NR ARQX
AU Kobayashi,A.; Satoh,S.; Ironside,J.W.; Mohri,S.; Kitamoto,T.
TI Type 1 and type 2 human PrPsc have different aggregation sizes in methionine homozygotes with sporadic, iatrogenic and variant Creutzfeldt-Jakob disease
QU Journal of General Virology 2005 Jan; 86(1): 237-40
PT journal article
AB In Creutzfeldt-Jakob disease (CJD), the type (type 1 or 2) of abnormal isoform of the prion protein (PrPsc) in the brain and the genotype at codon 129 of the PrP gene are major determinants of clinicopathological phenotype. Little is known about the difference in biochemical properties between the two types of PrPsc, except for the different proteinase K cleavage sites. To investigate the size of aggregates formed by PrPsc types 1 and 2, brain homogenates from various cases of CJD with the same genotype (homozygous for methionine at codon 129) were passed through filters with a mean pore size of 72+/-4 nm. Type 2 PrPsc was efficiently removed from the filtrates by the filters, in contrast to type 1. Even type 2 PrPsc from a patient without amyloid plaques was removed more efficiently than type 1 from patients with amyloid plaques. These results indicate that type 2 PrPsc has a larger aggregation size than type 1, irrespective of the existence of amyloid plaques.
MH Blotting, Western; *Brain Chemistry; Comparative Study; Creutzfeldt-Jakob Syndrome/*etiology/genetics; Filtration; *Homozygote; Humans; Iatrogenic Disease; Methionine; PrPsc Proteins/analysis/*chemistry/genetics; Research Support, Non-U.S. Gov't; Senile Plaques/chemistry
AD Division of CJD Science and Technology, Department of Prion Research, Center for Translational and Advanced Animal Research on Human Diseases, Tohoku University Graduate School of Medicine, 2-1 Seiryo-machi, Aoba-ku, Sendai 980-8575, Japan.
SP englisch
PO England