Western blotting analysis was performed by proteins extracted from brain tissues (n = 3 rats per group). Briefly, the hippocampus tissues were crushed and frozen at −80°C in a mortar. Radioimmunoprecipitation assay, phenylmethylsulfonyl fluoride, and a small amount of liquid nitrogen were added and ground into a uniform liquid state. The sample was transferred to an Eppendorf tube, incubated on ice for 15 min, and centrifuged by a cold centrifuge. Then, the target protein was separated and stored in the refrigerator at −80°C.49 (link) According to the protein concentration result, 5 × loading buffer was added to the total protein sample, denatured at 95°C for 10 min and stored on ice. During electrophoresis, the protein sample was added to the well, the power was turned on, the voltage adjusted to 80v for approximately 25 min, then increased to 120 v. After gel electrophoresis, the protein bands separated on the gel were transferred to Polyvinylidene fluoride (PVDF) membrane, and poly cloned with anti-Caspase1 (ABclonal, Wuhan, China; Catalogue: A0964, diluted at 1:200). The PVDF membrane was incubated with a horseradish peroxidase-labeled secondary antibody. Finally, the bands were visualized by enhanced chemiluminescence. Image J software was used to analyze the intensity of the bands.