Abstract
Water‐soluble amyloid β‐peptides (sAβ), ending at residue 42, precede amyloid plaques in Down's syndrome (DS). Here we report that sAβ consists of the full‐length Aβ1–42 and peptides truncated and modified by cyclization of the N‐terminal glutamates, Aβ3(pE)–42 and Aβ11(pE)–42. The Aβ3(pE)–42 peptide is the most abundant form of sAβ in Alzheimer's disease (AD) brains. In DS, sAβ3(pE)–42 concentration increases with age and the peptide becomes a dominant species in the presence of plaques. Both pyroglutamate‐modified peptides and the full‐length Aβ form a stable aggregate that is water soluble. The findings point to a crucial role of the aggregated and modified sAβ in the plaque formation and pathogenesis of AD.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 25, 2002, 3:16 p.m.) |
Deposited | 1 year, 11 months ago (Sept. 16, 2023, 1:51 p.m.) |
Indexed | 2 days, 9 hours ago (Sept. 4, 2025, 9:34 a.m.) |
Issued | 28 years, 2 months ago (June 16, 1997) |
Published | 28 years, 2 months ago (June 16, 1997) |
Published Online | 27 years, 9 months ago (Nov. 7, 1997) |
Published Print | 28 years, 2 months ago (June 16, 1997) |
@article{Russo_1997, title={Heterogeneity of water‐soluble amyloid β‐peptide in Alzheimer’s disease and Down’s syndrome brains}, volume={409}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/s0014-5793(97)00564-4}, DOI={10.1016/s0014-5793(97)00564-4}, number={3}, journal={FEBS Letters}, publisher={Wiley}, author={Russo, Claudio and Saido, Takaomi C. and DeBusk, Laura M. and Tabaton, Massimo and Gambetti, Pierluigi and Teller, Jan K.}, year={1997}, month=jun, pages={411–416} }