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. 2020 Jun 19;8:86. doi: 10.1186/s40478-020-00969-8

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© The Author(s) 2020

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 6 — Immunohistochemistry for GSK-3β in the amygdala of rTg4510 and control mice. The cytoplasmic uniform distribution of GSK-3β was found in both mice (a, c). GSK-3β-positive grains were found in rTg4510 mice (c). P-GSK-3β (Tyr216)-positive cells were found in rTg4510 mice (d), but not in control mice (b). Double-labeling immunofluorescence in the hippocampus of rTg4510 mice revealed that p-GSK-3β (Tyr216)-positive grains were localized in hp-tau-positive cells (e). The majority of p-GSK-3β (Tyr216) grains did not co-localize with hp-tau aggregates (e). P-αSyn-positive aggregates localized in p-GSK-3β (Tyr216)-positive cells (f). p-αSyn-positive aggregates co-localized with p-GSK-3β (Tyr216)-positive grains (f). The reactions to hp-tau (e) and p-αSyn (f) are shown in red, and those to p-GSK-3β (Tyr216) (e, f) in green. Scale bars: 20 μm (a-d); 50 μm (e, f)