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Role for the double-stranded RNA activated protein kinase PKR in E2F-1-induced apoptosis

Stephan A Vorburger1, Abujiang Pataer, Kazumi Yoshida

  • 1Department of Surgical Oncology, The University of Texas M.D. Anderson Cancer Center, Houston, Texas, TX 77030, USA.

Oncogene
|September 6, 2002
PubMed

Insights

The transcription factor E2F-1 triggers apoptosis in cancer cells via the protein kinase PKR pathway. This mechanism activates PKR-dependent apoptosis, independent of p53 or p73 tumor suppressors.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Oncology

Background:

  • The transcription factor E2F-1 promotes cell cycle progression and its deregulation can induce apoptosis in malignant cells.
  • Previously identified E2F-1-inducible genes mediating apoptosis include p14(ARF) and p73.

Purpose of the Study:

  • To investigate the role of the double-stranded RNA-dependent protein kinase PKR in E2F-1-induced apoptosis.
  • To elucidate the signaling pathway downstream of E2F-1 that leads to programmed cell death.

Main Methods:

  • Adenovirus-mediated overexpression of E2F-1 in various cancer cell lines.
  • Assessment of PKR and eIF-2alpha phosphorylation levels.
  • Inhibition of PKR activation using chemical inhibitors.
  • Analysis of E2F-1-induced apoptosis in PKR-deficient (PKR-/-) and wild-type (PKR+/+) mouse embryo fibroblasts.

Main Results:

  • Overexpression of E2F-1 induced expression and autophosphorylation of PKR.
  • PKR activation led to phosphorylation of eIF-2alpha and subsequent apoptotic cell death.
  • PKR-dependent apoptosis was observed in cell lines with mutated p53 and p73.
  • Chemical inhibition of PKR significantly reduced E2F-1-induced apoptosis.
  • PKR-/- mouse embryo fibroblasts exhibited resistance to E2F-1-induced apoptosis compared to PKR+/+ cells.

Conclusions:

  • E2F-1-mediated apoptosis can occur through a pathway involving PKR activation.
  • This PKR-dependent apoptotic pathway is independent of functional p53 or p73.
  • PKR represents a critical mediator in E2F-1-induced programmed cell death in cancer cells.

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