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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 Biology : Journal of the International Society for Matrix Biology
|April 21, 2009
PubMed

Insights

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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