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HSPA9 overexpression inhibits apoptin-induced apoptosis in the HepG2 cell line

Chuanmei Peng1, Pu Yang, Yingbo Cui

  • 1Clinical Laboratory of Yanan Hospital of Kunming, and Department of Biochemistry and Molecular Biology, Kunming Medical University, Kunming 650051, PR China.

Oncology Reports
|April 17, 2013
PubMed

Insights

Apoptin protein kills tumor cells by entering the nucleus. Its localization is influenced by HSPA9, a protein that affects cancer cell apoptosis rates, offering new insights into apoptin's anticancer mechanisms.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Apoptin, derived from chicken anemia virus, selectively induces apoptosis in tumor cells.
  • Apoptin's tumor-specific activity is linked to its subcellular localization: cytoplasmic in normal cells and nuclear in cancer cells.

Purpose of the Study:

  • To investigate the proteins interacting with apoptin and their role in its subcellular localization and tumor-selective activity.
  • To elucidate the mechanism by which HSPA9 influences apoptin's localization and apoptotic effects in cancer cells.

Main Methods:

  • Pull-down assays using His-apoptin to identify interacting proteins in HepG2 and L-02 cell lines.
  • Two-dimensional gel electrophoresis and mass spectrometry for protein identification.
  • Investigating the effects of HSPA9 overexpression and downregulation (using siRNA) on apoptin localization and apoptosis rates in HepG2 cells.

Main Results:

  • HSPA9 was identified as an apoptin-interacting protein.
  • HSPA9 overexpression led to partial cytoplasmic distribution of apoptin in HepG2 cells.
  • HSPA9 overexpression decreased HepG2 cell apoptosis, while HSPA9 downregulation significantly increased it.

Conclusions:

  • HSPA9 plays a crucial role in regulating apoptin's subcellular localization and its apoptotic function.
  • The interaction between HSPA9 and apoptin provides new insights into apoptin's anticancer mechanism and potential therapeutic strategies.

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