recombinant Proteins (NLM Chemicals)
KW  - Thiazoles (NLM Chemicals)
KW  - thioflavin T (NLM Chemicals)
KW  - Congo Red (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:20017612
UR  - <Go to ISI:>//WOS:000277602200020
DO  - DOI:10.1089/rej.2009.0932
UR  - https://juser.fz-juelich.de/record/9742
ER  -