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Corneal stromal extracellular matrix (ECM) proteins constitute the bulk of the human cornea and are essential for its structural integrity, shape, and optical transparency. This complex network is primarily composed of highly organized Type I, V, and VI collagen fibrils, interspersed with small leucine-rich proteoglycans (SLRPs) such as lumican, keratocan, decorin, and biglycan (PMID: 26335807, 21840310). These proteins regulate the precise spacing and diameter of collagen fibrils, which is a prerequisite for the destructive interference of light scattering that allows for corneal clarity. In pathological conditions like keratoconus or corneal scarring, the organization and composition of these proteins are disrupted, leading to vision loss (PMID: 30639209). Therapeutic strategies targeting the corneal ECM include collagen cross-linking using riboflavin and UV-A light to stabilize the matrix in ectatic diseases, and the use of anti-fibrotic agents like Mitomycin C or TGF-beta inhibitors to modulate the wound healing response and prevent opacity (PMID: 29120434, 31430510).
Photo-oxidative cross-linking of collagen fibers to increase biomechanical stability; inhibition of TGF-beta-mediated myofibroblast transformation to prevent fibrosis; enzymatic degradation of collagen; replacement of deficient proteoglycans.
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