Thermotolerance and cell death are distinct cellular responses to stress: dependence on heat shock proteins

A Samali, C I Holmberg, L Sistonen, S Orrenius

Research output: Contribution to journalArticleScientificpeer-review

115 Citations (Scopus)

Abstract

We tested the hypothesis that heat shock protein (Hsp) induction and cell death are mutually exclusive responses to stress. Despite activation of heat shock transcription factor 1 at temperatures ranging from 40 to 46 degrees C, Hsp72 and Hsp27 were not induced above 42 degrees C. Moreover, cells underwent apoptosis at 44 degrees C and necrosis at 46 degrees C, with mitochondrial cytochrome c release at both temperatures. However, only apoptosis was associated with caspase activation. Treatment of cells with z-VAD-fmk prior to heat shock at 44 degrees C failed to restore Hsp induction despite inhibition of heat-induced apoptosis. Furthermore, accumulation of Hsps after incubation at 42 degrees C rendered the cells resistant to apoptosis. These results suggest that lack of Hsp induction is the cause rather than the consequence of cell death.

Original languageEnglish
Pages (from-to)306–310
Number of pages5
JournalFEBS Letters
Volume461
Issue number3
DOIs
Publication statusPublished - 19 Nov 1999
MoE publication typeA1 Journal article-refereed

Keywords

  • Apoptosis/genetics
  • Caspases/physiology
  • Gene Expression Profiling
  • Gene Expression Regulation
  • Heat-Shock Proteins/physiology
  • Hot Temperature
  • Humans
  • Jurkat Cells
  • Kinetics
  • Mitochondria/physiology
  • Stress, Physiological/genetics

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