Calprotectin influences the aggregation of metal-free and metal-bound amyloid-β by direct interaction
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C8MT00091C.pdf
Description
Accepted version
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3.89 MB
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Checksum (MD5)
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Author(s)
Lee, Hyuck Jin
Savelieff, Masha G.
Kang, Juhye
Brophy, Megan Brunjes
Nakashige, Toshiki George
Lee, Shin Jung C.
Nolan, Elizabeth Marie
Lim, Mi Hee
Date Issued
July 2018
Journal
Metallomics
Publisher
Royal Society of Chemistry (RSC)
Citation
Lee, Hyuck Jin et al. "Calprotectin influences the aggregation of metal-free and metal-bound amyloid-β by direct interaction." Metallomics 10, 8 (July 2018): dx.doi.org/10.1039/c8mt00091c © 2018 The Royal Society of Chemistry.
Version
Author's final manuscript
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-β (Aβ; Aβ 40 and Aβ 42 ) aggregation in vitro. Studies performed with CP-Ser [S100A8(C42S)/S100A9(C3S) oligomer] indicate that the protein influences the aggregation profile for Aβ 40 in both the absence and presence of metal ions [i.e., Zn(ii) and Cu(ii)]. Moreover, the detection of Aβ 40 -CP-Ser complexes by mass spectrometry suggests a direct interaction as a possible mechanism for the involvement of CP in Aβ 40 aggregation. Although the interaction of CP-Ser with Aβ 40 impacts Aβ 40 aggregation in vitro, the protein does not attenuate Aβ-induced toxicity in SH-SY5Y cells. In contrast, S100B has a slight effect on the aggregation of Aβ. Overall, this work supports a potential association of CP with Aβ in the absence and presence of metal ions in AD.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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DOI of Published Version
https://doi.org/10.1039/c8mt00091c
