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  • Title: Isoaspartate formation at position 23 of amyloid beta peptide enhanced fibril formation and deposited onto senile plaques and vascular amyloids in Alzheimer's disease.
    Author: Shimizu T, Fukuda H, Murayama S, Izumiyama N, Shirasawa T.
    Journal: J Neurosci Res; 2002 Nov 01; 70(3):451-61. PubMed ID: 12391606.
    Abstract:
    Senile plaques and amyloid-bearing vessels consisting of fibrillar amyloid beta peptides (A beta) are characteristic neuropathological features of Alzheimer's disease (AD). A beta undergo spontaneous post-translational modifications, such as isomerization and racemization, at their aspartyl residues in AD brains. Here we present evidence that A beta isomerized at position 23 are deposited on plaques and vascular amyloids using an anti-isomerized A beta antibody. In vitro experiments showed that isomerization at position 23, but not position 7, enhanced aggregation. Furthermore, A beta with the Dutch mutation, but not the Flemish mutation, also showed greatly enhanced aggregation. These results suggest that mutations or modifications at positions Glu 22 and Asp 23 have a pathogenic role in the deposition of A beta. The development and progression of sporadic AD may be accelerated by spontaneous isomerization at position 23 of A beta.
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