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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, [35S]methionine and [35S]cysteine incorporation was assessed. Two 35S-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 [3H]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.
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