η-Secretase: Reduction of Amyloid Precursor Protein η-Site Cleavage in Alzheimers Disease (original) (raw)

The accumulation and deposition of fibrillar Aβ is thought the primary cause of Alzheimers disease (AD). Aβ is generated by sequential proteolytic processing involving β- and γ-secretase on Amyloid β protein precursor (APP). Recently, γ-secretase was shown to cleave near the cytoplasmic membrane boundary of APP, called η-site cleavage, as well as in the middle of the membrane domain, called γ-site cleavage. Recent findings indicate that γ- and η-site cleavage are regulated independently. In this review, the reduction of η-site cleavage in AD and the importance of η-site cleavage are discussed.

Keywords: Alzheimer's disease, APP, presenilin, γ-secretase, Aβ, AICD, η-secretase