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lüll APP processing in Alzheimer s disease Zhang YW; Thompson R; Zhang H; Xu HMol Brain 2011[Jan]; 4 (ä): 3An 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 (Abeta). Multiple lines of evidence demonstrate that overproduction/aggregation of Abeta in the brain is a primary cause of AD and inhibition of Abeta generation has become a hot topic in AD research. Abeta 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 Abeta domain to release soluble APPalpha and preclude Abeta 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.|Alzheimer Disease/*metabolism/pathology/physiopathology[MESH]|Amyloid Precursor Protein Secretases/metabolism[MESH]|Amyloid beta-Peptides/biosynthesis/genetics[MESH]|Amyloid beta-Protein Precursor/genetics/*metabolism[MESH]|Animals[MESH]|Caspases/metabolism[MESH]|Humans[MESH]|Isoenzymes/metabolism[MESH]|Plaque, Amyloid/pathology[MESH]|Signal Transduction/physiology[MESH] |