Feeding induces expression of heat shock proteins that reduce oxidative stress
Feeding induces expression of heat shock proteins that reduce oxidative stress
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DOI：
10.1016/j.febslet.2004.06.087
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发表时间：
2004-07-30
期刊：
影响因子：
3.5
通讯作者：
Nakai, A
中科院分区：
文献类型：
--
作者：
Katsuki, K;Fujimoto, M;Nakai, A
热休克蛋白（Heat shock proteins，Hsps）是机体对各种环境和生理胁迫的应答。然而，目前尚不清楚热休克蛋白是否在保护消化器官细胞免受外源性化学物质的影响中发挥作用。在这里，我们发现，喂养诱导一组热休克蛋白的表达，特别是在小鼠肝脏和肠道通过激活热休克转录因子1（HSF 1）。在肝脏中，需要HSF1来抑制亲电体的毒性作用，亲电体是引起氧化应激的异生化学物质。我们发现，Hsp27的过度表达，提高细胞谷胱甘肽水平，促进暴露于亲电试剂的培养细胞的存活。这些结果表明，一种新的机制，细胞保护对外源性化学物质的食物。(C)2004年由Elsevier B.V.代表欧洲生物化学学会联合会出版。
Heat shock proteins (Hsps) are induced in response to various kinds of environmental and physiological stresses. However, it is unclear whether Hsps play roles in protecting cells in the digestive organs against xenobiotic chemicals. Here, we found that feeding induces expression of a set of Hsps specifically in the mouse liver and intestine by activating heat shock transcription factor 1 (HSF1). In the liver, HSF1 is required to suppress toxic effects of electrophiles, which are xenobiotic chemicals causing oxidative stress. We found that overexpression of Hsp27, which elevates cellular glutathione level, promotes survival of culture cells exposed to electrophiles. These results suggest a novel mechanism of cell protection against xenobiotic chemicals in the food. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.