AI Article Synopsis
- The study focuses on the localization of 14.3.3 proteins in various brain amyloid plaques associated with different types of Creutzfeldt-Jakob disease as well as Alzheimer's disease.
- The researchers found that 14.3.3 zeta protein was present alongside abnormal prion protein (PrP(sc)) deposits in sporadic CJD and variant CJD, indicating a potential interaction between these proteins.
- However, in cases of GSS and Alzheimer's disease, 14.3.3 zeta did not co-occur with the amyloid plaques, suggesting that its role may be specific to certain prion diseases rather than general amyloid pathologies.
Article Abstract
The localization of 14.3.3 proteins was studied in different subtypes of brain amyloid plaques. We examined paraffin-embedded brain sections of sporadic MV2 Creutzfeldt-Jakob disease (sCJD) with Kuru plaques, sporadic VV2 CJD with plaque-like PrP(sc) (the abnornal form of prion protein) deposits, variant CJD (vCJD) with florid plaques, Gerstmann-Straüssler-Scheinker (GSS) with multicentric plaques and of Alzheimer's disease (AD) with senile plaques. Adjacent immunostaining revealed PrP(sc) and 14.3.3 zeta deposits in the same amyloid plaques in all cases of sporadic CJD and vCJD, whereas 14.3.3 zeta was not seen in amyloid plaques of GSS with A117V, P102L and D202N mutations. The same immunostaining method using anti-betaA4 and anti-14.3.3 zeta antibodies revealed no colocalization in patients with AD. Our data suggest that 14.3.3 zeta protein could interact either with PrP or with other components of PrP(sc) deposits in CJD.
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| http://dx.doi.org/10.1007/s00401-002-0642-5 | DOI Listing |
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