The β-amyloid peptide (β A4), proteolytically released from the amyloid precursor protein (APP), provides the principal component of senile plaques in Alzheimer’s disease. Cleavage of APP by α-secretase or alternatively by β-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-α and S-APP-β, respectively, and the retention of corresponding membrane-anchored C-terminal fragments, C83 and C99. Subsequent processing of C83 by γ-secretase yields P3 peptides. This is the major secretory pathway and is nonamyloidogenic. Alternatively, presenilin/ nicastrin-mediated γ-secretase processing of C99 releases the amyloid β proteins, amyloid-β 40 (Aβ40) and amyloid-β 42 (Aβ42), major components of amyloid plaques, and the cytotoxic C-terminal fragments, γ-CTF(50), γ-CTF(57) and γ-CTF(59).
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Regulatory Status |
RUO – Research Use Only |
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