Journal
MOLECULAR BRAIN
Volume 4, Issue -, Pages -Publisher
BMC
DOI: 10.1186/1756-6606-4-3
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Funding
- National Institutes of Health [R01AG021173, R01NS046673, R01AG030197, R03AG034366]
- Alzheimer's Association
- American Health Assistance Foundation
- National Natural Science Foundation of China [30973150]
- National S&T Major Project of China [2009ZX09103-731]
- 973 Prophase Project [2010CB535004]
- Natural Science Funds for Distinguished Young Scholar of Fujian Province [2009J06022]
- Program for New Century Excellent Talents in Universities (NCET)
- Fundamental Research Funds for the Central Universities
- Fok Ying Tung Education Foundation
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An important pathological feature of Alzheimer's disease (AD) is the presence of extracellular senile plaques in the brain. Senile plaques are composed of aggregations of small peptides called beta-amyloid (A beta). Multiple lines of evidence demonstrate that overproduction/aggregation of A beta in the brain is a primary cause of AD and inhibition of A beta generation has become a hot topic in AD research. A beta is generated from beta-amyloid precursor protein (APP) through sequential cleavages first by beta-secretase and then by gamma-secretase complex. Alternatively, APP can be cleaved by alpha-secretase within the A beta domain to release soluble APP alpha and preclude A beta generation. Cleavage of APP by caspases may also contribute to AD pathologies. Therefore, understanding the metabolism/processing of APP is crucial for AD therapeutics. Here we review current knowledge of APP processing regulation as well as the patho/physiological functions of APP and its metabolites.
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