A cellular model of amyloid precursor protein processing and amyloid-β peptide production

Journal of Neuroscience Methods
Mimi P MaciasBoris Decourt

Abstract

A hallmark pathologic feature of Alzheimer's disease (AD) is accumulation of neuritic senile plaques in the brain parenchyma. Neurotoxic plaque cores are composed predominantly of amyloid-β (Aβ) peptides of 40 and 42 amino acids in length, formed by sequential cleavage of amyloid precursor protein (APP) by β-, and γ-secretases. There is a great interest in approaches to modulate Aβ peptide production and develop therapeutic interventions to reduce Aβ levels to halt or slow the progression of neurodegeneration. We characterized and present the BE(2)-M17 human neuroblastoma cell line as a novel in vitro model of the APP-cleavage cascade to support future (1) functional studies of molecular regulators in Aβ production, and (2) high-throughput screening assays of new pharmacotherapeutics. In BE(2)-M17 cells, both RNA (i.e., RT-PCR, RNA sequencing) and protein analyses (i.e., Western blots, ELISA), show endogenous expression of critical components of the amyloidogenic pathway, APP-cleavage intermediates CTF83 and CTF99, and final cleavage products Aβ40 and Aβ42. We further report effects of retinoic acid-mediated differentiation on morphology and gene expression in this cell line. In contrast to primary isolates or other cell lines ...Continue Reading

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Citations

Mar 1, 2015·Neuropharmacology·Marta LeirósLuis M Botana
May 11, 2016·Journal of Alzheimer's Disease : JAD·Julie ColinCatherine Malaplate-Armand
Dec 18, 2015·International Journal of Molecular Medicine·Xueyuan LiRenzhi Wang
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Jun 10, 2019·Journal of Alzheimer's Disease : JAD·Richard McClureWellington Pham
Jan 5, 2019·BMC Research Notes·Li-Mei Chen, Karl X Chai
Oct 18, 2020·Molecular and Cellular Neurosciences·Giovanna CeniniOliver Brüstle

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