Journal
JOURNAL OF ALZHEIMERS DISEASE
Volume 84, Issue 3, Pages 937-957Publisher
IOS PRESS
DOI: 10.3233/JAD-210337
Keywords
Alzheimer's disease; amyloid-beta protein precursor; protein glycosylation; protein phosphorylation
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Funding
- Academic Research Projects of Beijing Union University [JZ10202001, XP202008, ZK70202101]
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Alzheimer's disease is a neurodegenerative disorder characterized by extracellular senile plaques and intracellular neurofibrillary tangles. The main constituent of senile plaques, Aβ peptide, is derived from AβPP through cleaving by enzymes. Post-translational modifications like phosphorylation and glycosylation of AβPP may affect its trafficking and cleavage.
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.
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