Phosphorylation and Glycosylation of Amyloid-β Protein Precursor: The Relationship to Trafficking and Cleavage in Alzheimer's Disease

被引:9
|
作者
Song, Xi-Jun [1 ,2 ]
Zhou, He-Yan [1 ,2 ]
Sun, Yu-Ying [1 ,2 ]
Huang, Han-Chang [1 ,2 ]
机构
[1] Beijing Union Univ, Beijing Key Lab Bioact Subst & Funct Foods, 197 Beitucheng West Rd, Beijing 100191, Peoples R China
[2] Beijing Union Univ, Res Inst Funct Factors & Brain Sci, Beijing, Peoples R China
关键词
Alzheimer's disease; amyloid-beta protein precursor; protein glycosylation; protein phosphorylation; TRANS-GOLGI NETWORK; N-ACETYLGLUCOSAMINE LEVELS; CELL-SURFACE; A-BETA; O-GLYCOSYLATION; INTRACELLULAR DOMAIN; TRANSCRIPTIONAL ACTIVITY; METALLOPROTEASE MEPRIN; ENDOPLASMIC-RETICULUM; LINKED GLYCOSYLATION;
D O I
10.3233/JAD-210337
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
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-beta (A beta) peptide is the main constituent of senile plaques, and this peptide is derived from the amyloid-beta protein precursor (A beta PP) through the successive cleaving by beta-site A beta PP-cleavage enzyme 1 (BACE1) and beta-secretase. A beta PP undergoes the progress of post-translational modifications, such as phosphorylation and glycosylation, which might affect the trafficking and the cleavage of A beta PP. In the recent years, about 10 phosphorylation sites of A beta PP were identified, and they play complex roles in glycosylation modification and cleavage of A beta PP. In this article, we introduced the transport and the cleavage pathways of A beta PP, then summarized the phosphorylation and glycosylation sites of A beta PP, and further discussed the links and relationship between phosphorylation and glycosylation on the pathways of A beta PP trafficking and cleavage in order to provide theoretical basis for AD research.
引用
收藏
页码:937 / 957
页数:21
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