Induction of heat shock protein 70 protects intestinal epithelial IEC-18 cells from oxidant and thermal injury
Induction of heat shock protein 70 protects intestinal epithelial IEC-18 cells from oxidant and thermal injury
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DOI：
10.1152/ajpcell.1996.270.2.c429
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发表时间：
1996-02-01
影响因子：
5.5
通讯作者：
Chang, EB
中科院分区：
文献类型：
--
作者：
Musch, MW;Ciancio, MJ;Chang, EB
利用IEC-18细胞研究了诱导热休克蛋白（HSPs）在肠上皮细胞保护中的潜在重要性。为了建立最佳的热休克蛋白诱导，评估了[S-35]蛋氨酸和[S-35]半胱氨酸的掺入情况。优先合成两个s -35标记的70和90 kDa蛋白。Western和Northern blot分析证实了HSP70的诱导作用。这种诱导对氧化单氯胺或致死热（49℃）处理的细胞提供了显著的保护。为了更好地确定HSP70的保护作用，在lac操作者的控制下，用人HSP70稳定转染细胞。当这些细胞受到损伤时，在非应激条件下，异丙基硫代半乳糖苷刺激的HSP70诱导可以保护这些细胞。此外，蛋白质合成速率（通过[H-3]亮氨酸掺入来评估）也得到了保护。这些结果表明，热休克蛋白在IEC-18细胞中被优先和快速诱导，诱导可诱导的HSP70在促进细胞损伤保护中起重要作用。
The potential importance of inducible heat shock proteins (HSPs) in conferring protection to intestinal epithelial cells was investigated using IEC-18 cells. To establish optimal HSP induction, [S-35]methionine and [S-35]cysteine incorporation was assessed. Two S-35-labeled proteins of 70 and 90 kDa were preferentially synthesized. Western and Northern blot analyses confirmed induction of HSP70. This induction provided significant protection to the cells treated with the oxidant monochloramine or lethal heat (49 degrees C). To better establish the protective role of HSP70, cells were stably transfected with human HSP70 under control of the lac operator. When these cells were subjected to injury, they were protected by isopropylthiogalactoside-stimulated HSP70 induction under nonstress conditions. Additionally the rate of protein synthesis (assessed by [H-3]leucine incorporation) was protected. These results demonstrate that HSPs are preferentially and rapidly induced in IEC-18 cells and that induction of inducible HSP70 is important in promoting protection against cellular injury.