Accumulation of the amyloid-b (Ab) plaque in the cerebral cortex is a critical event in the pathogenesis of 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 suffers 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) (1-4). BACE/Asp2 is a novel transmembrane aspartic protease and colocalizes with APP.
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Western blot analysis of BACE in human brain tissue lysate in the absence (A) or presence (B) of blocking peptide (2253P) and in mouse 3T3 cell lysate (C) with BACE antibody at 1 ug/ml.
