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Epilysin (MMP‐28) – structure, expression and potential functions
Author(s) -
Illman Sara A.,
Lohi Jouko,
KeskiOja Jorma
Publication year - 2008
Publication title -
experimental dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.108
H-Index - 96
eISSN - 1600-0625
pISSN - 0906-6705
DOI - 10.1111/j.1600-0625.2008.00782.x
Subject(s) - extracellular matrix , matrix metalloproteinase , microbiology and biotechnology , fibronectin , cell adhesion molecule , cell migration , downregulation and upregulation , biology , cell adhesion , epithelial–mesenchymal transition , transforming growth factor beta , cell growth , transforming growth factor , chemistry , cell , biochemistry , gene
Abstract: Epilysin (MMP‐28) is the newest member of the matrix metalloproteinase (MMP) family of extracellular proteases. Together the MMPs can degrade almost all components of the extracellular matrix (ECM). MMPs also regulate cell behaviour by releasing growth factors and biologically active peptides from the ECM by modulating cell surface receptors and adhesion molecules and by regulating the activity of mediators of the inflammatory pathways. Epilysin differs from most other MMPs as it is expressed in a number of normal tissues, suggestive of functions in tissue homeostasis. The epilysin homologue in Xenopus laevis (XMMP‐28) is expressed in neural tissues, where it cleaves the neural cell adhesion molecule. Enhanced expression of epilysin has been observed in basal keratinocytes during wound healing and in different forms of cancer. There are, however, also reports on the downregulation of epilysin in malignant cells. The roles of epilysin in cancer seem to vary based on tumor type and stage of the disease. Importantly, epilysin can induce stable epithelial to mesenchymal transition (EMT) when overexpressed in epithelial lung carcinoma cells. Transforming growth factor β (TGF‐β) is a crucial mediator of this process, which was characterized by the loss of E‐cadherin and increased cell migration and invasion. Current results suggest a plausible interaction between epilysin and TGF‐β also under physiological circumstances, where epilysin activity may not induce EMT but, instead, trigger less permanent changes in TGF‐β signalling and cell motility.