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

doi:10.1038/sj.onc.1205702

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 journal › Article

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 language	English
Pages (from-to)	5765-5772
Number of pages	8
Journal	Oncogene
Volume	21
Issue number	37
DOIs	https://doi.org/10.1038/sj.onc.1205702
Publication status	Published - 22 Aug 2002

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

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

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10.1038/sj.onc.1205702

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

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.",

keywords = "breast cancer cell, EMMPRIN, 5-lipoxygenase, fibroblast, MMP2, phospholipase A(2)",

author = "Paul Taylor and Richard Woodfield and Matthew Hodgkin and Trevor Pettitt and Ashley Martin and David Kerr and Michael Wakelam",

year = "2002",

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journal = "Oncogene",

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T1 - Breast cancer cell-derived EMMPRIN stimulates fibroblast MMP2 release through a phospholipase A2 and 5-lipoxygenase catalysed pathway

AU - Taylor, Paul

AU - Woodfield, Richard

AU - Hodgkin, Matthew

AU - Pettitt, Trevor

AU - Martin, Ashley

AU - Kerr, David

AU - Wakelam, Michael

PY - 2002/8/22

Y1 - 2002/8/22

N2 - 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.

AB - 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.

KW - breast cancer cell

KW - EMMPRIN

KW - 5-lipoxygenase

KW - fibroblast

KW - MMP2

KW - phospholipase A(2)

UR - https://www.scopus.com/pages/publications/0037158892

U2 - 10.1038/sj.onc.1205702

DO - 10.1038/sj.onc.1205702

M3 - Article

VL - 21

SP - 5765

EP - 5772

JO - Oncogene

JF - Oncogene

IS - 37

ER -

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

Abstract

UN SDGs

Keywords

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