scholarly journals The amyloid beta-protein precursor of Alzheimer's disease is degraded extracellularly by a Kunitz protease inhibitor domain-sensitive trypsin-like serine protease in cultures of chick sympathetic neurons

1999 ◽  
Vol 266 (2) ◽  
pp. 509-516 ◽  
Author(s):  
Mark D. Caswell ◽  
Su San Mok ◽  
Anna Henry ◽  
Roberto Cappai ◽  
Genevieve Klug ◽  
...  
2002 ◽  
Vol 38 ◽  
pp. 37-49 ◽  
Author(s):  
Janelle Nunan ◽  
David H Small

The proteolytic processing of the amyloid-beta protein precursor plays a key role in the development of Alzheimer's disease. Cleavage of the amyloid-beta protein precursor may occur via two pathways, both of which involve the action of proteases called secretases. One pathway, involving beta- and gamma-secretase, liberates amyloid-beta protein, a protein associated with the neurodegeneration seen in Alzheimer's disease. The alternative pathway, involving alpha-secretase, precludes amyloid-beta protein formation. In this review, we describe the progress that has been made in identifying the secretases and their potential as therapeutic targets in the treatment or prevention of Alzheimer's disease.


Biochemistry ◽  
1990 ◽  
Vol 29 (43) ◽  
pp. 10018-10022 ◽  
Author(s):  
Thomas R. Hynes ◽  
Michael Randal ◽  
Laura A. Kennedy ◽  
Charles Eigenbrot ◽  
Anthony A. Kossiakoff

2000 ◽  
Vol 54 (1) ◽  
pp. 45-54 ◽  
Author(s):  
Mikio Shoji ◽  
Takeshi Kawarabayashi ◽  
Etsuro Matsubara ◽  
Masaki Ikeda ◽  
Koji Ishiguro ◽  
...  

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