Abstract
It was difficult to make a definite pathological diagnosis in a 73-year-old man with Creutzfeldt-Jakob disease (CJD) due to extensive amyloid angiopathy which lacked any severe spongiform changes. Immunostaining using anti-prion protein (PrP) antibody revealed fine granular deposits in the gray matter, after hydrolytic autoclaving pretreatment on tissue sections. Western blotting also revealed an abnormal isoform of PrP, but PrP gene analysis did not show any abnormalities. The primary transmission experiments were repeated three times and induced spongiform encephalopathy in a few mice after a long incubation period.
Original language | English |
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Pages (from-to) | 559-563 |
Number of pages | 5 |
Journal | Acta neuropathologica |
Volume | 83 |
Issue number | 5 |
DOIs | |
Publication status | Published - 1992 Apr 1 |
Externally published | Yes |
Keywords
- Amyloid angiopathy
- Creutzfeldt-Jakob disease
- Experimental transmission
- Immunohistochemistry
- Prion protein
ASJC Scopus subject areas
- Pathology and Forensic Medicine
- Clinical Neurology
- Cellular and Molecular Neuroscience