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A protease activity associated with acetylcholinesterase releases the membrane-bound form of the amyloid protein precursor of Alzheimer's disease

Citation

Small, DH and Moir, RD and Fuller, S and Michaelson, S and Bush, AI and Li, QX and Milward, E and Hilbich, C and Weidemann, A and Beyreuther, K and Masters, CL, A protease activity associated with acetylcholinesterase releases the membrane-bound form of the amyloid protein precursor of Alzheimer's disease, Biochemistry, 30, (44) pp. 10795-10799. ISSN 0006-2960 (1991) [Refereed Article]

Copyright Statement

Copyright 1991 American Chemical Society

DOI: doi:10.1021/bi00108a027

Abstract

Amyloid deposits in the brains of patients with Alzheimer’s disease (AD) contain a protein (βA4) which is abnormally cleaved from a larger transmembrane precursor protein (APP). APP is believed to be normally released from membranes by the action of a protease referred to as APP secretase. Amyloid deposits have also been shown to contain the enzyme acetylcholinesterase (AChE). In this study, a protease activity associated with AChE was found to possess APP secretase activity, stimulating the relase of a soluble 100K form of APP from HeLa cells transfected with an APP cDNA. The AChE-associated protease was strongly and specifically inhibited by soluble APP (10 nM) isolated from human brain. The AChE-associated protease cleaved a synthetic βA4 peptide at the predicted cleavage site. As AChE is decreased in AD, a deficiency of its associated protease might explain why APP is abnormally processed in AD. © 1991, American Chemical Society. All rights reserved.

Item Details

Item Type:Refereed Article
Research Division:Medical and Health Sciences
Research Group:Neurosciences
Research Field:Neurosciences not elsewhere classified
Objective Division:Health
Objective Group:Clinical Health (Organs, Diseases and Abnormal Conditions)
Objective Field:Neurodegenerative Disorders Related to Ageing
Author:Small, DH (Professor David Small)
ID Code:75469
Year Published:1991
Web of Science® Times Cited:66
Deposited By:Research Division
Deposited On:2012-01-31
Last Modified:2013-05-07
Downloads:1 View Download Statistics

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