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Oxidants differentially regulate the heat shock response

E S Wallen1, G R Buettner, P L Moseley

  • 1Department of Internal Medicine, University of New Mexico, Albuquerque 87131-5271, USA.

International Journal of Hyperthermia : the Official Journal of European Society for Hyperthermic Oncology, North American Hyperthermia Group
|November 14, 1997
PubMed
Summary
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Cells synthesize heat shock proteins (HSPs) in response to heat. This study investigated if oxidative stress also triggers HSP70 production, finding menadione induced it, but not hydrogen peroxide or xanthine/xanthine oxidase.

Area of Science:

  • Cellular stress response
  • Molecular biology
  • Biochemistry

Background:

  • Hyperthermia induces heat shock proteins (HSPs) in cells, animals, and humans.
  • Hyperthermic stress can cause mitochondrial dysfunction and reactive oxygen species (ROS) generation.
  • The relationship between oxidative stress and HSP synthesis requires further investigation.

Purpose of the Study:

  • To determine if oxidative stress alone is sufficient to increase cellular levels of heat shock protein 70 (HSP70).
  • To compare the effects of different types of oxidant stress on HSP70 expression.

Main Methods:

  • Cellular heat treatment.
  • Treatment of cells with menadione, a source of oxidative stress.
  • Treatment of cells with hydrogen peroxide and xanthine/xanthine oxidase as other sources of oxidative stress.

Related Experiment Videos

  • Detection and quantification of HSP70 levels.
  • Main Results:

    • HSP70 was detected in cells subjected to heat stress.
    • HSP70 was also detected in cells treated with menadione.
    • HSP70 was not detected in cells treated with hydrogen peroxide or xanthine/xanthine oxidase.

    Conclusions:

    • Oxidant stress can induce HSP70 synthesis, but the response is dependent on the specific agent used.
    • The mechanism of oxidative stress induced by menadione may differ qualitatively from that induced by hydrogen peroxide or xanthine/xanthine oxidase.
    • Further research is needed to elucidate the distinct pathways involved in HSP70 regulation under different oxidative stress conditions.