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

Oncogene volume 21, pages 5765–5772 (2002)Cite this article

Abstract

Metalloproteinases (MMP) 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 A2 and 5-lipoxygenase. These results suggest that the production of soluble EMMPRIN, phospholipase A2 and 5-lipoxygenase activities are sites for potential therapeutic intervention.

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Acknowledgements

This work was supported by Cancer Research UK and The Wellcome Trust, MN Hodgkin was a Beit Memorial Research Fellow.

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  1. Matthew N Hodgkin

    Present address: Department of Biological Sciences, Molecular Physiology Group, University of Warwick, Coventry, CV4 7AL, UK

Authors and Affiliations

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

    Paul M Taylor, Richard J Woodfield, Matthew N Hodgkin, Trevor R Pettitt, Ashley Martin, David J Kerr & Michael JO Wakelam

  2. Department of Clinical Pharmacology, University of Oxford, Radcliffe Infirmary, Woodstock Road, Oxford, OX2 6HE, UK

    David J Kerr

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Correspondence to Michael JO Wakelam.

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Taylor, P., Woodfield, R., Hodgkin, M. et al. Breast cancer cell-derived EMMPRIN stimulates fibroblast MMP2 release through a phospholipase A2 and 5-lipoxygenase catalyzed pathway. Oncogene 21, 5765–5772 (2002). https://doi.org/10.1038/sj.onc.1205702

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