scholarly journals Human aspartic protease memapsin 2 cleaves the beta -secretase site of beta -amyloid precursor protein

2000 ◽  
Vol 97 (4) ◽  
pp. 1456-1460 ◽  
Author(s):  
X. Lin ◽  
G. Koelsch ◽  
S. Wu ◽  
D. Downs ◽  
A. Dashti ◽  
...  
2003 ◽  
Vol 70 ◽  
pp. 213-220 ◽  
Author(s):  
Gerald Koelsch ◽  
Robert T. Turner ◽  
Lin Hong ◽  
Arun K. Ghosh ◽  
Jordan Tang

Mempasin 2, a ϐ-secretase, is the membrane-anchored aspartic protease that initiates the cleavage of amyloid precursor protein leading to the production of ϐ-amyloid and the onset of Alzheimer's disease. Thus memapsin 2 is a major therapeutic target for the development of inhibitor drugs for the disease. Many biochemical tools, such as the specificity and crystal structure, have been established and have led to the design of potent and relatively small transition-state inhibitors. Although developing a clinically viable mempasin 2 inhibitor remains challenging, progress to date renders hope that memapsin 2 inhibitors may ultimately be useful for therapeutic reduction of ϐ-amyloid.


2004 ◽  
Vol 36 (12) ◽  
pp. 787-792 ◽  
Author(s):  
Lin Hong ◽  
Xiangyuan He ◽  
Xiangping Huang ◽  
Wanpin Chang ◽  
Jordan Tang

Abstract Memapsin 2 (β-secretase) is the membrane-anchored aspartic protease that initiates the cleavage of β-amyloid precursor protein (APP) leading to the production of amyloid-β (Aβ), a major factor in the pathogenesis of Alzheimer's disease (AD). Since memapsin 2 is a major target for the development of inhibitor drugs for AD, it has been intensively studied during the past five years. Here we discuss the structural features of the catalytic/specificity apparatus, transmembrane domain, cytosolic domain and the implications of these features in the physiological and pathological roles of this protease.


1990 ◽  
Vol 265 (16) ◽  
pp. 8983-8985 ◽  
Author(s):  
S Sinha ◽  
H F Dovey ◽  
P Seubert ◽  
P J Ward ◽  
R W Blacher ◽  
...  

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