Corneal stromal fibrillar collagen and associated extracellular matrix components (Corneal ECM)

The corneal stromal fibrillar collagen and associated extracellular matrix (ECM) components constitute the bulk of the human cornea, providing both structural integrity and the precise organization required for optical transparency. This complex matrix is primarily composed of Type I and Type V collagen fibrils, which are organized into highly ordered lamellae, and specialized small leucine-rich proteoglycans (SLRPs) such as lumican, keratocan, and decorin that regulate fibril spacing (Source: NIH, StatPearls). In diseases like keratoconus, the biomechanical stability of this matrix is compromised, leading to progressive thinning and protrusion of the cornea. Therapeutic interventions often target these components directly, most notably through corneal collagen cross-linking (CXL), where riboflavin acts as a photosensitizer to induce new covalent bonds between collagen fibers, thereby stiffening the tissue (Source: American Academy of Ophthalmology). Additionally, pharmacological agents like Losartan are being investigated to modulate the ECM by inhibiting fibrotic responses following injury or refractive surgery (Source: PubMed).

Other names

Corneal stromaCorneal extracellular matrixCorneal collagen fibrilsCorneal stromal matrix

Photo-oxidative cross-linking (via Riboflavin and UV-A) to increase mechanical stiffness; enzymatic degradation of collagen fibers; inhibition of TGF-beta signaling to reduce myofibroblast differentiation and fibrosis.