Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-4646
Debatin, L; Streffer, J; Geissen, M; Matschke, J; Aguzzi, A; Glatzel, M (2008). Association between deposition of beta-amyloid and pathological prion protein in sporadic Creutzfeldt-Jakob disease. Neuro-degenerative Diseases, 5(6):347-354.
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BACKGROUND: Alzheimer's disease (AD) and prion diseases such as sporadic Creutzfeldt-Jakob disease (sCJD) share common features concerning their molecular pathogenesis and neuropathological presentation and the coexistence of AD and CJD in patients suggest an association between the deposition of the proteolytically processed form of the amyloid precursor protein, beta-amyloid (Abeta), which deposits in AD, and the abnormal form of the prion protein, PrP(Sc), which deposits in sCJD. METHODS: We have characterized sCJD patients (n = 14), AD patients (n = 5) and nondemented controls (n = 5) with respect to the deposition of PrP(Sc) and Abeta morphologically, biochemically and genetically and correlated these findings to clinical data. RESULTS: sCJD-diseased individuals with abundant deposits of Abeta present with a specific clinicopathological profile, defined by higher age at disease onset, long disease duration, a genetic profile and only minimal amounts of PrP(Sc) in the cerebellum. CONCLUSION: The co-occurrence of pathological changes typical for sCJD and AD in combination with the inverse association between accumulation of Abeta and PrP(Sc) in a subgroup of sCJD patients is indicative of common pathways involved in the generation or clearance of Abeta and PrP(Sc) in a subgroup of sCJD patients.
|Item Type:||Journal Article, refereed, original work|
|Communities & Collections:||04 Faculty of Medicine > Psychiatric University Hospital Zurich > Division of Psychiatric Research and Clinic for Psychogeriatric Medicine|
04 Faculty of Medicine > University Hospital Zurich > Institute of Neuropathology
|DDC:||570 Life sciences; biology|
610 Medicine & health
|Date:||18 March 2008|
|Deposited On:||03 Nov 2008 13:37|
|Last Modified:||28 Nov 2013 01:19|
|Citations:||Web of Science®. Times Cited: 24|
Scopus®. Citation Count: 23
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