Keratoconus corneas: increased gelatinolytic activity appears after modification of inhibitors

Curr Eye Res. 1993 Jun;12(6):571-81. doi: 10.3109/02713689309001835.


We examined the metalloproteinase activity from normal and keratoconus corneal extracts. No differences were detected in the total amount of the metalloproteinase or its physical form of activation. However, there was a significant elevation in enzymatic activity in the keratoconus extracts after chemical modification of inhibitory elements. This suggests either a difference in the enzymatic capabilities of keratoconus corneas or, as suggested previously, a decrease in the amount of TIMP (tissue inhibitor of metalloproteinase) present in the tissue.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Cells, Cultured
  • Cornea / enzymology*
  • Electrophoresis, Polyacrylamide Gel
  • Glycoproteins / metabolism
  • Humans
  • Immunoenzyme Techniques
  • In Situ Hybridization
  • Keratoconus / enzymology*
  • Matrix Metalloproteinase 2
  • Matrix Metalloproteinase Inhibitors
  • Metalloendopeptidases / genetics
  • Metalloendopeptidases / metabolism*
  • Neoplasm Proteins / metabolism
  • Phenylmercuric Acetate / analogs & derivatives
  • Phenylmercuric Acetate / pharmacology
  • RNA, Messenger / metabolism
  • Tissue Inhibitor of Metalloproteinase-2
  • Tissue Inhibitor of Metalloproteinases


  • Glycoproteins
  • Matrix Metalloproteinase Inhibitors
  • Neoplasm Proteins
  • RNA, Messenger
  • Tissue Inhibitor of Metalloproteinases
  • Tissue Inhibitor of Metalloproteinase-2
  • 4-aminophenylmercuriacetate
  • Metalloendopeptidases
  • Matrix Metalloproteinase 2
  • Phenylmercuric Acetate