Cristóvão JS, Morris VK, Cardoso I, Leal SS, Martínez J, Botelho HM, Göbl C, David R, Kierdorf K, Alemi M, Madl T, Fritz G, Reif B, Gomes CM. The neuronal S100B protein is a calcium-tuned suppressor of amyloid-β aggregation. Sci Adv. 2018 Jun;4(6):eaaq1702. Epub 2018 Jun 29 PubMed.

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  1. For the first time, the authors present compelling evidence that S100B is a direct molecular chaperone for Aβ. The upshot is that, at physiological concentrations and with help from Ca2+, a promiscuous S100B motif binds to Aβ monomers and prevents aggregation.

    At face value, this may seem to contrast with prior work from our group showing that S100B transgenic-mutant human APP/PS1 mice have exacerbated AD-like pathology.  However, as is typical with many protein-protein interactions, binding kinetics are exquisitely concentration-dependent—in this case, stabilizing Aβ monomers at physiological S100B levels but promoting Abβ aggregation at supraphysiological abundance.

    View all comments by Terrence Town

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