Affiliations: [a] Beijing Key Laboratory of Bioactive Substances and Functional Foods, Beijing Union University, Beijing, China
| [b] Research Institute of Functional Factors and Brain Science, Beijing Union University, Beijing, China
Correspondence:
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Correspondence to: Han-Chang Huang, Beijing Key Laboratory of Bioactive Substances and Functional Foods, Beijing Union University, No. 197, Beitucheng West Road, Haidian District, Beijing 100191, P. R. China. Tel.: +8610 62004534; E-mail: [email protected].
Abstract: Alzheimer’s disease (AD) is a neurodegenerative disorder in the central nervous system, and this disease is characterized by extracellular senile plaques and intracellular neurofibrillary tangles. Amyloid-β (Aβ) peptide is the main constituent of senile plaques, and this peptide is derived from the amyloid-β protein precursor (AβPP) through the successive cleaving by β-site AβPP-cleavage enzyme 1 (BACE1) and γ-secretase. AβPP undergoes the progress of post-translational modifications, such as phosphorylation and glycosylation, which might affect the trafficking and the cleavage of AβPP. In the recent years, about 10 phosphorylation sites of AβPP were identified, and they play complex roles in glycosylation modification and cleavage of AβPP. In this article, we introduced the transport and the cleavage pathways of AβPP, then summarized the phosphorylation and glycosylation sites of AβPP, and further discussed the links and relationship between phosphorylation and glycosylation on the pathways of AβPP trafficking and cleavage in order to provide theoretical basis for AD research.
Keywords: Alzheimer’s disease, amyloid-β protein precursor, protein glycosylation, protein phosphorylation
