Purpose: Decorin is a small chondroitin sulfate proteoglycan that inhibits vascular endothelial cell migration and tube formation. Membrane type 1ĝ€"matrix metalloproteinase (MT1-MMP) has been shown to be an important angiogenic enzyme in the cornea. We evaluated the specific role of MT1-MMP in decorin cleavage in the cornea. Methods: Western blotting was used to evaluate decorin degradation by MT1-MMP. Aortic ring tube formation assays were used to assay the inhibitory effect of decorin and the stimulatory effect of MT1ĝ€"MMP on vascular endothelial cells in vitro. Corneal micropocket assays using basic fibroblast growth factor (bFGF) were used to assess changes in the levels of decorin and MT1-MMP. Results: MT1-MMP cleaves decorin in a time-and concentration-dependent manner in vitro. MT1-MMP levels were upregulated after in vivo bFGF pellet implantation in the cornea, and decorin cleavage products were detected in bFGF-implanted corneas but not in normal corneas. MT1-MMP reduced the inhibitory effects of decorin on aortic ring tube formation in vitro. CONCLUSION:: MT1-MMP may play an essential role in angiogenesis through proteolytic processing of decorin in the cornea.
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