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Blocking HSF1 by dominant-negative mutant to sensitize tumor cells to hyperthermia

Jin-Hui Wang1, Ming-Zhong Yao, Jin-Fa Gu

  • 1Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, People's Republic of China.

Insights

Inhibiting heat shock protein 70 (HSP70) via heat shock transcription factor 1 (HSF1) disruption enhances hyperthermia cancer therapy. This approach promotes apoptosis and reduces tumor growth in breast cancer models.

Area of Science:

  • Oncology
  • Molecular Biology
  • Gene Therapy

Background:

  • Heat shock protein 70 (HSP70) is highly expressed in human breast tumors.
  • HSP70 confers resistance to therapies like hyperthermia.
  • Targeting HSP70 may overcome treatment resistance.

Purpose of the Study:

  • To inhibit HSP70 expression by blocking heat shock transcription factor 1 (HSF1) function.
  • To evaluate the efficacy of dominant-negative HSF1 mutant (mHSF1) in sensitizing breast cancer cells to hyperthermia.
  • To assess mHSF1 gene therapy combined with hyperthermia in a preclinical cancer model.

Main Methods:

  • Utilized retrovirus-mediated transfer of mHSF1 into Bcap37 breast cancer cells.
  • Applied hyperthermia treatment to cells and tumor-bearing nude mice.
  • Monitored cell death, apoptosis induction, and tumor growth inhibition.

Main Results:

  • Retroviral transfer of mHSF1 led to significant Bcap37 cell death post-hyperthermia.
  • mHSF1 sensitized Bcap37 cells to hyperthermia by promoting heat-induced apoptosis.
  • mHSF1 gene therapy combined with hyperthermia resulted in diminished tumor growth in vivo.

Conclusions:

  • Disrupting HSF1 function is a viable strategy to sensitize thermotolerant breast cancer cells to hyperthermia.
  • mHSF1 gene therapy in combination with hyperthermia shows promise for treating heat-resistant cancers.
  • This combined approach offers a potential new therapeutic avenue for overcoming resistance to heat treatment in cancer.

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