Radiation sensitivity depends on OGG1 activity status in human leukemia cell lines

Free Radic Biol Med. 2002 Feb 1;32(3):212-20. doi: 10.1016/s0891-5849(01)00793-6.

Abstract

To assess the role of 8-oxoguanine glycosylase (OGG1) in the cell defense against radiation injury, the radiation-induced cytotoxicities were compared between the mutant type KG-1 featuring a loss of OGG1 activity due to a homozygous mutation of Arg 229 Gln, and the wild type U937. While the following three obvious toxicities were displayed in KG-1, they were observed only minimally in U937. These were: a dramatic arrest at the G2/M phase indicated by a marked increase in both the number of G2/M cells and the expression of cyclin B1, cdc2, and mitotic phosphoprotein monoclonal-2 (MPM-2)-reactive proteins; a severe apoptosis shown by a marked increase in the number of cells with hypo-diploid DNA and DNA fragmentation; and as a result, a severe inhibition of cell growth and proliferation measured by the MTT test and [(3)H]-thymidine uptake assay. As expected, KG-1 exhibited a significant increase in the 8-hydroxyguanine level in DNA whereas U937 did not. However, the level of irradiation-induced lipid peroxidation was almost the same in both cell lines. All of these symptoms shown by KG-1 were observed in Molt-4 and CEM-CM3, which were also found to feature low OGG1 activity. These findings suggest that OGG1 plays an important role in cell survival from radiation-induced damage and are also indicative of the capability of 8-hydroxyguanine in DNA to induce cellular toxicities.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apoptosis / radiation effects
  • Blotting, Western
  • CDC2 Protein Kinase / metabolism
  • Cell Cycle / radiation effects
  • Cell Division / radiation effects
  • Cell Line
  • Cell Survival / radiation effects
  • Cyclin B / metabolism
  • Cyclin B1
  • DNA Damage / radiation effects
  • DNA-Formamidopyrimidine Glycosylase
  • Dose-Response Relationship, Radiation
  • Flow Cytometry
  • Gamma Rays
  • Humans
  • Jurkat Cells
  • Leukemia / enzymology*
  • Leukemia / genetics
  • Lipid Peroxidation / radiation effects
  • N-Glycosyl Hydrolases / metabolism*
  • Protein Serine-Threonine Kinases / metabolism
  • Radiation Tolerance*
  • Time Factors
  • Tumor Cells, Cultured

Substances

  • CCNB1 protein, human
  • Cyclin B
  • Cyclin B1
  • Protein Serine-Threonine Kinases
  • CDC2 Protein Kinase
  • N-Glycosyl Hydrolases
  • DNA-Formamidopyrimidine Glycosylase