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. 2019 Apr 17;10:1801. doi: 10.1038/s41467-019-09588-x

Fig. 7.

Fig. 7

MVP inhibits the activity of TRAF6 in cells. a, b Western blot analysis of the effect of MVP on TRAF6 ubiquitination in BMDMs (a) and HEK293T cells (b). c, d Western blot analysis of the effect of MVP on IRAK1–TRAF6 interaction in BMDMs (c) and HEK293T cells (d). e Western blot analysis of the effect of MVP on the oligomerization of TRAF6 in HEK293T cells. f, g Western blot analysis of the effect of full-length and truncated MVPs on the oligomerization (f) and ubiquitination (g) of TRAF6 in HEK293T cells. hk RAW264.7 cells were transfected with lenti-viruses expressing control Flag, Flag-MVP-FL, and Flag-MVP-(686–870). Western blot analysis of Flag-MVP-FL and Flag-MVP-(686–870) expression in RAW264.7 cells (h). Expression of TNF-α and CCL2 in RAW264.7 cells treated by LPS. Expressional levels were measured by RT-qPCR (i) and ELISA (j) (n = 3). Western blot analysis of nuclear extracts prepared from RAW264.7 cells treated by LPS for 1 h (k). l Model illustrating the mechanism of MVP function in macrophages mediated metabolic inflammation in the context of obesity and atherosclerosis. Representative results from three independent experiments are shown. Data are expressed as mean ± SEM. *P < 0.05 and **P < 0.01 by ANOVA with post hoc test