Expression of the cochaperone HspBP1 is not coordinately regulated with Hsp70 expression

Eric Gottwald, Mechthild Herschbach, Brigitte Lahni, Roger L. Miesfeld, Susan Kunz, Deborah A. Raynes, Vince Guerriero

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


Intracellular levels of the heat stress protein Hsp70 are elevated following exposure to elevated temperature. The cochaperone HspBP1 is an intracellular protein that is known to bind to and regulate Hsp70 activity. The purpose of this study was to determine if HspBP1 levels changed when Hsp70 levels were altered. Heat stress resulted in an increase in Hsp70 levels but no change in HspBP1 levels. Treatment of cells with the apoptosis inducing drug camptothecin lowered Hsp70 levels but again had no effect on HspBP1 levels. Cells treated with camptothecin plus heat stress did not exhibit an increase in Hsp70 levels. Over-expression in cells stably transfected with HspBP1 cDNA resulted in a 290% increase in HspBP1 levels without a similar change in Hsp70 levels. These results demonstrate that Hsp70 and HspBP1 are not coordinately regulated but provide evidence that an increase in the ratio of HspBP1 to Hsp70 correlates with apoptosis, in a similar way to reducing the amount of Hsp70.

Original languageEnglish (US)
Pages (from-to)553-558
Number of pages6
JournalCell Biology International
Issue number6
StatePublished - Jun 2006


  • Cochaperone
  • Heat stress
  • Hsp70
  • HspBP1

ASJC Scopus subject areas

  • Cell Biology


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