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[Cancer Research 53, 12-15, January 1, 1993]
© 1993 American Association for Cancer Research

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Oxidative Injury Rapidly Activates the Heat Shock Transcription Factor but Fails to Increase Levels of Heat Shock Proteins1

Jacqueline L. Bruce2, Brendan D. Price, C. Norman Coleman and Stuart K. Calderwood

Stress Protein Group, Joint Center for Radiation Therapy, Dana-Farber Cancer Institute, Boston, Massachusetts 02115

When cells are exposed to heat shock, heavy metals, amino acid analogues, and other stresses, the heat shock transcription factor (HSF) is activated. The HSF then binds to the promoter of the heat shock genes, stimulating transcription of the heat shock proteins. Here, we demonstrate that exposure of NIH-3T3 cells to oxidants (H2O2 or menadione) also causes activation of the HSF. This activation is not blocked by inhibitors of protein synthesis (cycloheximide) or by inhibitors of protein kinases (2-aminopurine or genistein). In addition, the oxidant activated HSF is located in the nucleus of the cells. However, oxidant activation of the HSF does not result in the accumulation of hsp70 mRNA or of heat shock proteins. This is in contrast to the accumulation of heat shock proteins seen after heat shock activation of the HSF. This suggests that oxidant induced activation of HSF binding may have a function different from that of heat induced activation of HSF binding.

1 Supported by NIH Grants R29CA-44940 and RO1 47407.

2 To whom requests for reprints should be addressed, at Dana-Farber Cancer Institute, Rm. JF205, 44 Binney St., Boston MA 02115.

Received 10/28/92. Accepted 11/11/92.




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HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cancer Prevention Research
Cancer Prevention Journals Portal Cancer Reviews Online
Annual Meeting Education Book Meeting Abstracts Online
Copyright © 1993 by the American Association for Cancer Research.