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

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

Volume: 5 Issue: 2

Author(s): Fuyuki Kametani

Affiliation:

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

Abstract: 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.

Cite this article as:

Kametani Fuyuki, η-Secretase: Reduction of Amyloid Precursor Protein η-Site Cleavage in Alzheimers Disease, Current Alzheimer Research 2008; 5 (2) . https://dx.doi.org/10.2174/156720508783954776