1. Creutzfeldt-Jakob disease with a novel extra-repeat insertional mutation in the PRNP gene
- Author
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Vladimiro Pietrini, Puoti, G., Limido, L., Rossi, G., Di Fede, G., Giaccone, G., Mangieri, M., Tedeschi, F., Bondavalli, A., Mancia, D., Bugiani, O., Tagliavini, F., Pietrini, V, Puoti, Gianfranco, Limido, L, Rossi, G, DI FEDE, G, Giaccone, G, Mangieri, M, Tedeschi, F, Bondavalli, A, Mancia, D, Bugiani, O, and Tagliavini, F.
- Subjects
Brain Chemistry ,Male ,Amyloid ,Heterozygote ,Tyrosine 3-Monooxygenase ,Prions ,Homozygote ,Immunoblotting ,Brain ,Electroencephalography ,tau Proteins ,Middle Aged ,Immunohistochemistry ,Polymerase Chain Reaction ,Creutzfeldt-Jakob Syndrome ,Prion Proteins ,14-3-3 Proteins ,Endopeptidases ,Mutation ,Humans ,Neurology (clinical) ,Protein Precursors - Abstract
—The authors investigated two unrelated patients with Creutzfeldt-Jakob disease (CJD) with clinical features of sporadic CJD (sCJD) carrying one extra octapeptide repeat in the prion protein (PrP) gene (PRNP). A synaptic type PrP distribution throughout the cerebral gray matter and plaque-like PrP deposits in the subcortical gray structures were detected immunocytochemically. The different patterns of PrP deposition were associated with distinct types of proteaseresistant PrP, similar to type 1 and type 2 of sCJD. The features suggest that this insertion is a pathogenic mutation.