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Differential roles for two gelatinolytic enzymes of the matrix metalloproteinase family in the remodelling cornea.
- Source :
-
Developmental biology [Dev Biol] 1991 Oct; Vol. 147 (2), pp. 425-39. - Publication Year :
- 1991
-
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.
- Subjects :
- Animals
Blotting, Western
Chromatography, Affinity
Eye Injuries metabolism
In Vitro Techniques
Matrix Metalloproteinase 2
Matrix Metalloproteinase 3
Metalloendopeptidases biosynthesis
Microbial Collagenase biosynthesis
Rabbits
Cornea enzymology
Extracellular Matrix enzymology
Metalloendopeptidases physiology
Wound Healing physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0012-1606
- Volume :
- 147
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Developmental biology
- Publication Type :
- Academic Journal
- Accession number :
- 1655541
- Full Text :
- https://doi.org/10.1016/0012-1606(91)90300-r