Localization of TIMP-1, TIMP-2, TIMP-3, gelatinase A and gelatinase B in pathological human corneas
- 1 January 1998
- journal article
- Published by Informa UK Limited in Current Eye Research
- Vol. 17 (3), 238-246
- https://doi.org/10.1076/ceyr.17.3.238.5222
Abstract
PURPOSE. Determine the tissue distribution patterns for tissue inhibitors of metalloproteinases (TIMP-1, TIMP-2, TIMP-3), gelatinase A and gelatinase B in normal and pathologic corneas. METHOD. Corneas were examined by immunohistochemistry, using antibodies to TIMP-1, TIMP-2, TIMP-3, gelatinase A or gelatinase B. RESULTS. In normal corneas, TIMP-1 antibody stained the epithelium and endothelium. TIMP-2 and TIMP-3 stained the epithelium, keratocytes and endothelium. Gelatinase A staining was weak and restricted to the epithelial cells. Radial keratotomy scars showed increased staining for TIMP-1 and TIMP-2 around the epithelial cell plug and along the incision. Bullous keratopathy corneas showed TIMP staining patterns similar to normal corneas and increased gelatinase A staining in regions of subepithelial fibrosis. Stromal scars of keratoconus corneas also had increased staining with TIMP-1 and TIMP-2 antibodies. In many keratoconus corneas, the TIMP-3 staining pattern was similar to normal corneas. However, in some keratoconus corneas, when Bowman's layer was missing, the stroma beneath was completely devoid of TIMP-3 antibody staining. No gelatinase B was seen in either the normal or diseased corneas. CONCLUSIONS. These data suggest that TIMP-1 and TIMP-2 are important for scar formation and corneal remodeling, since they were found in increased amounts at radial keratotomy incision sites and keratoconus scars. The significance of the focal stromal defects in TIMP-3 staining, associated with absence of Bowman's layer on keratoconus corneas, needs to be elucidated. At the stages of disease examined in this study, gelatinase B may not play a significant role in these pathological processes, since it was not seen in any of the corneas examined.Keywords
This publication has 22 references indexed in Scilit:
- Changes in rat corneal matrix metalloproteinases and serine proteinases under vitamin A deficiencyCurrent Eye Research, 1997
- Suppression of in vivo tumor growth and induction of suspension cell death by tissue inhibitor of metalloproteinases (TIMP)-3Carcinogenesis: Integrative Cancer Research, 1996
- 92‐kDa type IV collagenase and TIMP‐3, but not 72‐kDa type IV collagenase or TIMP‐1 or TIMP‐2, are highly expressed during mouse embryo implantationDevelopmental Dynamics, 1995
- Identification and characterization of human tissue inhibitor of metalloproteinase-3 and detection of three additional metalloproteinase inhibitor activities in extracellular matrixMatrix Biology, 1995
- Increased Gelatinolytic Activity in Keratoconus Keratocyte CulturesCornea, 1994
- Cloning of the cDNA Encoding Human Tissue Inhibitor of Metalloproteinases-3 (TIMP-3) and Mapping of the TIMP3 Gene to Chromosome 22Genomics, 1994
- Tumor invasion, proteolysis, and angiogenesisJournal of Neuro-Oncology, 1994
- Differential roles for two gelatinolytic enzymes of the matrix metalloproteinase family in the remodelling corneaDevelopmental Biology, 1991
- Growth Stimulation of Human Keratinocytes by Tissue Inhibitor of MetalloproteinasesJournal of Investigative Dermatology, 1991
- Human gelatinase/type IV procollagenase is a regular plasma componentFEBS Letters, 1989