Heterogeneity of water-soluble amyloid beta-peptide in Alzheimer's disease and Down's syndrome brains.

Abstract:

:Water-soluble amyloid beta-peptides (sA beta), ending at residue 42, precede amyloid plaques in Down's syndrome (DS). Here we report that sA beta consists of the full-length A beta(1-42) and peptides truncated and modified by cyclization of the N-terminal glutamates, A beta[3(pE)-42] and A beta[11(pE)-42]. The A beta[3(pE)-42] peptide is the most abundant form of sA beta in Alzheimer's disease (AD) brains. In DS, sA beta[3(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 A beta form a stable aggregate that is water soluble. The findings point to a crucial role of the aggregated and modified sA beta in the plaque formation and pathogenesis of AD.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Russo C,Saido TC,DeBusk LM,Tabaton M,Gambetti P,Teller JK

doi

10.1016/s0014-5793(97)00564-4

subject

Has Abstract

pub_date

1997-06-16 00:00:00

pages

411-6

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(97)00564-4

journal_volume

409

pub_type

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