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Relative Abundance of apoE and A beta 1-42 Associated with Abnormal Prion Protein Differs between Creutzfeldt-Jakob Disease Subtypes

Authors
Moore, Roger A.Choi, Young PyoHead, Mark W.Ironside, James W.Faris, RobertRitchie, Diane L.Zanusso, GianluigiPriola, Suzette A.
Issue Date
Dec-2016
Publisher
AMER CHEMICAL SOC
Keywords
prion protein; transmissible spongiform encephalopathies; Creutzfeld-Jakob disease; mass spectrometry; proteomics; creatine kinase; apolipoprotein E; amyloid beta
Citation
JOURNAL OF PROTEOME RESEARCH, v.15, no.12, pp.4518 - 4531
Journal Title
JOURNAL OF PROTEOME RESEARCH
Volume
15
Number
12
Start Page
4518
End Page
4531
URI
http://scholarworks.bwise.kr/kbri/handle/2023.sw.kbri/842
DOI
10.1021/acs.jproteome.6b00633
ISSN
1535-3893
Abstract
Aggregated and protease-resistant mammalian prion protein (PrPsc) is the primary protein component of infectious prions. Enriched PrPsc preparations are often used to study the mechanisms that underly prion disease. However, most enrichment procedures are relatively nonspecific and tend to yield significant amounts of non-PrPsc components including various proteins that could confound functional and structural studies. It is thus important to identify these proteins and assess their potential relevance to prion pathogenesis. Following proteinase K treatment and phosphotungstic acid precipitation of brain homogenate, we have used mass spectrometry to analyze the protein content of PrPsc isolated from prion-infected mice, multiple cases of sporadic Creutzfeldt-Jakob disease (sCJD), and human growth hormone associated cases of iatrogenic CJD (iCJD). Creatine kinase was the primary protein contaminant in all PrPsc samples, while many of the other proteins identified were also found in non-CJD controls, which suggests that they are not CJD specific. Interestingly, the Alzheimer's disease associated peptide amyloid beta 1-42 (A beta 1-42) was identified in the majority of the sCJD cases as well as non-CJD age-matched controls, while apoliprotein E was found in greater abundance in the sCJD cases. By contrast, while some of the iCJD cases showed evidence of higher molecular weight A beta oligomers, monomeric A beta 1-42 peptide was not detected by immunoblot, and only one case had significant levels of apolipoprotein E. Our data are consistent with the age-associated deposition of A beta 1-42 in older sporadic CJD and non-CJD patients and suggest that both apolipoprotein E and A beta 1-42 abundance can differ depending upon the type of CJD.
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