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First published online September 7, 2006

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Epilysin spurs epithelial transition

An important step in carcinogenesis is the conversion of polarized epithelial cells to migrating mesenchymal cells. Several matrix metalloproteinases (MMPs) - proteases that remodel the extracellular matrix - have been implicated in such epithelial-to-mesenchymal transitions (EMTs). Now, Jouko Lohi and colleagues report that epilysin (MMP28), the newest member of this protein family, induces TGF-ß-dependent EMT in human A549 lung adenocarcinoma cells (see p. 3856). Stable expression of catalytically active epilysin in A549 cells, they report, results in EMT, loss of the cell-cell adhesion molecule E-cadherin from the surface, and proteolytic processing of latent TGF-ß complexes in the extracellular matrix. Although the EMT is irreversible, the authors show that an MMP inhibitor and TGF-ß-neutralizing antibodies prevent its onset. They also reveal that epilysin is attached to the surface of epithelial cells through its hemopexin domain but released after EMT by MT1-MMP, which is upregulated by epilysin. The authors suggest, therefore, that transient epilysin activity helps to regulate the phenotype of epithelial cells and may help to induce cell invasion during carcinogenesis.

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Related articles in JCS:

Epilysin (MMP-28) induces TGF-ß mediated epithelial to mesenchymal transition in lung carcinoma cells

Sara A. Illman, Kaisa Lehti, Jorma Keski-Oja, and Jouko Lohi
JCS 2006 119: 3856-3865. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?