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. 2019 Oct 29;9:15557. doi: 10.1038/s41598-019-51914-2

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© The Author(s) 2019

Open Access This 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Aβ-mediated SHIP2 activation reduces the expression level of ARAP3. (a) Representative images of ARAP3 (green) in HT22 cells incubated without or with 1 μM Aβ in the absence or presence of 10 μM AS09. Cell nuclei were stained with hoechst33342 (blue). (b) The fluorescence intensity of cytosolic ARAP3 was quantified (means ± SEM; t-test; *p < 0.05; n = 78~100 cells per group). (c,d) The expression levels of ARAP3 in SH-SY5Y cells with or without the treatment of 1 μM Aβ for 24 hr. ARAP3 level was quantified by densitometry analysis and normalized to β-actin (means ± SEM; t-test; *p < 0.05; n = 4). (e) The expression level of ARAP3 in HT22 cells treated by various concentrations of PI(3,4)P₂ with or without histone carriers for 24 hr. β-actin was used as a loading control. (f) ARAP3 level was quantified by densitometry analysis and normalized to β-actin (means ± SEM; t-test; *p < 0.05; n = 3).