In the present study, we found that MLKL and its phosphorylated protein p-MLKL were upregulated in the pancreas of a cerulein-induced mouse AP model and cerulein-treated pancreatic acinar cells, independent of its canonical upstream molecule Ripk3. CaMKII may be a novel upstream molecule of Mlkl in this setting. Here, RIPK3 is linked to alkaline phosphatase measurement.