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The corneal stromal collagen and extracellular matrix (ECM) represent the primary structural component of the eye's anterior segment, accounting for approximately 90% of the corneal thickness (Sridhar, 2018). This matrix is composed of highly organized, lamellar arrangements of Type I and Type V collagen fibrils, which are precisely spaced by small leucine-rich proteoglycans (SLRPs) such as lumican, keratocan, and decorin to ensure optical transparency (Meek & Knupp, 2015). In pathological states like keratoconus or corneal ectasia, the biomechanical stability of this matrix is compromised, leading to progressive thinning and visual distortion. The ECM serves as a direct therapeutic target for corneal collagen cross-linking (CXL), where riboflavin and UV-A light induce covalent bond formation to stiffen the tissue and arrest disease progression (Raiskup & Spoerl, 2013). Furthermore, the matrix is a site of action for protease inhibitors that prevent enzymatic degradation during corneal melting and for agents that dissolve metabolic deposits in systemic diseases like cystinosis (Fini & Stramer, 2005).
Photo-oxidative cross-linking of collagen fibrils; Inhibition of matrix metalloproteinases; Chelation of minerals or cystine crystal dissolution
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