Proteolytic activation of corneal matrix metalloproteinase by Pseudomonas aeruginosa elastase.
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.
Matsumoto
K
K
Schepens Eye Research Institute, Department of Ophthalmology, Harvard Medical School, Boston, MA 02114.
Shams
N B
NB
Hanninen
L A
LA
Kenyon
K R
KR
D000469:Alkaline Phosphatase / Q000494:pharmacology; D001426:Bacterial Proteins; D002478:Cells, Cultured; D003315:Cornea / Q000187:drug effects* / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D005109:Extracellular Matrix / Q000201:enzymology; D005347:Fibroblasts / Q000187:drug effects; D006801:Humans; D020778:Matrix Metalloproteinase 2; D008666:Metalloendopeptidases / Q000378:metabolism* / Q000494:pharmacology*
D001426:Bacterial Proteins; D000469:Alkaline Phosphatase; D008666:Metalloendopeptidases; D020778:Matrix Metalloproteinase 2; C043859:pseudolysin, Pseudomonas aeruginosa