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PARK, Jiyong
분자활성 촉매반응 연구단
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APP-C31: An Intracellular Promoter of Both Metal-Free and Metal-Bound Amyloid-β40 Aggregation and Toxicity in Alzheimer's Disease

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Title
APP-C31: An Intracellular Promoter of Both Metal-Free and Metal-Bound Amyloid-β40 Aggregation and Toxicity in Alzheimer's Disease
Author(s)
Nam, Eunju; Lin, Yuxi; Jiyong Park; Do, Hyunsu; Han, Jiyeon; Jeong, Bohyeon; Park, Subin; Lee, Da Yong; Kim, Mingeun; Han, Jinju; Mu-Hyun Baik; Lee, Young-Ho; Lim, Mi Hee
Publication Date
2024-01
Journal
Advanced Science, v.11, no.4
Publisher
John Wiley and Sons Inc
Abstract
Intracellular C-terminal cleavage of the amyloid precursor protein (APP) is elevated in the brains of Alzheimer's disease (AD) patients and produces a peptide labeled APP-C31 that is suspected to be involved in the pathology of AD. But details about the role of APP-C31 in the development of the disease are not known. Here, this work reports that APP-C31 directly interacts with the N-terminal and self-recognition regions of amyloid-β40 (Aβ40) to form transient adducts, which facilitates the aggregation of both metal-free and metal-bound Aβ40 peptides and aggravates their toxicity. Specifically, APP-C31 increases the perinuclear and intranuclear generation of large Aβ40 deposits and, consequently, damages the nucleus leading to apoptosis. The Aβ40-induced degeneration of neurites and inflammation are also intensified by APP-C31 in human neurons and murine brains. This study demonstrates a new function of APP-C31 as an intracellular promoter of Aβ40 amyloidogenesis in both metal-free and metal-present environments, and may offer an interesting alternative target for developing treatments for AD that have not been considered thus far. © 2023 The Authors. Advanced Science published by Wiley-VCH GmbH.
URI
https://pr.ibs.re.kr/handle/8788114/14738
DOI
10.1002/advs.202307182
ISSN
2198-3844
Appears in Collections:
Center for Catalytic Hydrocarbon Functionalizations(분자활성 촉매반응 연구단) > 1. Journal Papers (저널논문)
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