Fig. 6: Acetate promotes NLRP3 degradation through autophagy. | Experimental & Molecular Medicine

Fig. 6: Acetate promotes NLRP3 degradation through autophagy.

From: Acetate attenuates inflammasome activation through GPR43-mediated Ca2+-dependent NLRP3 ubiquitination

Fig. 6

a–c ELISA of IL-1β indicated that acetate (25, 30, and 35 mM) mediated suppression of the NLRP3 inflammasome in a manner dependent on autophagy but not the proteasome. Inhibition of autophagy (3-MA and bafilomycin A1) reversed the suppression of IL-1β (a, b), whereas inhibition of the proteasome induced few alterations (c) in BMDMs (n = 3). c, d Western blot of NLRP3, ASC, p62, and LC3B. The degradation of NLRP3 was accompanied by increased NLRP3 expression and decreased p62 expression in BMDMs (n = 3). n = biological replicates. Data are presented as the mean ± SEM. *P < 0.05, **P < 0.01, ***P < 0.001, and ****P < 0.0001, Student’s t-test compared with the control group (a–c) or one-way ANOVA for comparisons of differences (d)

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