Feeding induces expression of heat shock proteins that reduce oxidative stress

FEBS Lett. 2004 Jul 30;571(1-3):187-91. doi: 10.1016/j.febslet.2004.06.087.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animal Feed*
  • Animals
  • DNA-Binding Proteins / genetics
  • Eating / physiology*
  • Glutathione / metabolism
  • HSP70 Heat-Shock Proteins / genetics*
  • HeLa Cells
  • Heat Shock Transcription Factors
  • Heat-Shock Proteins / genetics*
  • Humans
  • Kinetics
  • Liver / metabolism
  • Mice
  • Mice, Inbred ICR
  • Organ Specificity
  • Oxidative Stress / physiology*
  • Transcription Factors

Substances

  • DNA-Binding Proteins
  • HSF1 protein, human
  • HSP70 Heat-Shock Proteins
  • Heat Shock Transcription Factors
  • Heat-Shock Proteins
  • Transcription Factors
  • Glutathione