HSP70 and genomic stability.

Tej K. Pandita, Ryuji Higashikubo, Clayton R Hunt

Research output: Contribution to journalArticle

18 Scopus citations


The 70 kDa heat shock proteins (HSP70s) were initially identified by their elevated expression following hyperthermic cell stress, however, these highly conserved proteins also protect critical cellular functions from a wider range of important environmental and physiological stresses. At least one result of HSP70 expression is inhibition of stress induced caspase activation as well as downstream events in the apoptotic cell death pathway. HSP70 have been reported upregulated in tumor cells, selective inhibition of such proteins might be valuable approach to treat cancer. A recent study revealed that cells with inactivated HSP70 displayed telomere instability and high frequency of spontaneous chromosomal aberrations, indicating a possible role for HSP70 proteins in the maintenance of genomic stability.

Original languageEnglish (US)
Pages (from-to)591-592
Number of pages2
JournalCell cycle (Georgetown, Tex.)
Issue number5
StatePublished - May 1 2004


  • Heat
  • HSP70
  • Ionizing radiations
  • Stress
  • Telomerase
  • Telomeres

ASJC Scopus subject areas

  • Cell Biology
  • Biochemistry
  • Molecular Biology

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