Proteolytic activation of corneal matrix metalloproteinase by Pseudomonas aeruginosa elastase

Curr Eye Res. 1992 Nov;11(11):1105-9. doi: 10.3109/02713689209015082.


Purified Pseudomonas aeruginosa elastase cleaved a 65 kDa gelatinase [inactive proenzyme form of matrix metalloproteinase (MMP-2)] from human corneal fibroblasts into a biologically active fragment with an approximate molecular mass of 58 kDa. However, purified pseudomonal alkaline protease did not cleave MMP-2 appreciably. Since activated MMP-2 is known to degrade native type IV, V and VII collagens, all components of the corneal basement membrane or stroma, our results suggest a new role for pseudomonal elastase in the pathogenesis of corneal infection, inflammation and ulceration.

Publication types

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

MeSH terms

  • Alkaline Phosphatase / pharmacology
  • Bacterial Proteins*
  • Cells, Cultured
  • Cornea / drug effects*
  • Cornea / enzymology*
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Activation
  • Extracellular Matrix / enzymology
  • Fibroblasts / drug effects
  • Humans
  • Matrix Metalloproteinase 2
  • Metalloendopeptidases / metabolism*
  • Metalloendopeptidases / pharmacology*


  • Bacterial Proteins
  • Alkaline Phosphatase
  • Metalloendopeptidases
  • Matrix Metalloproteinase 2
  • pseudolysin, Pseudomonas aeruginosa