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Arch Physiol Biochem. 2020 Feb 12:1-8. doi: 10.1080/13813455.2020.1722707. [Epub ahead of print]

In vitro study of the mechanism of intraneuronal β-amyloid aggregation in Alzheimer's disease.

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Biochemistry department, Faculty of science, King Abdulaziz University (KAU), Jeddah, Saudi Arabia.
Biochemistry Department, Faculty of science and Experimental Biochemistry Unit, King Fahd Medical Research Center and Production of Bio-products for Industrial Applications Research Group, KAU, Jeddah, Saudi Arabia.
Department of Molecular Biology and Biochemistry, University of California, Irvine, CA, USA.
Biochemistry department, Faculty of Science, KAU and Production of Bio-Products for Industrial Applications Research Group, Jeddah, Saudi Arabia.
Biochemistry Department, Faculty of Science, Cairo, Egypt.


Alzheimer's disease (AD) is atrophy of brain cells that lead to decline in the mental capacity and memory. This study investigated the mechanism which postulates that intraneuronal accumulation of amyloid aggregates for pathogenesis of AD. The PC12 cell line was used to examine the amyloid beta (Aβ) aggregation in different stages. It was found that dot-blot filter retardation assay for Ub-CTF was 0.25 and 0.2 µM for SS-CTF. In addition, incubation of SS-CTF with 200 µM Aβ-42 then bounded with an antibody directed against Aβ. It was suggested that most bound Aβ-42 in the oligomeric form. Confocal microscope showed that stained with DAPI (blue) in the neuritic plaques, APP-GFP (green) and specific monoclonal M78 (red). Aß oligomeric taken up by neurons and accumulation of misfolded Aß aggregates continue in a perinuclear location. Fluorescence intensities correlate with the priming effect observed on the Aβ (p < .001). It was concluded that a new amyloid hypothesis is promising in therapy development to reduce the incidence of disease by inhibition of intraneuronal amyloid aggregation.


Alzheimer disease; PC12; aggregation; amyloid β-protein

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