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. 2020 Jan 8;10(1):3. doi: 10.1038/s41408-019-0270-0

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© The Author(s) 2020

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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Fig. 1 — a HL60 and MOLM-13 cell lines were treated with the p38 inhibitors SB203580 (2.5 µM) and PH797804 (250 nM) for 24 h. Protein expression for p-HSP27/HSP27 (p38 substrate) and SET was analyzed by western blot. b Measurement of PP2A activity after p38 inhibition by immunoprecipitation and phosphatase assay. c Silencing of p38α and p38β with specific siRNA (50 nM for 48 h), and analysis of total protein by western blot. d Measurement of PP2A activity by immunoprecipitation and phosphatase assay. e Western blot analysis of total protein in AML cell lines and AML patient samples, compared to peripheral blood mononuclear cells (PB-MC). The results are corrected by the specific loading control and are expressed as fold-change of the control, which are assigned a value of 1 and are mean values. Experiments were performed in triplicate four times. *p < 0.05.