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Issue 8, 2018
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Calprotectin influences the aggregation of metal-free and metal-bound amyloid-β by direct interaction

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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; 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., Zn(II) and Cu(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 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.

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

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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, 2018,10, 1116-1127
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    Calprotectin influences the aggregation of metal-free and metal-bound amyloid-β by direct interaction

    H. J. Lee, M. G. Savelieff, J. Kang, M. B. Brophy, T. G. Nakashige, S. J. C. Lee, E. M. Nolan and M. H. Lim, Metallomics, 2018, 10, 1116
    DOI: 10.1039/C8MT00091C

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