Matsumoto K, Shams N B, Hanninen L A, Kenyon K R
Schepens Eye Research Institute, Department of Ophthalmology, Harvard Medical School, Boston, MA 02114.
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.
