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Abstract
We have documented changes in collagenolytic/gelatinolytic enzymes of the matrix metalloproteinase
family (MMP) in remodelling rabbit cornea. MMP-2 (65 kDa gelatinase) in the proenzyme
form is synthesized by the cells of the normal corneal stroma. After keratectomy the
level of MMP-2 is increased in the stroma and enzyme appears in both pro- and activated
forms. In addition, corneal cells synthesize MMP-9 (92 kDa gelatinase) in the proenzyme
form after keratectomy; expression occurs in both the epithelial as well as stromal
corneal layers. Changes in expression of both enzymes are precisely localized to the
repairing portion of cornea, but demonstrate important differences in timing that
correlate with the timing of specific events of matrix remodelling. Our data suggest
that each of the gelatinases plays a different role in tissue remodelling after injury.
We hypothesize that MMP-2 performs a surveillance function in normal cornea, catalyzing
degradation of collagen molecules that occasionally become damaged. After wounding,
this enzyme appears to participate in the prolonged process of collagen remodelling
in the corneal stroma that eventually results in functional regeneration of the tissue.
MMP-9 expression does not correlate with stromal remodelling, but we suggest that
the enzyme might play a part in controlling resynthesis of the epithelial basement
membrane.