Inhibition of p38 mitogen-activated protein kinase phosphorylation decreases H2O2-induced apoptosis in human lens epithelial cells

Oxidative damage resulting from ROS is a known causal factor for cataractogenesis. The mitogen-activated protein kinases (MAPK) pathway plays an important role in the apoptosis of HLE cells. The purpose of this study was to investigate the role of phosphorylated p38 mitogen-activated protein kinase in H2O2-induced apoptosis in cultured human lens epithelial (HLE) cells. The effect of SB203580 on HLE cells treated with H2O2 was determined by various assays. Cell viability was monitored by the MTT assay. The rates of apoptosis and ROS generation were determined by flow cytometric analysis. The numbers of mitotic and apoptotic cell nuclei were determined after staining with Hoechst 33342. The protein level of phospho-p38 was measured using western blot analysis. SB203580 reduced H2O2-induced cellular apoptosis and inhibited the generation of reactive oxygen species (ROS); it also delayed the progression of H2O2-induced opacification of lenses. The level of p-p38 was increased when cells were exposed to H2O2 and significantly SB203580-inhibited phosphorylation of p38. The p38MAPK pathway plays an important role in H2O2-induced apoptosis of HLE cells. The study demonstrates that activation of p38MAPK plays an important role in H2O2-induced apoptosis of HLE cells. SB203580 may potentially be exploited as a useful tool for cataract prevention.