RRM2 induces NF-kappaB-dependent MMP-9 activation and enhances cellular invasiveness

Mark S Duxbury, Edward E Whang

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

Ribonucleotide reductase is a dimeric enzyme that catalyzes conversion of ribonucleotide 5'-diphosphates to their 2'-deoxynucleotide forms, a rate-limiting step in the production of 2'-deoxyribonucleoside 5'-triphosphates required for DNA synthesis. The ribonucleotide reductase M2 subunit (RRM2) is a determinant of malignant cellular behavior in a range of human cancers. We examined the effect of RRM2 overexpression on pancreatic adenocarcinoma cellular invasiveness and nuclear factor-kappaB (NF-kappaB) transcription factor activity. RRM2 overexpression increases pancreatic adenocarcinoma cellular invasiveness and MMP-9 expression in a NF-kappaB-dependent manner. RNA interference (RNAi)-mediated silencing of RRM2 expression attenuates cellular invasiveness and NF-kappaB activity. NF-kappaB is a key mediator of the invasive phenotypic changes induced by RRM2 overexpression.
Original languageEnglish
Pages (from-to)190-6
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - 2007

Keywords / Materials (for Non-textual outputs)

  • Adenocarcinoma
  • Cell Line, Tumor
  • Cell Proliferation
  • Enzyme Activation
  • Humans
  • Matrix Metalloproteinase 9
  • NF-kappa B
  • Neoplasm Invasiveness
  • Pancreatic Neoplasms
  • Ribonucleoside Diphosphate Reductase


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