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. 2018 Apr 30;8:6736. doi: 10.1038/s41598-018-24233-1

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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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HDL impairs activation of TLR2-mediated intracellular signalings. THP1 macrophages were cultured with or without (control) adding HDL (50 µg/ml) for 24 hours. The macrophages were then infected with BCG (multiplicity of infection = 10) for 15 minutes. Immunoblot of p65 phosphorylation (phospho-p65), total p65, p38 phosphorylation (phospho-p38), total p38, ERK phosphorylation (phospho-ERK), total ERK, JNK phosphorylation (phospho-JNK) and total JNK (relative to total β-actin) were detected. Each whole cell lysate was fractionated by SDS-PAGE and transferred on a membrane.Immunoblot experiments were then performed to validate the level of each target protein. The western blot bands of phospho-p65 (65 kDa) total p65 (65 kDa), phospho-p38 (43 kDa), total p38 (43 kDa), phospho-ERK (44 and 42 kDa), total ERK (44 and 42 kDa), phospho-JNK (46 and 54 kDa) and total JNK(46 and 54 kDa) and total beta-actin (43 kDa)are displayed in the figure. Wholemembranes were also displayed in Supplemental Fig. S5. The immunoblots are representative of three independent experiments.