ABSTRACT
OBJECTIVE: To elucidate the regulation of p38 and PKC for water channel protein AQP9 and the effect on As intake in lour kinds of mammal cells, and to investigate the regulation mechanism of AOP9 phosphorylation. METHODS: p38, PKC protein and phosphorylation levels were analyzed by Western blotting, and phosphorylation level of AQP9 was detected by immuno-precipitation. Intracellular arsenic content was determined by inductively coupled plasma mass spectrometry (ICP-MS). Experimental data were analysed by SPSS statistical software. RESULTS: p38 protein and phosphorylation levels increased significantly with time in four kinds of cells treated with NaAsO2, while no significant change had been observed in PKC protein and phosphorylation levels. AQP9 phosphorylation level was inhibited in L-02 cells when p38 activity was inhibited, and As accumulation also decreased significantly in L-02 cells. CONCLUSION: AQP9 phosphorylation has effect on As intake and rate. But the regulated mechanism may be different in different cells. p38 kinase attends partly AQP9 phosphorylation in liver normal cells L-02, PKC has no effect on AQP9 phosphorylation in all kinds cells used in this paper.