?- and ?-secretase: Profound changes in Alzheimer's disease

Dawbarn, David; Tyler, Susan J.; Allen, Shelley J.; Wilcock, Gordon

Abstract

The amyloid plaque, a neuropathological hallmark of Alzheimer's disease, is produced by the deposition of β-amyloid (Aβ) peptide, which is cleaved from Amyloid Precursor Protein (APP) by the enzyme β-secretase. Only small amounts of Aβ form in normal brain; more typically this is precluded by the processing of APP by α-secretase. Here, we describe a decrease in α-secretase (81% of normal) and a large increase in β-secretase activity (185%) in sporadic Alzheimer's disease temporal cortex. Since α-secretase is present principally in neurons known to be vulnerable in Alzheimer's disease, and there is known competition between α- and β-secretase for the substrate APP, it is significant that the majority of Alzheimer samples tested here were low in α-secretase. Eighty percent of Alzheimer brains examined had an increase in β-secretase, a decrease in α-secretase, or both; which may account for the means by which the majority of people develop Alzheimer's disease. © 2002 Elsevier Science (USA). All rights reserved.

Citation

Allen, S. J., Dawbarn, D., Tyler, S. J., & Wilcock, G. (2002). ?- and ?-secretase: Profound changes in Alzheimer's disease. Biochemical and Biophysical Research Communications, 299(3), 373-376. https://doi.org/10.1016/S0006-291X%2802%2902635-9

• Journal Article Type: Article
• Publication Date: Dec 2, 2002
• Journal: Biochemical and Biophysical Research Communications
• Print ISSN: 0006-291X
• Publisher: Elsevier
• Peer Reviewed: Not Peer Reviewed
• Volume: 299
• Issue: 3
• Pages: 373-376
• DOI: https://doi.org/10.1016/S0006-291X%2802%2902635-9
• Keywords: secretase, Alzheimer's disease
• Public URL: https://uwe-repository.worktribe.com/output/1075483
• Publisher URL: http://dx.doi.org/10.1016/S0006-291X(02)02635-9