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  • Title: Characterization of insulin-degrading enzyme-mediated cleavage of Aβ in distinct aggregation states.
    Author: Hubin E, Cioffi F, Rozenski J, van Nuland NA, Broersen K.
    Journal: Biochim Biophys Acta; 2016 Jun; 1860(6):1281-90. PubMed ID: 26968463.
    Abstract:
    To enhance our understanding of the potential therapeutic utility of insulin-degrading enzyme (IDE) in Alzheimer's disease (AD), we studied in vitro IDE-mediated degradation of different amyloid-beta (Aβ) peptide aggregation states. Our findings show that IDE activity is driven by the dynamic equilibrium between Aβ monomers and higher ordered aggregates. We identify Met(35)-Val(36) as a novel IDE cleavage site in the Aβ sequence and show that Aβ fragments resulting from IDE cleavage form non-toxic amorphous aggregates. These findings need to be taken into account in therapeutic strategies designed to increase Aβ clearance in AD patients by modulating IDE activity.
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