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. 2021 Oct 7;59(1):17–34. doi: 10.1007/s12035-021-02566-9

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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/.

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Fig. 3 — Relative expression of APP and various proteoforms of Aβ in brain samples. The expression of (a) APP, (b) Aβ_Total, (c) C-terminally truncated proteoforms, (d) N-terminally truncated proteoforms, and (f) Aβ₄₀ in controls, sAD and rpAD cases quantified using IB and ELISA analysis (n = 4–6). (e) Comparison of various truncations within the tris-soluble fraction is also presented. (g) The average spectrum counts obtained for common proteoforms, other than Aβ_11-42, by MALDI-MS also reflected results similar to ELISA analysis. All blots were subjected to total protein normalization and data from three independent experiments was used for densitometric analysis while the ELISA averages were obtained by analyzing all samples as duplicates. Error bars represent SEM. One-way ANOVA, followed by Tukey’s multiple comparisons test, was used for statistical analysis. (*p ≤ 0.05; **p ≤ 0.01; ***p ≤ 0.001)