Abstract | PURPOSE: MATERIALS AND METHODS: Seventy-one AH samples were collected during cataract extraction and trabeculectomy. The expression and molecular forms of MMP-2, -8, -9, -13, and -14 and tissue inhibitor of metalloproteinases-1 and -2 (TIMPs) were analyzed by Western immunoblotting. Gelatinase and collagenase activities were studied by zymography and type I collagen degradation assays, respectively. MMP-2 and TIMP-2 concentrations were measured by ELISA assays. RESULTS: By Western immunoblotting all the studied MMPs were mainly in their latent form in all diagnostic groups. Zymography demonstrated that MMP-2 represents the major gelatinase in AH. Similarly, type I collagenolytic activity was low and similar in cataract and glaucoma samples. In ELISA measurements the TIMP-2 levels were significantly elevated in glaucoma and EXS samples in comparison to cataract controls (P < 0.05). CONCLUSION:
TIMP-2 is elevated in glaucomatous process over MMP-2, which support and further extend the conjuncture that the ECM accumulation rather than degradation predominates in the pathogenesis of POAG and EXG.
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Authors | Marko Määttä, Taina Tervahartiala, Mika Harju, Juhani Airaksinen, Helena Autio-Harmainen, Timo Sorsa |
Journal | Journal of glaucoma
(J Glaucoma)
Vol. 14
Issue 1
Pg. 64-9
(Feb 2005)
ISSN: 1057-0829 [Print] United States |
PMID | 15650607
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Tissue Inhibitor of Metalloproteinases
- Matrix Metalloproteinases
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Topics |
- Aged
- Aged, 80 and over
- Aqueous Humor
(enzymology)
- Blotting, Western
- Enzyme-Linked Immunosorbent Assay
- Exfoliation Syndrome
(enzymology)
- Extracellular Matrix
(metabolism)
- Female
- Glaucoma, Open-Angle
(enzymology)
- Humans
- Intraocular Pressure
- Male
- Matrix Metalloproteinases
(metabolism)
- Middle Aged
- Tissue Inhibitor of Metalloproteinases
(metabolism)
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