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研究检测了γ辐射对IEC 6肠上皮细胞丝裂原激活的蛋白激酶 (MAPKS)的激活效应。 6Gyγ辐射未引起ERK蛋白磷酸化的显著改变 ,而辐照射后 30minJNK与 p38MAPK蛋白磷酸化显著增强 ,ERK、JNK和p38MAPK的总蛋白表达水平未见明显的变化。受照后 12h细胞存活率显著降低。螯合细胞内Ca2 +可几乎完全抑制γ辐照引起的JNK与 p38MAPK的蛋白磷酸化 ,而清除细胞外Ca2 +却无此作用。p38MAPK的激活与γ辐射诱导的细胞凋亡显著相关 ,而ERK则无明显的关联。实验结果表明 ,γ辐射是一种强的JNK与 p38MAPK激活因素 ,并且细胞内储存Ca2 +的释放在γ辐射诱导的IEC 6细胞MAPKs激活与细胞凋亡过程中起重要作用
The study examined the effect of gamma irradiation on the activation of mitogen-activated protein kinases (MAPKS) in IEC 6 intestinal epithelial cells. 6Gyγ radiation did not cause significant changes in phosphorylation of ERK protein, and 30min after irradiation, the phosphorylation of JNK and p38MAPK protein was significantly increased. The expression of total protein of ERK, JNK and p38MAPK showed no significant change. After 12h irradiated cell survival rate was significantly reduced. Chelation of intracellular Ca2 + can almost completely inhibit the phosphorylation of JNK and p38MAPK induced by γ-irradiation, but no effect of removing extracellular Ca2 +. Activation of p38 MAPK was significantly associated with γ-irradiation-induced apoptosis, whereas ERK was not significantly associated. The experimental results show that γ-irradiation is a strong JNK and p38MAPK activator, and the release of intracellular storage Ca2 + plays an important role in the activation of γ-irradiation-induced IEC6 cells and the process of apoptosis