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. 2021 Nov 12;9:182. doi: 10.1186/s40478-021-01281-9

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© The Author(s) 2021

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. 2 — Deposits of phosphorylated αSyn at C-terminal tyrosine residues are present in LBD brain. a Immunohistochemical staining using antibodies against pS129-αSyn ab51253, pY125-αSyn, pY133-αSyn, and pY136-αSyn in the frontal cortex from two patients with DN-LBD (case #3) and Li-LBD (case #2). Regions surrounded by white rectangles in the upper panels are magnified and shown in the lower panels. Typical pathological αSyn deposits are indicated by arrowheads. Scale bars, 50 μm. b The number of phosphorylated αSyn deposits > 2 μm² was counted in 12 randomly selected areas of 10 mm² in each tissue specimen using ImageJ. Data are presented as means ± standard deviation. Statistical significance was determined using the 2-tailed Student’s t test. **s < 0.01, ***P < 0.001 vs. Li-LBD