Impaired elimination of DNA double-strand break-containing lymphocytes in ataxia telangiectasia and Nijmegen breakage syndrome

DNA Repair (Amst). 2006 Aug 13;5(8):904-13. doi: 10.1016/j.dnarep.2006.05.002. Epub 2006 Jun 12.

Abstract

The repair of DNA double-strand breaks is critical for genome integrity and tumor suppression. Here we show that following treatment with the DNA-intercalating agent actinomycin D (ActD), normal quiescent T cells accumulate double-strand breaks and die, whereas T cells from ataxia telangiectasia (AT) and Nijmegen breakage syndrome (NBS) patients are resistant to this death pathway despite a comparable amount of DNA damage. We demonstrate that the ActD-induced death pathway in quiescent T lymphocytes follows DNA damage and H2AX phosphorylation, is ATM- and NBS1-dependent and due to p53-mediated cellular apoptosis. In response to genotoxic 2-Gy gamma-irradiation, on the other hand, quiescent T cells from normal donors survive following complete resolution of the damage thus induced. T cells from AT and NBS patients also survive, but retain foci of phosphorylated H2AX due to a subtle double-strand break (DSB) repair defect. A common consequence of these two genetic defects in the DSB response is the apparent tolerance of cells containing DNA breaks. We suggest that this tolerance makes a major contribution to the oncogenic risk of patients with chromosome instability syndromes.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apoptosis / genetics*
  • Ataxia Telangiectasia / genetics*
  • DNA Damage*
  • DNA Primers
  • DNA Repair / genetics*
  • Dactinomycin / toxicity
  • Flow Cytometry
  • Gamma Rays
  • Histones / metabolism
  • Humans
  • Immunoblotting
  • Microscopy, Fluorescence
  • Nijmegen Breakage Syndrome / genetics*
  • Phosphorylation
  • Reverse Transcriptase Polymerase Chain Reaction
  • T-Lymphocytes / cytology
  • T-Lymphocytes / drug effects
  • T-Lymphocytes / radiation effects*

Substances

  • DNA Primers
  • H2AX protein, human
  • Histones
  • Dactinomycin