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. 2018 May 24;9(6):621. doi: 10.1038/s41419-018-0691-x

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© The Author(s) 2018

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. 2 — a, b Lapatinib-resistant human BT474R cells (a) and mouse 125R cells (b) are more resistant to proteotoxic stress induced by the proteasome inhibitor MG132 (0.5 μM for 48 h) than their corresponding lapatinib-sensitive control cells. Cell viability assay. One representative experiment out of two independent experiments (each performed in triplicate) is shown; *p < 0.05 for three technical replicas, Student’s t-test. c–e Under proteotoxic stress induced by (c) the proteasome inhibitor MG132 (1 μM for 48 h) and (d) heat shock (43 C, 30 min, Western blot 48 h after) lapatinib-resistant human and murine cells have decreased apoptosis (cleaved PARP) and increased phospho-HSF1 (Ser326 e, f) compared to lapatinib-sensitive cells. Lapatinib-resistant murine 125R cells show upregulated heat shock protein Hsp70 to lapatinib-sensitive cells after proteotoxic stress induced by (g) heat shock (43 C, 30 min, Western blot 2 h after) and proteasome inhibitor MG132 (h). Western blot analysis. GAPDH and Hsc70 as a loading control