Fuyuki Kametani Pages 165 - 171 ( 7 )
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.
Alzheimer's disease, APP, presenilin, γ-secretase, Aβ, AICD, η-secretase
Tokyo Institute of Psychiatry,Tokyo Metropolitan Organization for Medical Research, 2-1-8 Kamikitazawa,Setagaya-ku, Tokyo 156-8585, Japan.