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

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 Aβ40 and Aβ42 aggregation in vitro. Studies performed with CP-Ser [S100A8(C42S)/S100A9(C3S) oligomer] indicate that the protein influences the aggregation profile for Aβ40 in both the absence and presence of metal ions [i.e., Cu(II) and Zn(II)]. Moreover, the detection of Aβ40–CP-Ser complexes by mass spectrometry suggests a direct interaction as a possible mechanism for the involvement of CP in Aβ40 aggregation. Although the interaction of CP-Ser with Aβ40 impacts Aβ40 aggregation in vitro, the protein is not shown to 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.

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Publication details

The article was received on 22 Apr 2018, accepted on 03 Jul 2018 and first published on 03 Jul 2018


Article type: Paper
DOI: 10.1039/C8MT00091C
Citation: Metallomics, 2018, Accepted Manuscript
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    Calprotectin influences the aggregation of metal-free and metal-bound amyloid-β by direct interaction

    H. J. Lee, M. Savelieff, J. Kang, M. Brophy, T. Nakashige, S. J. C. Lee, E. Nolan and M. H. Lim, Metallomics, 2018, Accepted Manuscript , DOI: 10.1039/C8MT00091C

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