Accumulation of the amyloid- (A ) plaque in the cerebral cortex is a critical event in the pathogenesis of AlzheimerÕs disease. A peptide is generated by proteolytic cleavage of the amyloid protein precursor (APP) at - and -sites by two proteases. APP is first cleaved by 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 secretase to generate the 4 kDa amyloid- peptide, which is deposited in the brains of all suffers of AlzheimerÕs disease. The long-sought secretase was recently identified by several groups independently and designated beta-site APP cleaving enzyme (BACE) and aspartyl protease 2 (Asp2)1-4. BACE/Asp2 is a novel transmembrane aspartic protease and colocalizes with APP.
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