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MT1-MMP-mediated cleavage of decorin in corneal angiogenesis

Tatsuya Mimura1, Kyu Yeon Han, Tatsuya Onguchi

  • 1Department of Ophthalmology and Visual Sciences, University of Illinois at Chicago, Chicago, IL 60612, USA.

Journal of Vascular Research
|July 3, 2009
PubMed
Abstract

Insights

The enzyme membrane type 1-matrix metalloproteinase (MT1-MMP) promotes blood vessel growth in the cornea by cleaving decorin, an antiangiogenic molecule. This cleavage reduces decorin's ability to inhibit new blood vessel formation.

Area of Science:

  • Ophthalmology
  • Angiogenesis Research
  • Extracellular Matrix Biology

Background:

  • Decorin exhibits antiangiogenic properties.
  • Membrane type 1-matrix metalloproteinase (MT1-MMP) is a proangiogenic enzyme.

Purpose of the Study:

  • To investigate the role of MT1-MMP in decorin cleavage within the cornea.
  • To understand how MT1-MMP affects decorin's antiangiogenic function.

Main Methods:

  • Immunohistochemistry to confirm MT1-MMP expression in corneal cells.
  • Western blotting to assess decorin degradation by MT1-MMP.
  • Aortic ring assays to evaluate the impact of decorin and MT1-MMP on vascularization.

Main Results:

  • MT1-MMP expression increases in the cornea after bFGF implantation.
  • MT1-MMP directly cleaves decorin in vitro, reducing its antiangiogenic effect.
  • MT1-MMP-deficient cells show diminished decorin processing.

Conclusions:

  • MT1-MMP contributes to corneal proangiogenesis by cleaving decorin.
  • This cleavage mechanism may be a key factor in pathological corneal neovascularization.

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