Incubation of isolated proteasomes with PHF-tau isolated from AD brain, and with PHFs after in vitro assembly from human recombinant tau protein, resulted in a distinct inhibition of proteasome activity by PHF-tau.
This study evaluated the sensitivity and specificity of the cerebrospinal fluid (CSF) levels of tau-protein, amyloid-beta-peptide 1-42 (Abeta1-42), ApoE-genotype and the degree of cognitive decline as diagnostic markers for Alzheimer's disease (AD).
To investigate the role of tau glycosylation in neurofibrillary pathology, we isolated various pools of tau protein from AD brain which represent different stages of tau pathology.
Microtubule associated protein tau is abnormally phosphorylated in Alzheimer's disease (AD) and aggregates as paired helical filaments (PHFs) in neurofibrillary tangles (NFTs).
Thus, we analyzed insoluble (pathological) tau proteins in five argyrophilic grain disease brains in comparison with those seen in Alzheimer's disease and Pick's disease.