Corneal stromal collagen and extracellular matrix components

The corneal stromal collagen and extracellular matrix (ECM) components constitute the primary structural framework of the eye's anterior segment, accounting for approximately 90% of corneal thickness. This complex is predominantly composed of highly organized Type I and Type V collagen fibrils, which are precisely spaced by small leucine-rich proteoglycans (SLRPs) such as lumican, keratocan, and decorin to maintain optical transparency [1][2]. The unique lamellar arrangement of these fibers provides the mechanical strength necessary to withstand intraocular pressure while allowing for the refraction of light. In pathological conditions like keratoconus or corneal ectasia, the biochemical and biomechanical stability of this matrix is degraded, resulting in progressive thinning and visual impairment [3]. Therapeutic interventions often target these components to stabilize or remodel the tissue; for instance, corneal collagen cross-linking (CXL) utilizes riboflavin as a photosensitizer to induce covalent bonds between collagen fibers, thereby increasing biomechanical rigidity [4]. Additionally, the ECM serves as a dynamic reservoir for growth factors that regulate the wound-healing response and the behavior of resident keratocytes [5]. Understanding the molecular architecture and turnover of the corneal stroma is vital for advancing treatments for corneal scarring and degenerative disorders.

Other names

Corneal stromaCorneal ECMCorneal collagen matrixCorneal extracellular matrix

Riboflavin acts as a photosensitizer that, when activated by UV-A light, generates reactive oxygen species to induce covalent cross-links between collagen fibrils. Collagenase catalyzes the hydrolysis of peptide bonds in collagen. Mitomycin C inhibits the proliferation of myofibroblasts, thereby reducing disordered ECM deposition.