Regulation of APP cleavage by α‐, β‐ and γ‐secretases

FEBS Letters

Nunan, Janelle¹  Small, David H¹ 

[1] Laboratory of Molecular Neurobiology, Department of Pathology, University of Melbourne, Melbourne, Vic. 3010, Australia

关键词: Alzheimer's disease;    Amyloid protein precursor;    Secretase;    Dementia;   

DOI  :  10.1016/S0014-5793(00)02076-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Proteolytic cleavage of the amyloid protein from the amyloid protein precursor (APP) by APP secretases is a key event in Alzheimer's disease (AD) pathogenesis. α-Secretases cleave APP within the amyloid sequences, whereas β- and γ-secretases cleave on the N- and C-terminal ends respectively. The transmembrane aspartyl protease BACE has been identified as β-secretase and several proteases (ADAM-10, TACE, PC7) may be α-secretases. A number of studies have suggested that presenilins could be γ-secretases, although this remains to be demonstrated conclusively. Inhibition of β- and γ-secretase, or stimulation of α-secretase, is a rational strategy for therapeutic intervention in AD.

【 授权许可】

Unknown