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Current Alzheimer Research


ISSN (Print): 1567-2050
ISSN (Online): 1875-5828

η-Secretase: Reduction of Amyloid Precursor Protein η-Site Cleavage in Alzheimers Disease

Author(s): Fuyuki Kametani

Volume 5, Issue 2, 2008

Page: [165 - 171] Pages: 7

DOI: 10.2174/156720508783954776

Price: $65


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, , AICD, η-secretase

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