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Feeding induces expression of heat shock proteins that reduce oxidative stress
Author(s) -
Katsuki Kensaku,
Fujimoto Mitsuaki,
Zhang Xiu-Ying,
Izu Hanae,
Takaki Eiichi,
Tanizawa Yukio,
Inouye Sachiye,
Nakai Akira
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.06.087
Subject(s) - heat shock protein , xenobiotic , hsf1 , heat shock factor , hsp27 , hsp70 , oxidative stress , glutathione , microbiology and biotechnology , heat shock , transcription factor , biology , shock (circulatory) , chemistry , biochemistry , gene , medicine , enzyme
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.