Loss of caspase-3 sensitizes colon cancer cells to genotoxic stress via RIP1-dependent necrosis

Cell Death Dis. 2015 Apr 23;6(4):e1729. doi: 10.1038/cddis.2015.104.

Abstract

Caspase-3 is the best known executioner caspase in apoptosis. We generated caspase-3 knockout (C3KO) and knockdown human colorectal cancer cells, and found that they are unexpectedly sensitized to DNA-damaging agents including 5-fluorouracil (5-FU), etoposide, and camptothecin. C3KO xenograft tumors also displayed enhanced therapeutic response and cell death to 5-FU. C3KO cells showed intact apoptosis and activation of caspase-7 and -9, impaired processing of caspase-8, and induction of necrosis in response to DNA-damaging agents. This form of necrosis is associated with HMGB1 release and ROS production, and suppressed by genetic or pharmacological inhibition of RIP1, MLKL1, or caspase-8, but not inhibitors of pan-caspases or RIP3. 5-FU treatment led to the formation of a z-VAD-resistant pro-caspase-8/RIP1/FADD complex, which was strongly stabilized by caspase-3 KO. These data demonstrate a key role of caspase-3 in caspase-8 processing and suppression of DNA damage-induced necrosis, and provide a potentially novel way to chemosensitize cancer cells.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Caspase 3 / deficiency*
  • Caspase 3 / genetics
  • Caspase 3 / metabolism
  • Cell Death / physiology
  • Colonic Neoplasms / enzymology*
  • Colonic Neoplasms / genetics*
  • DNA Damage
  • HCT116 Cells
  • HEK293 Cells
  • HT29 Cells
  • Humans
  • Nuclear Pore Complex Proteins / genetics
  • Nuclear Pore Complex Proteins / metabolism*
  • RNA-Binding Proteins / genetics
  • RNA-Binding Proteins / metabolism*
  • Transfection

Substances

  • AGFG1 protein, human
  • Nuclear Pore Complex Proteins
  • RNA-Binding Proteins
  • Caspase 3