Biogenesis and metabolism of Alzheimer's disease Abeta amyloid peptides |
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Authors: | Evin Geneviève Weidemann Andreas |
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Affiliation: | Department of Pathology, The University of Melbourne and Mental Health Research Institute, Parkville, Vic. 3010, Australia. gmevin@unimelb.edu.au. |
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Abstract: | Biochemical and genetic evidence indicates the balance of biogenesis/clearance of Abeta amyloid peptides is altered in Alzheimer's disease. Abeta is derived, by two sequential cleavages, from the receptor-like amyloid precursor protein (APP). The proteases involved are beta-secretase, identified as the novel aspartyl protease BACE, and gamma-secretase, a multimeric complex containing the presenilins (PS). Gamma-secretase can release either Abeta40 or the more aggregating and cytotoxic Abeta42. Secreted Abeta peptides become either degraded by the metalloproteases insulin-degrading enzyme (IDE) and neprilysin or metabolized through receptor uptake mediated by apolipoprotein E. Therapeutic approaches based on secretase inhibition or amyloid clearance are currently under development. |
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