Accumulation of the amyloid-b (Ab) plaque in the cerebral cortex is a critical event in the pathogenesis Alzheimer's disease. Ab peptide is generated by proteolytic cleavage of the b-amyloid protein precursor(APP) at b- and g-sites by two proteases. APP is first cleaved by b-secretase, producing a soluble derivative of the protein and a membrane anchored 99-amino acid carboxy-terminal fragment (C99). The C99 fragment serves as substrate for g-secretase to generate the 4 kDa amyloid-b peptide, which is deposited in the brains of all sufferers of Alzheimer's disease. The long-sought b-secretase was recently identified by several groups independently and designated beta-site APP cleaving enzyme (BACE) and aspartyl protease 2 (Asp2). bACE/Asp2 is a novel transmembrane aspartic protease and colocalizes with APP.
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Protein Aliases: APP beta-secretase; asp 2; ASP2; Aspartyl protease 2; BACE 1; BACE-1D; BACE-I-432; Beta secretase; Beta-secretase 1; beta-secretase 1 precursor variant 1; beta-site amyloid beta A4 precursor protein-cleaving enzyme; Beta-site amyloid precursor protein cleaving enzyme 1; Beta-site APP cleaving enzyme 1; beta-site APP-cleaving enzyme 1; Memapsin; Memapsin-2; Memapsin2; Membrane-associated aspartic protease 2; transmembrane aspartic proteinase Asp2
Gene Aliases: ASP2; BACE; BACE1; C76936; HSPC104; KIAA1149; zgc:77409