Proteolytic Activation of Corneal Matrix Metalloproteinase byPseudomonas AeruginosaElastase
| Autor: | Koki Matsumoto, Kenneth R. Kenyon, Laila A. Hanninen, Naveed Shams |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Corneal Infection
Matrix metalloproteinase Biology medicine.disease_cause Microbiology Cornea Cellular and Molecular Neuroscience Bacterial Proteins medicine Humans Gelatinase Polyacrylamide gel electrophoresis Cells Cultured Basement membrane Molecular mass Pseudomonas aeruginosa Elastase Metalloendopeptidases Fibroblasts Alkaline Phosphatase Sensory Systems Extracellular Matrix Enzyme Activation Ophthalmology medicine.anatomical_structure Matrix Metalloproteinase 2 Electrophoresis Polyacrylamide Gel |
| Zdroj: | Current Eye Research. 11:1105-1109 |
| ISSN: | 1460-2202 0271-3683 |
| DOI: | 10.3109/02713689209015082 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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