Cerebral vascular amyloid seeds drive amyloid β-protein fibril assembly with a distinct anti-parallel structure

Feng Xu, Ziao Fu, Sharmila Dass, AnnMarie E. Kotarba, Judianne Davis, Steven O. Smith and William E. Van Nostrand ()
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Feng Xu: Stony Brook University
Ziao Fu: Stony Brook University
Sharmila Dass: Stony Brook University
AnnMarie E. Kotarba: Stony Brook University
Judianne Davis: Stony Brook University
Steven O. Smith: Stony Brook University
William E. Van Nostrand: Stony Brook University

Nature Communications, 2016, vol. 7, issue 1, 1-10

Abstract: Abstract Cerebrovascular accumulation of amyloid β-protein (Aβ), a condition known as cerebral amyloid angiopathy (CAA), is a common pathological feature of patients with Alzheimer’s disease. Familial Aβ mutations, such as Dutch-E22Q and Iowa-D23N, can cause severe cerebrovascular accumulation of amyloid that serves as a potent driver of vascular cognitive impairment and dementia. The distinctive features of vascular amyloid that underlie its unique pathological properties remain unknown. Here, we use transgenic mouse models producing CAA mutants (Tg-SwDI) or overproducing human wild-type Aβ (Tg2576) to demonstrate that CAA-mutant vascular amyloid influences wild-type Aβ deposition in brain. We also show isolated microvascular amyloid seeds from Tg-SwDI mice drive assembly of human wild-type Aβ into distinct anti-parallel β-sheet fibrils. These findings indicate that cerebrovascular amyloid can serve as an effective scaffold to promote rapid assembly and strong deposition of Aβ into a unique structure that likely contributes to its distinctive pathology.

Date: 2016
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DOI: 10.1038/ncomms13527

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