BCR-ABL down-regulates the DNA repair protein DNA-PKcs

Blood. 2001 Apr 1;97(7):2084-90. doi: 10.1182/blood.v97.7.2084.

Abstract

This study demonstrates in both stable and inducible BCR-ABL-expressing hematopoietic cells a down-regulation of the major mammalian DNA repair protein DNA-PKcs by BCR-ABL. Similar results were found in BCR-ABL CD34(+) cells from patients with chronic myelogenous leukemia (CML). DNA-PKcs down-regulation is a proteasome-dependent degradation that requires tyrosine kinase activity and is associated with a marked DNA repair deficiency along with increased sensitivity to ionizing radiation. The conjunction of a major DNA repair deficiency and a resistance to apoptosis, both induced by BCR-ABL, provides a new mechanism to explain how secondary genetic alterations can accumulate in CML, eventually leading to blast crisis. The down-regulation of DNA-PKcs was reversible in CD34(+) CML cells suggesting that this approach might offer a novel and powerful therapeutic strategy in this disease, especially to delay the blast crisis. (Blood. 2001;97:2084-2090)

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcysteine / analogs & derivatives*
  • Acetylcysteine / pharmacology
  • Animals
  • Apoptosis / genetics
  • Apoptosis / radiation effects
  • Blast Crisis / genetics
  • Child
  • Cysteine Endopeptidases / metabolism
  • DNA Repair / genetics*
  • DNA, Neoplasm / metabolism
  • DNA-Activated Protein Kinase
  • DNA-Binding Proteins*
  • Enzyme Induction
  • Enzyme Inhibitors / pharmacology
  • Fusion Proteins, bcr-abl / physiology*
  • Gene Expression Regulation, Leukemic*
  • Humans
  • In Situ Hybridization, Fluorescence
  • Leukemia, Myelogenous, Chronic, BCR-ABL Positive / enzymology*
  • Leukemia, Myelogenous, Chronic, BCR-ABL Positive / genetics
  • Leukemia, Myelogenous, Chronic, BCR-ABL Positive / pathology
  • Mice
  • Multienzyme Complexes / antagonists & inhibitors
  • Multienzyme Complexes / metabolism
  • Neuroblastoma / pathology
  • Nuclear Proteins
  • Oligopeptides / pharmacology
  • Precursor B-Cell Lymphoblastic Leukemia-Lymphoma / pathology
  • Protease Inhibitors / pharmacology
  • Proteasome Endopeptidase Complex
  • Protein Serine-Threonine Kinases / biosynthesis
  • Protein Serine-Threonine Kinases / genetics*
  • Recombinant Fusion Proteins / physiology
  • Reverse Transcriptase Polymerase Chain Reaction
  • Transfection
  • Tumor Cells, Cultured / enzymology
  • Tumor Stem Cell Assay
  • Tyrphostins / pharmacology

Substances

  • DNA, Neoplasm
  • DNA-Binding Proteins
  • Enzyme Inhibitors
  • Multienzyme Complexes
  • Nuclear Proteins
  • Oligopeptides
  • Protease Inhibitors
  • Recombinant Fusion Proteins
  • Tyrphostins
  • tyrphostin AG957
  • lactacystin
  • Fusion Proteins, bcr-abl
  • DNA-Activated Protein Kinase
  • PRKDC protein, human
  • Protein Serine-Threonine Kinases
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex
  • Acetylcysteine