Journal: Journal of Experimental & Clinical Cancer Research : CR
Article Title: Lactate-driven lactylation of HNRNPA1 orchestrates PKM2 splicing and glycolytic reprogramming in bladder cancer
doi: 10.1186/s13046-025-03591-5
Figure Lengend Snippet: Polydatin inhibits HNRNPA1 lactylation and its biological activity in bladder cancer. A Binding free energy of ten candidate compounds docked to the HNRNPA1 active pocket. B Chemical structure of polydatin. C Docking visualization of polydatin within the active pocket of HNRNPA1. D IC 50 values of polydatin in the EJ-1 cell line, as determined by CCK8 assay. E EJ-1 cells were lysed and immunoprecipitated using an anti-HNRNPA1 antibody, followed by detection of HNRNPA1-K350 lactyl lysine. F Colony formation assays were performed to assess the proliferative capacity of EJ-1 cells following 24-h treatment with 30 μM polydatin or 20 mM NaLa. G-H Tumor gross images and tumor weights were assessed in nude mice after subcutaneous injection of EJ-1 cells. Tumors were harvested on Day 19 after subcutaneous implantation. Statistical analyses were performed with unpaired two-tailed Student’s t-test ( n = 5). I Tumor volume measurements throughout the experiment. J Immunohistochemical staining visualized PKM2 levels in xenograft tumors. Scale bars: 100 μm (left panel), 50 μm (right panel). K Schematic representation of the proposed mechanism of HNRNPA1 lactylation. * p < 0.05, ** p < 0.01
Article Snippet: Cells were treated with polydatin (27208–80-6, TargetMol, USA) for 24 h to examine cell proliferation.
Techniques: Activity Assay, Binding Assay, CCK-8 Assay, Immunoprecipitation, Injection, Two Tailed Test, Immunohistochemical staining, Staining
