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Updated: Jun 23, 2026

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Published on: March 30, 2022
Expression and function of matrix metalloproteinase (MMP)-28.
Ursula R Rodgers1, Lara Kevorkian, Alison K Surridge
1Biomedical Research Centre, School of Biological Sciences, University of East Anglia, Norwich, UK.
Matrix metalloproteinase-28 (MMP-28) alters cell behavior, increasing adhesion and decreasing migration in chondrosarcoma cells. Its activity is linked to the extracellular matrix and heparan sulfate proteoglycans.
Area of Science:
- Biochemistry
- Cell Biology
- Oncology
Background:
- Matrix metalloproteinase-28 (MMP-28), also known as epilysin, is expressed in various human tissues, including skin, nervous system, cartilage, and synovium.
- MMP-28 expression is elevated in osteoarthritis patients and plays a role in epithelial-to-mesenchymal transition in epithelial cells.
- Previous research indicated MMP-28 activation by proprotein convertases in chondrosarcoma cells.
Purpose of the Study:
- To investigate the functional consequences of MMP-28 over-expression in human chondrosarcoma cells.
- To determine the localization and binding characteristics of active MMP-28.
- To explore the effects of MMP-28 on other matrix metalloproteinases and their inhibitors.
Main Methods:
- Over-expression of wild-type and mutant MMP-28 in human chondrosarcoma cells.
- Analysis of cell morphology, actin organization, and cell adhesion.
- Assessment of cell migration across type II collagen.
- Investigation of MMP-28 localization using cell surface and extracellular matrix association studies.
- Evaluation of the impact of heparin on MMP-28 binding.
- Measurement of MMP-2 and MMP-19 expression and TIMP3 mRNA levels.
Main Results:
- Over-expression of MMP-28 altered chondrosarcoma cell morphology with increased actin organization.
- Adhesion to type II collagen and fibronectin increased, while migration across type II collagen decreased.
- Active MMP-28 associated with the extracellular matrix and cell surface, dependent on heparan sulfate proteoglycans.
- Heparin inhibited both extracellular matrix and cell surface binding of MMP-28.
- Over-expression of activatable MMP-28 increased MMP-2 expression and activity.
- MMP-28 increased MMP-19 and TIMP3 mRNA expression.
Conclusions:
- MMP-28 expression shifts chondrosarcoma cell phenotype towards increased adhesion and reduced migration.
- MMP-28 activity is primarily located in the extracellular matrix, potentially mediated by heparan sulfate proteoglycans.
- MMP-28 influences the expression of other MMPs and TIMPs, suggesting a broader role in matrix remodeling.
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