Breast cancer cell-derived EMMPRIN stimulates fibroblast MMP2 release through a phospholipase A2 and 5-lipoxygenase catalysed pathway

Paul Taylor, Richard Woodfield, Matthew Hodgkin, Trevor Pettitt, Ashley Martin, David Kerr, Michael Wakelam

Research output: Contribution to journalArticle

127 Citations (Scopus)

Abstract

Metalloproteinases (NIMP) produced by both cancer and normal stromal fibroblast cells play a critical role in the metastatic spread of tumours, however little is known of the regulation of their release. In this report we demonstrate that breast cancer cells in culture release apparently full length soluble EMMPRIN that promotes the release of pro-MMP2 from fibroblasts. The generation of MMP2 is mediated by activation of phospholipase A(2) and 5-lipoxygenase. These results suggest that the production of soluble EMMPRIN, phospholipase A(2) and 5-lipoxygenase activities are sites for potential therapeutic intervention.
Original languageEnglish
Pages (from-to)5765-5772
Number of pages8
JournalOncogene
Volume21
Issue number37
DOIs
Publication statusPublished - 22 Aug 2002

Keywords

  • breast cancer cell
  • EMMPRIN
  • 5-lipoxygenase
  • fibroblast
  • MMP2
  • phospholipase A(2)

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