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Updated: Apr 2, 2026

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
Published on: October 17, 2015
Unique Expression and Glycosylation of Amyloid Precursor Protein in Alzheimer's Disease
Yuriko Tachida1, Shinobu Kitazume2
1Glycan and Life Systems Integration Center (GaLSIC), Soka University, Hachiōji, Japan.
Abstract:
Accumulation of amyloid β (Aβ) peptide in the brain is a characteristic pathological feature of Alzheimer's disease that occurs several decades before the onset of symptoms. Aβ is produced from the membrane-bound amyloid β precursor protein (APP) by β-secretase 1 (BACE1) and γ-secretase-mediated proteolytic cleavage. Alternatively, ADAM10/17 α-secretase and γ-secretase cleavage does not generate Aβ. Accumulating evidence indicates that intracellular trafficking of APP to each secretase determines the level of Aβ production. In this chapter, we summarize how glycosylation affects the Aβ production, possibly by modulating the intracellular localization of APP and its secretases.
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