Nitric oxide-induced cellular stress and p53 activation in chronic inflammation

Proc Natl Acad Sci U S A. 2003 Jan 7;100(1):143-8. doi: 10.1073/pnas.0237083100. Epub 2002 Dec 23.

Abstract

Free radical-induced cellular stress contributes to cancer during chronic inflammation. Here, we investigated mechanisms of p53 activation by the free radical, NO. NO from donor drugs induced both ataxia-telangiectasia mutated (ATM)- and ataxia-telangiectasia mutated and Rad3-related-dependent p53 posttranslational modifications, leading to an increase in p53 transcriptional targets and a G(2)M cell cycle checkpoint. Such modifications were also identified in cells cocultured with NO-releasing macrophages. In noncancerous colon tissues from patients with ulcerative colitis (a cancer-prone chronic inflammatory disease), inducible NO synthase protein levels were positively correlated with p53 serine 15 phosphorylation levels. Immunostaining of HDM-2 and p21(WAF1) was consistent with transcriptionally active p53. Our study highlights a pivotal role of NO in the induction of cellular stress and the activation of a p53 response pathway during chronic inflammation.

MeSH terms

  • Animals
  • Ataxia Telangiectasia / genetics
  • Ataxia Telangiectasia Mutated Proteins
  • Breast Neoplasms
  • Cell Cycle
  • Cell Cycle Proteins
  • Cell Line
  • Coculture Techniques
  • Colitis, Ulcerative / pathology
  • Colitis, Ulcerative / physiopathology*
  • Comet Assay
  • Cyclin-Dependent Kinase Inhibitor p21
  • Cyclins / metabolism
  • DNA Damage*
  • DNA-Binding Proteins
  • Female
  • Free Radicals / metabolism
  • Humans
  • Inflammation / genetics
  • Inflammation / physiopathology*
  • Interferon-gamma / pharmacology
  • Lipopolysaccharides / pharmacology
  • Macrophages / drug effects
  • Macrophages / physiology
  • Mice
  • Nitric Oxide / physiology*
  • Nitric Oxide Synthase / metabolism
  • Nitric Oxide Synthase Type II
  • Phosphorylation
  • Phosphoserine / metabolism
  • Protein Processing, Post-Translational
  • Protein Serine-Threonine Kinases / metabolism
  • Transcription, Genetic
  • Tumor Cells, Cultured
  • Tumor Suppressor Protein p53 / genetics
  • Tumor Suppressor Protein p53 / metabolism*
  • Tumor Suppressor Proteins

Substances

  • CDKN1A protein, human
  • Cdkn1a protein, mouse
  • Cell Cycle Proteins
  • Cyclin-Dependent Kinase Inhibitor p21
  • Cyclins
  • DNA-Binding Proteins
  • Free Radicals
  • Lipopolysaccharides
  • Tumor Suppressor Protein p53
  • Tumor Suppressor Proteins
  • Phosphoserine
  • Nitric Oxide
  • Interferon-gamma
  • NOS2 protein, human
  • Nitric Oxide Synthase
  • Nitric Oxide Synthase Type II
  • Nos2 protein, mouse
  • ATM protein, human
  • Ataxia Telangiectasia Mutated Proteins
  • Atm protein, mouse
  • Protein Serine-Threonine Kinases