Lysine acetyltransferase 2A-mediated succinylation of adenosine monophosphate-activated protein kinase suppresses gallstone formation by inhibiting inflammation and pyroptosis

Figure 1 Lysine acetyltransferase 2A-mediated succinylation was involved in the regulation of cholelithiasis. A: Body weight of the normal and the model groups (n = 6); B: Biliary bile cholesterol saturation index; C: Total bile acids content; D: Total cholesterol (TC) content in bile were measured (n = 6); E: Enzyme-linked immunosorbent assay analysis of the concentrations of alanine aminotransferase; F: Aspartate aminotransferase; G: Alkaline phosphatase; H: TC; I: Total triglycerides; J: High density lipoprotein cholesterol; K: Low density lipoprotein cholesterol; L: Tumor necrosis factor-α; M: Interleukin (IL)-1β; N: IL-18 (n = 6); O: Representive image of gallbladder stones of each group mice; P: Histological examination of the gallbladder by hematoxylin and eosin staining; Q: RNA-seq was performed to show differentially expressed genes between the normal and the model groups; R: Succinyltransferase enzymes were present in the differentially expressed genes between the normal and model groups; S: Gene Ontology; T: Kyoto Encyclopedia of Genes and Genomes databases were used to analyze the signaling pathways and metabolic processes enriched by differentially expressed genes; U-W: Western blot was performed to assess the protein levels of succinylation and enzymes associated with succinylation (n = 6). KAT2A: Lysine acetyltransferase 2A; KAT3B: Lysine acetyltransferase 3B; CPT1A: Carnitine palmitoyltransferase 1A; SIRT1: Sirtuin 1.