Abstract:
PURPOSE:Decorin is a small chondroitin sulfate proteoglycan that inhibits vascular endothelial cell migration and tube formation. Membrane type 1-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 MT1-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.
journal_name
Corneajournal_title
Corneaauthors
Mimura T,Chang JH,Kim TI,Onguchi T,Kojima T,Sakimoto T,Azar DTdoi
10.1097/ICO.0b013e31822816e0subject
Has Abstractpub_date
2011-10-01 00:00:00pages
S45-9eissn
0277-3740issn
1536-4798pii
00003226-201110001-00010journal_volume
30 Suppl 1pub_type
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