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Calprotectin influences the aggregation of metal-free and metal-bound amyloid- beta by direct interaction

Author(s)
Lee, Hyuck JinSavelieff, Masha G.Kang, JuhyeBrophy, Megan BrunjesNakashige, Toshiki G.Lee, Shin Jung C.Nolan, Elizabeth M.Lim, Mi Hee
Issued Date
2018-08
DOI
10.1039/c8mt00091c
URI
https://scholarworks.unist.ac.kr/handle/201301/24920
Fulltext
http://pubs.rsc.org/en/Content/ArticleLanding/2018/MT/C8MT00091C#!divAbstract
Citation
METALLOMICS, v.10, no.8, pp.1116 - 1127
Abstract
Proteins from the S100 family perform numerous functions and may contribute to Alzheimer's disease (AD). Herein, we report the effects of S100A8/S100A9 heterooligomer calprotectin (CP) and the S100B homodimer on metal-free and metal-bound amyloid- (A; A(40) and A(42)) aggregation in vitro. Studies performed with CP-Ser [S100A8(C42S)/S100A9(C3S) oligomer] indicate that the protein influences the aggregation profile for A(40) in both the absence and presence of metal ions [i.e., Zn(ii) and Cu(ii)]. Moreover, the detection of A(40)-CP-Ser complexes by mass spectrometry suggests a direct interaction as a possible mechanism for the involvement of CP in A(40) aggregation. Although the interaction of CP-Ser with A(40) impacts A(40) aggregation in vitro, the protein does not attenuate A-induced toxicity in SH-SY5Y cells. In contrast, S100B has a slight effect on the aggregation of A. Overall, this work supports a potential association of CP with A in the absence and presence of metal ions in AD.
Publisher
ROYAL SOC CHEMISTRY
ISSN
1756-5901
Keyword
HUMAN SERUM-ALBUMINALZHEIMERS-DISEASEA-BETAS100 PROTEINSINFLAMMATORY S100A9FIBRIL FORMATIONZINC-BINDINGMOUSE MODELIN-VITROPEPTIDE

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