Doxorubicin prevents endoplasmic reticulum stress-induced apoptosis

Soo Jung Kim, Kyung Mi Park, Nayoung Kim, Young Il Yeom

Research output: Contribution to journalArticlepeer-review

26 Scopus citations


Several cellular stress signaling pathways initiate apoptosis in eukaryotic cells, but the interactions and coordination between the pathways have not been elucidated. In this study, apoptosis was triggered in MCF7 human breast carcinoma cells using doxorubicin, a topoisomerase inhibitor, and an endoplasmic reticulum (ER) stress inducer, thapsigargin, the latter causing the unfolded protein response (UPR). Interestingly, compared to treatment with doxorubicin or thapsigargin alone, cell death was reduced by treatment with both stress inducers. In contrast to another topoisomerase inhibitor, etoposide, doxorubicin markedly decreased apoptosis induced by thapsigargin; this doxorubicin effect was accompanied by reduced expression of the UPR-specific proapoptotic protein, C/EBP-homologous protein, and its upstream transcription factor, ATF4. We further found that doxorubicin downregulates the expression of ATF4 mRNA, indicating that doxorubicin interferes with the UPR at the level of ATF4 transcription. Taken together, the data suggest that ER stress-initiated cell death might be regulated by doxorubicin.

Original languageEnglish (US)
Pages (from-to)463-468
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Jan 13 2006
Externally publishedYes


  • Apoptosis
  • Doxorubicin
  • Stress signaling
  • Thapsigargin
  • Unfolded protein response

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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