Selective cell death of p53-insufficient cancer cells is induced by knockdown of the mRNA export molecule GANP

Apoptosis. 2012 Jul;17(7):679-90. doi: 10.1007/s10495-012-0711-8.

Abstract

Cancer cells often contain p53 abnormalities that impair cell-cycle checkpoint progression and cause resistance to various anti-cancer treatments. DNA damage occurs at actively transcribed genes during G1-phase in yeast cells that have a deficient mRNA export capacity. Here, we show that germinal center-associated nuclear protein (GANP), a homologue of yeast Sac3 that is involved in mRNA export, is indispensable for ensuring the stability of human genomic DNA and that GANP knockdown causes apoptosis and necrosis of p53-insufficient cancer cells. Ganp small interfering RNA (siGanp)-induced DNA damage, accompanied by a decrease in the number of cells in S-phase, caused late apoptosis and necrosis in p53-insufficient cancer cells through both caspase-dependent and -independent mechanisms. siGanp effectively induced DNA damage leading to cell death in p53-insufficient cancer cells in vitro and protect the growth of cancer cells transplanted into immunocompromized mice, suggesting that siGanp has potential as a selective treatment for p53-insufficient cancer cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetyltransferases / genetics
  • Acetyltransferases / metabolism*
  • Animals
  • Caspases / metabolism
  • Cell Death
  • Cell Line, Tumor
  • Cell Proliferation
  • Cholangiocarcinoma / metabolism
  • Cholangiocarcinoma / pathology
  • DNA Damage
  • Gene Knockdown Techniques*
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Mice
  • Microscopy, Electron
  • RNA Transport / genetics*
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • RNA, Small Interfering / metabolism
  • Tumor Suppressor Protein p53 / metabolism*

Substances

  • Intracellular Signaling Peptides and Proteins
  • RNA, Messenger
  • RNA, Small Interfering
  • Tumor Suppressor Protein p53
  • Acetyltransferases
  • MCM3AP protein, human
  • Caspases