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. 2020 Apr 28;10:7139. doi: 10.1038/s41598-020-64004-5

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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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Analysis of PERK, IRE1 and ATF6 pathways and PDI proteins involved in UPR activation. Western blot analysis of (A) phospho-PERK, eIF2-α and ATF6, (B) phospho-IRE1α, total JNK and phospho-JNK (C) PDI, Erp72, Erp57 and calnexin in rat FaO hepatoma cells treated with 500 µM α-LA from 6 up to 48 hours. β-actin was used as loading control. For densitometric analysis specific protein expression was normalized to β-actin expression and values (reported over each band) have been expressed as fold change respect to control. Each lane represents a pool of three individual samples. TG: Thapsigargin. (D) Splicing of XBP-1 in rat FaO hepatoma cells after exposure to 0,5 uM TG from 1 up to 24 hours or 500 μM α-LA from 3 up to 48 hours. The data are representative of three different individual experiments. Images (A–D) have been cropped for clarity with full blot presented in Supplementary Fig. 7.