Regulation of matrix metalloproteinases 2 and 9 in corneal neovascularization
- PMID: 31002472
- DOI: 10.1111/cbdd.13529
Regulation of matrix metalloproteinases 2 and 9 in corneal neovascularization
Abstract
Corneal neovascularization (CNV), a pathological process of angiogenesis, can lead to serious consequences in the cornea. CNV is generally proved to associate with inflammation in the cornea closely, which is mainly elicited by the disruption of equilibrium between angiogenic and antiangiogenic factors. Angiogenic factors including vascular endothelial growth factors (VEGFs), basic fibroblast growth factors (bFGFs), and matrix metalloproteinases (MMPs) are vital factors in the formation of CNV. Especially VEGFs are convinced to be the core angiogenic factors in CNV, and MMPs are proved to exert dual effects on the process. Strikingly, matrix metalloproteinase 2 (MMP-2) and matrix metalloproteinase 9 (MMP-9) are determined to play key roles in the formation of CNV, while the mechanism is still vague. In this review, the latest researches are reviewed to discuss the role of MMP-2 and MMP-9 in CNV, respectively, and some inhibitors of them are presented. We hope to provide a new direction of drug research for CNV.
Keywords: corneal neovascularization; matrix metalloproteinase 2; matrix metalloproteinase 9; vascular endothelial growth factor.
© 2020 John Wiley & Sons A/S.
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References
REFERENCES
-
- Al-Raawi, D., Abu-El-Zahab, H., El-Shinawi, M., & Mohamed, M. M. (2011). Membrane type-1 matrix metalloproteinase (MT1-MMP) correlates with the expression and activation of matrix metalloproteinase-2 (MMP-2) in inflammatory breast cancer. International Journal of Clinical and Experimental Medicine, 4(4), 265-275.
-
- Baker, A. H., Edwards, D. R., & Murphy, G. (2002). Metalloproteinase inhibitors: Biological actions and therapeutic opportunities. Journal of Cell Science, 115(Pt 19), 3719-3727. https://doi.org/10.1242/jcs.00063
-
- Bergers, G., Brekken, R., McMahon, G., Vu, T. H., Itoh, T., Tamaki, K., … Hanahan, D. (2000). Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis. Nature Cell Biology, 2(10), 737-744. https://doi.org/10.1038/35036374
-
- Bode, W., Fernandez-Catalan, C., Grams, F., Gomis-Ruth, F. X., Nagase, H., Tschesche, H., & Maskos, K. (1999). Insights into MMP-TIMP interactions. Annals of the New York Academy of Sciences, 878, 73-91. https://doi.org/10.1111/j.1749-6632.1999.tb07675.x
-
- Brew, K., & Nagase, H. (2010). The tissue inhibitors of metalloproteinases (TIMPs): An ancient family with structural and functional diversity. Biochimica et Biophysica Acta, 1803(1), 55-71. https://doi.org/10.1016/j.bbamcr.2010.01.003
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