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. 2019 Dec 6;4:58. doi: 10.1038/s41392-019-0091-4

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© The Author(s) 2019

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 — Sp1 inhibited MKP-1 expression in N2A^APP cells. a The protein level of MKP-1 assessed by western blot in N2A cells after treatment with different concentrations of Aβ. **p < 0.01 and ***p < 0.001 by one-way ANOVA. n = 5 in each group. b The effect of Aβ (10 µm) on the degradation of MKP-1 assessed by half-life measurements in N2A cells treated with 100 μg/ml cycloheximide (CHX). p = 0.352 by two-way ANOVA. n = 5–8 in each group. c The mRNA level of MKP-1 assessed by qPCR in N2A cells after treatment with different concentrations of Aβ. *p < 0.05 and **p < 0.01 by one-way ANOVA. n = 6 in each group. d The promoter activity of MKP-1 assessed by luciferase assay in N2A cells after treatment with different concentrations of Aβ. *p < 0.05, **p < 0.01 and ***p < 0.001 by one-way ANOVA. n = 5 in each group. e–i Functional Sp1-binding sites to the MKP-1 gene promoter. EMSA with MKP-1 Sp1 probe in nuclear extract of HEK 293 cells transfected with Sp1 expression plasmid. Lane 1 is the labeled human consensus Sp1 probe only. Lane 2 shows a shifted DNA–protein complex formed between the labeled Sp1 and nuclear extracts. Competition assays were performed by further adding different competitions of oligonucleotides that included consensus wild-type Sp1 (lane 3), mutant Sp1 (lane 4), putative Sp1-binding site 1 in MKP-1 and mutant Sp1-binding site 1 in MKP-1 (lanes 5 and 6 in a), putative Sp1-binding site 2 in MKP-1 and mutant Sp1-binding site 2 in MKP-1 (lanes 5 and 6 in b), putative Sp1-binding site 3 in MKP-1 and mutant Sp1-binding site 3 in MKP-1 (lanes 5 and 6 in c), putative Sp1-binding site 4 in MKP-1 and mutant Sp1-binding site 4 in MKP-1 (lanes 5 and 6 in d), putative Sp1-binding site 5 in MKP-1 and mutant Sp1-inding site 5 in MKP-1 (lanes 5 and 6 in e). Lane 7 shows the supershifted band with the anti-Sp1 antibody. j, k Effects of different Sp1-binding sites in MKP-1 on the promoter activity of MKP-1 as assessed by luciferase assay. *p < 0.05, **p < 0.01 and ***p < 0.001 by one-way ANOVA. n = 4 in each group. l Effect of different concentrations of Aβ on the expression of Sp1 as assessed by western blot in HEK 293 cells. *p < 0.05 and **p < 0.01 by one-way ANOVA. n = 4 in each group. m, n The protein level of Sp1 assessed by western blot in the hippocampus m and temporal cortex n of control (Ctrl) and AD patients. *p < 0.05 by unpaired Student’s t test. n = 4 to 6 in each group.