Several lines of evidence indicate that the Aβ peptide is involved at some level in the pathological process that results in the clinical symptoms of AD (Alzheimer's disease). The N-terminus of Aβ is generated by cleavage of the Met-Asp bond at position 671–672 of APP (amyloid precursor protein), catalysed by a proteolytic activity called β-secretase. Two ‘β-secretase’ proteases have been identified: BACE (β-site APP-cleaving enzyme) and BACE2. The cause of sporadic AD is currently unknown, but some studies have reported elevated BACE/β-secretase activity in brain regions affected by the disease. We have demonstrated that robust β-secretase activity is also detectable in platelets that contain APP and release Aβ. This review considers the current evidence for alterations in β-secretase activity, and/or alterations in BACE expression, in post-mortem brain tissue and platelets from individuals with AD.
Expression and activity of β-site amyloid precursor protein cleaving enzyme in Alzheimer's disease
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J.A. Johnston, W.W. Liu, S.A. Todd, D.T.R. Coulson, S. Murphy, G.B. Irvine, A.P. Passmore; Expression and activity of β-site amyloid precursor protein cleaving enzyme in Alzheimer's disease. Biochem Soc Trans 26 October 2005; 33 (5): 1096–1100. doi: https://doi.org/10.1042/BST0331096
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