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FIGURE 48–3. Proteolytic cleavage of amyloid precursor protein (APP) and amyloidogenesis.The APP molecule is metabolized via alternate pathways with distinct cleavages. A nonamyloidogenic pathway involves an -secretase cleavage (1) within the A peptide sequence (lightly shaded), shedding an N-terminal ectodomain. Degradation of the membrane-bound C-terminus does not produce A, because part of the peptide sequence has been cleaved. In contrast, A is produced via the amyloidogenic pathway involving sequential cleavages by -secretase (2) and -secretase (3). Presenilin is a necessary component for -secretase activity. The final -secretase cleavage releases A peptides of predominantly 40–42 amino acids. The longer 42-residue peptide is more toxic and hydrophobic, and it seeds aggregation into extracellular deposits of amyloid plaques. BACE = beta-site APP cleaving enzyme.

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