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Article type: Research Article
Authors: Mukherjee, Atish | Hersh, Louis B.; *
Affiliations: Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY 40536-0298, USA
Correspondence: [*] Corresponding author: Louis B. Hersh, Department of Molecular and Cellular Biochemistry, University of Kentucky, College of Medicine, 800 Rose St. Lexington, KY 40536-0298, USA. Tel.: +1 859 323 5549; Fax: +1 859 323 1727; E-mail: lhersh@uky.edu.
Abstract: It is generally accepted that amyloid β peptides (Aβ) play a significant role in the etiology of Alzheimer's disease. The Aβ peptides are produced by the sequential cleavage of an amyloid precursor protein by a βsecretase followed by cleavage by a γ secretase. The clearance of β appears to be due primarily by the action of one or more peptidases. An imbalance between the rate of synthesis and the rate of clearance of Aβ is now considered a possible contributor to the onset of Alzheimer's disease. This review focuses on peptidases that have been proposed to contribute to Aβ catabolism and discusses the evidence for their participation in Aβ peptide clearance in vivo.
DOI: 10.3233/JAD-2002-4501
Journal: Journal of Alzheimer's Disease, vol. 4, no. 5, pp. 341-348, 2002
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