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1 Department of Neurological Science, Tohoku University Graduate School of Medicine, 2-1 Seiryo-machi, Sendai 980-8575, Japan
2 CREST, JST (Japan Science and Technology), Kawaguchi, Japan
3 Sakai City Institute of Public Health, Sakai, Japan
4 Prion Research Project, Ministry of Health, Labour and Welfare, Japan
5 School of Humanities for Environmental Policy and Technology, Himeji Institute of Technology, Himeji, Japan
6 CJD Surveillance Unit, Western General Hospital, Edinburgh, UK
7 Laboratory of Molecular and Cellular Pathology, Hokkaido University School of Medicine, Sapporo, Japan
8 Department of Neurology and Neurobiology of Ageing, Kanazawa University Graduate School of Medical Science, Kanazawa, Japan
9 Kohnodai Hospital, National Center of Neurology and Psychiatry, Ichikawa, Japan
10 Department of Laboratory Animal Science, Graduate School of Medical Sciences, Kyushu University, Fukuoka, Japan
Correspondence
Tetsuyuki Kitamoto (at address 1)
kitamoto{at}mail.cc.tohoku.ac.jp
Creutzfeldt–Jakob disease can develop in subjects given a cadaveric dura mater graft (dCJD). This disease has a phenotypic heterogeneity despite the lack of genetic variation. Numerous plaque-type prion protein (PrP) deposits are found in the brain of some but not all subjects; hence, there may be two subtypes of this clinical entity. To validate dCJD subtypes further, we carried out a larger-scale clinicopathological analysis and typing of protease-resistant PrP (PrPSc) in dCJD cases. Cases with plaque-type PrP deposits (p-dCJD) were shown to be distinct from those without PrP plaques (np-dCJD), from several clinicopathological aspects. Analysis of PrPSc revealed that, while the major PrPSc species from both subtypes was of 21 kDa after deglycosylation (type 1 PrPSc), a C-terminal PrP fragment of 11–12 kDa (fPrP11–12) was associated with np-dCJD but not with p-dCJD. The disease type-specific association of fPrP11–12 was also observed in subjects with other prion diseases. An fPrP11–12-like C-terminal PrP fragment was detected in brain lysates from patients associated with fPrP11–12, but not from patients or normal subjects unassociated with fPrP11–12. Results indicated that fPrP was produced by CJD-associated processes in vivo. The present data provide several lines of evidence that support the need for subtyping of dCJD and contribute to the understanding of the processing of disease-specific PrP species. The unique relationship of fPrP11–12 with CJD phenotype supports the view that the phenotypic heterogeneity of CJD is related to the formation of different types of disease-specific PrP and fragments thereof.
Present address: The First Department of Internal Medicine, Nagasaki University School of Medicine, Nagasaki, Japan.
This article has been cited by other articles:
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