Regulation of AβPP Glycosylation Modification and Roles of Glycosylation on AβPP Cleavage in Alzheimer's Disease

ACS Chemical Neuroscience
Peng-Fei Tao, Han-Chang Huang

Abstract

The presence of senile plaques in the gray matter of the brain is one of the major pathologic features of Alzheimer's disease (AD), and amyloid-β (Aβ) is the main component of extracellular deposits of the senile plaques. Aβ derives from amyloid-β precursor protein (AβPP) cleaved by β-secretase (BACE1) and γ-secretase, and the abnormal cleavage of AβPP is an important event leading to overproduction and aggregation of Aβ species. After translation, AβPP undergoes post-translational modifications (PTMs) including glycosylation and phosphorylation in the endoplasmic reticulum (ER) and Golgi apparatus, and these modifications play an important role in regulating the cleavage of this protein. In this Review, we summarize research progress on the modification of glycosylation, especially O-GlcNAcylation and mucin-type O-linked glycosylation (also known as O-GalNAcylation), on the regulation of AβPP cleavage and on the influence of AβPP's glycosylation in the pathogenesis of AD.

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Citations

Dec 22, 2019·Chembiochem : a European Journal of Chemical Biology·Madhu RameshThimmaiah Govindaraju
Aug 14, 2020·Alzheimer's Research & Therapy·Claudia P BoixJavier Sáez-Valero
Nov 10, 2020·Journal of Alzheimer's Disease : JAD·Xinquan LiBiao Cai

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