This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Heck, L W Articles by Abrahamson, D R Search for Related Content PubMed PubMed Citation Articles by Heck, L W Articles by Abrahamson, D R

Degradation of soluble laminin and depletion of tissue-associated basement membrane laminin by Pseudomonas aeruginosa elastase and alkaline protease.

ABSTRACT

Purified Pseudomonas aeruginosa elastase and alkaline protease rapidly cleaved soluble laminin, with each enzyme yielding different cleavage products. These cleavage fragments were separated from the intact laminin A and B polypeptide chains by sodium dodecyl sulfate-polyacrylamide gradient gel electrophoresis and detected by their characteristic Coomassie blue staining patterns. Pseudomonas elastase produced rapid and extensive degradation of both A and B chains, including the disulfide-rich regions. Apparently complete degradation to limit digests was obtained after 30 min with a substrate/enzyme ratio of 30:0.5. Under similar conditions, alkaline protease rapidly degraded the A chain while slowly degrading the B chain. In addition, immunoreactive laminin was released from authentic basement membranes after incubation with either enzyme as detected by an enzyme-linked immunoabsorption assay and by immunofluorescence. The results from these studies suggest a direct role for elastase and alkaline protease in both tissue invasion and hemorrhagic tissue necrosis in P. aeruginosa infections.

This article has been cited by other articles:

• Bandara, M. B. K., Zhu, H., Sankaridurg, P. R., Willcox, M. D. P. (2006). Salicylic Acid Reduces the Production of Several Potential Virulence Factors of Pseudomonas aeruginosa Associated with Microbial Keratitis.. IOVS 47: 4453-4460 [Abstract] [Full Text]  
• Rocha, C. L., Rucks, E. A., Vincent, D. M., Olson, J. C. (2005). Examination of the Coordinate Effects of Pseudomonas aeruginosa ExoS on Rac1. Infect. Immun. 73: 5458-5467 [Abstract] [Full Text]  
• Feltzer, R. E., Trent, J. O., Gray, R. D. (2003). Alkaline Proteinase Inhibitor of Pseudomonas aeruginosa: A MUTATIONAL AND MOLECULAR DYNAMICS STUDY OF THE ROLE OF N-TERMINAL RESIDUES IN THE INHIBITION OF PSEUDOMONAS ALKALINE PROTEINASE. J. Biol. Chem. 278: 25952-25957 [Abstract] [Full Text]  
• Thakur, A., Xue, M., Stapleton, F., Lloyd, A. R., Wakefield, D., Willcox, M. D. P. (2002). Balance of Pro- and Anti-Inflammatory Cytokines Correlates with Outcome of Acute Experimental Pseudomonas aeruginosa Keratitis. Infect. Immun. 70: 2187-2197 [Abstract] [Full Text]  
• Feltzer, R. E., Gray, R. D., Dean, W. L., Pierce, W. M. Jr. (2000). Alkaline Proteinase Inhibitor of Pseudomonas aeruginosa. INTERACTION OF NATIVE AND N-TERMINALLY TRUNCATED INHIBITOR PROTEINS WITH PSEUDOMONAS METALLOPROTEINASES. J. Biol. Chem. 275: 21002-21009 [Abstract] [Full Text]