The insidious progression of AD (Alzheimer's disease) is believed to be linked closely to the production, accumulation and aggregation of the ∼4.5 kDa protein fragment called Aβ (amyloid β-peptide). Aβ is produced by sequential cleavage of the amyloid precursor protein by two enzymes referred to as β- and γ-secretase. β-Secretase is of central importance, as it catalyses the rate-limiting step in the production of Aβ and was identified 7 years ago as BACE1 (β-site APP-cleaving enzyme 1). Soon afterwards, its homologue BACE2 was discovered, and both proteins represent a new subclass of the aspartyl protease family. Studies examining the regulation and function of β-secretase in the normal and AD brain are central to the understanding of excessive production of Aβ in AD, and in targeting and normalizing this β-secretase process if it has gone awry in the disease. Several reports indicate this, showing increased β-secretase activity in AD, with recent findings by our group showing changes in β-secretase enzyme kinetics in AD brain caused by an increased Vmax. This article gives a brief review of studies which have examined BACE1 protein levels and β-secretase activity in control and AD brain, considering further the expression of BACE2 in the human brain.
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June 2007
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Conference Article|
May 22 2007
The proteins BACE1 and BACE2 and β-secretase activity in normal and Alzheimer's disease brain
J.H. Stockley;
J.H. Stockley
1Department of Biochemistry, BioSciences Institute, University College Cork, Cork, Ireland
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C. O'Neill
C. O'Neill
1
1Department of Biochemistry, BioSciences Institute, University College Cork, Cork, Ireland
1To whom correspondence should be addressed (email c.oneill@ucc.ie).
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Publisher: Portland Press Ltd
Received:
February 19 2007
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2007 Biochemical Society
2007
Biochem Soc Trans (2007) 35 (3): 574–576.
Article history
Received:
February 19 2007
Citation
J.H. Stockley, C. O'Neill; The proteins BACE1 and BACE2 and β-secretase activity in normal and Alzheimer's disease brain. Biochem Soc Trans 1 June 2007; 35 (3): 574–576. doi: https://doi.org/10.1042/BST0350574
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