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. 2022 May 18;13(5):466. doi: 10.1038/s41419-022-04918-2

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© The Author(s) 2022

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 Increased MIF acetylation in cells treated with aspirin. HEK293T cells were transfected with MIF-Flag and treated with aspirin at indicated concentrations. MIF protein was immunoprecipitated with anti-Myc antibody and probed with anti-Ac-K antibody. B Quantification of MIF acetylation showed in (A). Data shown were independent points and mean; one-way ANOVA; n = 3; ***p < 0.001. C Incubation of recombinant GST-MIF protein with aspirin (1 mM), and immunoblot with anti-Ac-K antibody. D Quantification of MIF acetylation showed in (C). Data shown were independent points and mean; paired t-test; n = 3; ***p < 0.001. E Representative K78-acetylated peptides of MIF were analyzed by mass spectrometry. HEK293T cells were transfected with MIF-Flag and treated with aspirin (2 mM). The MIF protein was immunoprecipitated with an anti-Flag antibody and acetylated peptides were analyzed by mass spectrometry. The y ion peaks are shown in blue, and the b ion peaks are shown in red. F Incubation of recombinant GST-MIF protein with aspirin at indicated concentrations, and immunoblot with MIF K78 acetylation antibody. G Quantification of MIF K78 acetylation is shown in (F). Data shown were independent points and mean; paired t-test; n = 3; *p < 0.05. H Decreased MIF K78 acetylation in HDAC6-overexpressing cells. HEK293T cells were transfected with Flag-HDAC6. Acetylated MIF protein was immunoprecipitated with anti-Ac-MIF antibody and probed with anti-MIF antibody. I Quantification of MIF K78 acetylation shown in H. Data shown were independent points and mean; paired t-test; n = 3; **p < 0.01. J Increased MIF K78 acetylation in HDAC6 mutant cortex. Lysates from WT and HDAC6 mutant cortex were immunoprecipitated with anti-Ac-MIF antibody and probed with anti-MIF antibody. K Quantification of MIF K78 acetylation is shown in (J). Data shown were independent points and mean; paired t-test; n = 3; *p < 0.05. L Reduced MIF K78 acetylation in the penumbra regions of the cortex. Lysates of the cortex from the control and ischemia-induced mice were immunoprecipitated with anti-Ac-MIF antibody and probed with anti-MIF antibody. M Quantification of MIF K78 acetylation is shown in (L). Data shown were independent points and mean; paired t-test; n = 3; *p < 0.05.