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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 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 publication

DOI

10.1038/sj.onc.1205702

Type

Journal article

Journal

Oncogene

Publication Date

22/08/2002

Volume

21

Pages

5765 - 5772

Keywords

Antigens, CD, Antigens, Neoplasm, Arachidonate 5-Lipoxygenase, Basigin, Breast Neoplasms, Catalysis, Female, Fibroblasts, Humans, Matrix Metalloproteinase 2, Membrane Glycoproteins, Phospholipases A, Tumor Cells, Cultured