Heat shock protein hsp70 accelerates the recovery of heat-shocked mammalian cells through its modulation of heat shock transcription factor HSF1 Journal Article


Authors: Kim, D.; Ouyang, H.; Li, G. C.
Article Title: Heat shock protein hsp70 accelerates the recovery of heat-shocked mammalian cells through its modulation of heat shock transcription factor HSF1
Abstract: The role of mammalian 70-kDa heat shock protein (hsp70) in regulating cellular response to heat shock was examined by using three closely related rat cells: control Rat-1 cells, thermotolerant Rat-1 (TT Rat-1) cells, and heat-resistant M21 cells, a derivative of Rat-1 cells that constitutively overexpress human hsp70. In all these cells, after a prescribed heat shock, the level of the phosphorylated form of heat shock transcription factor HSF1 and that of HSF1 capable of binding to its cognitive DNA sequence heat shock element (HSE) exhibit similar time dependence. The amount of a constitutive HSE-binding activity (CHBA), on the other hand, inversely correlates with those of the two aforementioned forms of HSF1. The recovery kinetics from heat shock are different for the three cell lines, with the thermal- resistant TT Rat-1 and M21 cells showing faster recovery in terms of the state of phosphorylation of HSF1 and its ability to bind HSE or in terms of the reappearance of CHBA. Treatment with okadaic acid, a serine/threonine phosphatase inhibitor, delays the recovery kinetics of Rat-1 cells but not that of thermal-resistant M21 cells. These results are interpreted in terms of a role for hsp70 in the recovery of heat-shocked mammalian cells.
Keywords: dna-binding proteins; sequence deletion; nonhuman; binding affinity; animal cell; animal; mammalia; gene expression; cell line; transcription factor; transfection; phosphorylation; animalia; transcription factors; molecular sequence data; kinetics; saccharomyces cerevisiae; recombinant proteins; fibroblasts; base sequence; gene control; dna sequence; rats; dna binding; heat tolerance; thermoregulation; phosphoprotein phosphatase; mammal cell; modulation; oligodeoxyribonucleotides; gene regulation; ethers, cyclic; heat shock protein; okadaic acid; heat; human; priority journal; article; support, u.s. gov't, p.h.s.; heat-shock proteins 70; heat resistance
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 92
Issue: 6
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 1995-03-14
Start Page: 2126
End Page: 2130
Language: English
DOI: 10.1073/pnas.92.6.2126
PUBMED: 7892235
PROVIDER: scopus
PMCID: PMC42436
DOI/URL:
Notes: Article -- Export Date: 28 August 2018 -- Source: Scopus
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MSK Authors
  1. Dooha Kim
    21 Kim
  2. Gloria C Li
    132 Li
  3. Honghai Ouyang
    16 Ouyang