December 1991
Volume 32, Issue 13
Articles  |   December 1991
Mechanism of basement membrane dissolution preceding corneal ulceration.
Author Affiliations
  • M Matsubara
    Eye Research Institute, Boston, Massachusetts.
  • J D Zieske
    Eye Research Institute, Boston, Massachusetts.
  • M E Fini
    Eye Research Institute, Boston, Massachusetts.
Investigative Ophthalmology & Visual Science December 1991, Vol.32, 3221-3237. doi:
  • Views
  • PDF
  • Share
  • Tools
    • Alerts
      This feature is available to authenticated users only.
      Sign In or Create an Account ×
    • Get Citation

      M Matsubara, J D Zieske, M E Fini; Mechanism of basement membrane dissolution preceding corneal ulceration.. Invest. Ophthalmol. Vis. Sci. 1991;32(13):3221-3237.

      Download citation file:

      © ARVO (1962-2015); The Authors (2016-present)

  • Supplements
This content is PDF only. Please click on the PDF icon to access.

In animal models for corneal ulceration, the degradation of extracellular matrix components of the stroma does not occur until after the basement membrane underlying the corneal epithelium has disappeared. Using a thermal-burn model, it was demonstrated that epithelial basement membrane is degraded actively by products of corneal cells in a process that does not require the participation of polymorphonuclear leukocytes. A new gelatinolytic metalloproteinase, preliminarily identified as the matrix metalloproteinase, MMP-9, is synthesized and secreted by corneal cells with a timing appropriate for a role in basement membrane degradation. During healing of ulcers, when new matrix is being deposited actively in the burned tissue, a second new gelatinase appears in the cornea, preliminarily identified as a stable activated form of the matrix metalloproteinase, MMP-2. The timing of expression suggests a role for this enzyme in appropriate deposition and remodeling of new matrix in the regenerating corneal tissue.


This PDF is available to Subscribers Only

Sign in or purchase a subscription to access this content. ×

You must be signed into an individual account to use this feature.