Background: Arsenic metabolism is primarily undergoing in hepatocytes, but the underlying mechanisms are to be defined. It is essential to study the response of aquaporin AQP9, protein kinase p38, and JNK with the sti...Background: Arsenic metabolism is primarily undergoing in hepatocytes, but the underlying mechanisms are to be defined. It is essential to study the response of aquaporin AQP9, protein kinase p38, and JNK with the stimulation of arsenic in mouse models of hepatocellular carcinoma. Methods: Mouse model of hepatocellular carcinoma (HCC) was induced with H22 cells injected subcutaneously on the lateral side of each right axilla in C57BL/6 mice. Then, western blotting and co-immunoprecipitation were used to detect the protein expression and phosphorylation of molecules AQP9, p38 and JNK in mouse models of hepatocellular carcinoma, respectively. The hepatocellular distribution of AQP9 was examined by the immunofluorescent method. Results: In both wild mice and a mouse model of liver tumor, there was no significant difference in the expressions of AQP9, protein kinase p38, and JNK after arsenic treatment, but the phosphorylation expression levels of the three were significantly increased to varying degrees, and the tumor model Compared with the wild-type group, the expression increased. Laser confocal experiments showed that in HepG2 cells, phosphorylated AQP9 was mainly distributed on the cell membrane under the stimulation of arsenic. Conclusion: Arsenic stimulation can increase the phosphorylation of AQP9, p38, and JNK in both wild-type C57 mice and liver tumor mice models. Arsenic stimulation facilitates phosphorylated-AQP9 predominantly distributed on the cell membrane of hepatoma cells HepG2.展开更多
文摘Background: Arsenic metabolism is primarily undergoing in hepatocytes, but the underlying mechanisms are to be defined. It is essential to study the response of aquaporin AQP9, protein kinase p38, and JNK with the stimulation of arsenic in mouse models of hepatocellular carcinoma. Methods: Mouse model of hepatocellular carcinoma (HCC) was induced with H22 cells injected subcutaneously on the lateral side of each right axilla in C57BL/6 mice. Then, western blotting and co-immunoprecipitation were used to detect the protein expression and phosphorylation of molecules AQP9, p38 and JNK in mouse models of hepatocellular carcinoma, respectively. The hepatocellular distribution of AQP9 was examined by the immunofluorescent method. Results: In both wild mice and a mouse model of liver tumor, there was no significant difference in the expressions of AQP9, protein kinase p38, and JNK after arsenic treatment, but the phosphorylation expression levels of the three were significantly increased to varying degrees, and the tumor model Compared with the wild-type group, the expression increased. Laser confocal experiments showed that in HepG2 cells, phosphorylated AQP9 was mainly distributed on the cell membrane under the stimulation of arsenic. Conclusion: Arsenic stimulation can increase the phosphorylation of AQP9, p38, and JNK in both wild-type C57 mice and liver tumor mice models. Arsenic stimulation facilitates phosphorylated-AQP9 predominantly distributed on the cell membrane of hepatoma cells HepG2.
