Photochemically Induced Crosslinking of Tarsal Collagen as a Treatment for Eyelid Laxity: Assessing Potentiality in Animal Tissue

Ophthalmic Plast Reconstr Surg. 2018 Sep/Oct;34(5):477-482. doi: 10.1097/IOP.0000000000001063.

Abstract

Purpose: An experimental study to demonstrate in animal eyelids that the controlled exposure of excised tarsal plate to ultraviolet-A radiation can induce a rigidification effect due to photochemical crosslinking of the constitutive collagen.

Methods: Excised strips of sheep tarsus were irradiated with ultraviolet-A rays (wavelength 365 nm) at low and high irradiances, in the presence of riboflavin as a photosensitizer, using radiation sources available for corneal collagen crosslinking procedure. The tensile strength and Young's modulus (stiffness) of irradiated and control samples were measured in a mechanical tester and analyzed statistically. Histologic examination of the specimens was carried out to evaluate the effect of radiation on the meibomian glands and collagen organization.

Results: Mechanical evaluation showed that irradiation induced both stiffening and strengthening of the tarsal plate specimens, and this effect was enhanced at the higher levels of irradiance. The changes in mechanical properties can be attributed to a process of photochemically induced crosslinking of tarsal collagen. Histology revealed no changes in the meibomian glands or in the fibrous collagen system of the tarsus.

Conclusions: These findings indicate that irradiation of tarsal collagen leading to tissue stiffening could be a safe procedure for treating lax eyelid conditions in human patients.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Collagen / radiation effects*
  • Cross-Linking Reagents / pharmacology
  • Eyelids / radiation effects*
  • Photosensitizing Agents / pharmacology
  • Riboflavin / pharmacology
  • Sheep
  • Tensile Strength / radiation effects
  • Ultraviolet Rays*

Substances

  • Cross-Linking Reagents
  • Photosensitizing Agents
  • Collagen
  • Riboflavin