Fig. 5

Identified STAT3 as a potential target of 4-OI which was suppressed by 4-OI in LPS-induces AKI models. (A) Venn diagram composed of the number of proteins modified by the specific bioorthogonal probe, PharmMapper database retrieved 4-OI targets, SEA database retrieved 4-OI targets and SwissTargetPrediction database retrieved 4-OI targets. (B) Molecular docking of 4-OI with STAT3. The pink structures in the panel represent screened macromolecular receptor structures, while the yellow sticks represent the interacted residuals, and the yellow dotted line represents intermolecular hydrogen bonding. (C) Representative western blot bands of p-STAT3 (Y705), p-STAT3 (S727), and total STAT3 in BUMPT cells. (D) Relative band intensity of p-STAT3 (Y705), p-STAT3 (S727), and total STAT3 in BUMPT cells (n = 4). (E) Real-time polymerase chain reaction analysis of mRNA of Haptoglobin, SAA1, and SAA3 in BUMPT cells (n = 4). (F) Representative western blot bands of p-STAT3 (Y705), p-STAT3 (S727), and total STAT3 in renal tissues (n = 6). (G) Relative band intensity of p-STAT3 (Y705), p-STAT3 (S727), and total STAT3 in renal tissues (n = 6). (H) Representative IHC staining images of p-STAT3 (Y705) and IF staining images of p-STAT3 (S727) (red) in renal tissues. Scale bar: 50 μm. Each symbol (circle) represents an independent experiment. Data are presented as means ± SDs. *P < 0.05, **P < 0.01, ***P < 0.001; ns, not significant. SEA, Similarity ensemble approach