Breast cancer cell-derived EMMPRIN stimulates fibroblast MMP2 release through a phospholipase A(2) and 5-lipoxygenase

Related Experiment Video

Updated: Aug 17, 2026

Analyzing the Communication Between Monocytes and Primary Breast Cancer Cells in an Extracellular Matrix Extract (ECME)-based Three-dimensional System
10:55

Analyzing the Communication Between Monocytes and Primary Breast Cancer Cells in an Extracellular Matrix Extract (ECME)-based Three-dimensional System

Published on: January 8, 2018

Paul M Taylor1, Richard J Woodfield, Matthew N Hodgkin

  • 1Cancer Research UK Institute for Cancer Studies, Birmingham University, Birmingham, B15 2TT, UK.

Oncogene
|August 13, 2002
PubMed

Insights

Breast cancer cells release soluble EMMPRIN, promoting pro-MMP2 release from fibroblasts via phospholipase A(2) and 5-lipoxygenase activation. This pathway offers potential therapeutic targets for inhibiting tumor metastasis.

Area of Science:

  • Oncology
  • Cell Biology
  • Biochemistry

Background:

  • Matrix metalloproteinases (MMPs) are crucial for tumor metastasis.
  • Regulation of MMP release from cancer and stromal cells is not well understood.

Purpose of the Study:

  • To investigate the role of breast cancer cells in promoting MMP release from fibroblasts.
  • To identify the molecular mechanisms involved in MMP regulation.

Main Methods:

  • In vitro culture of breast cancer cells and fibroblasts.
  • Analysis of soluble EMMPRIN release.
  • Assay of pro-MMP2 release and activation.
  • Enzyme activity assays for phospholipase A(2) and 5-lipoxygenase.

Main Results:

  • Breast cancer cells release soluble EMMPRIN.
  • Soluble EMMPRIN stimulates fibroblasts to release pro-MMP2.
  • MMP2 generation is dependent on phospholipase A(2) and 5-lipoxygenase activation.

Conclusions:

  • Soluble EMMPRIN produced by breast cancer cells promotes pro-MMP2 release from fibroblasts.
  • The phospholipase A(2) and 5-lipoxygenase pathways are key mediators of this process.
  • Targeting soluble EMMPRIN, phospholipase A(2), or 5-lipoxygenase may offer therapeutic strategies against cancer metastasis.

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