Тип публикации: статья из журнала
Год издания: 2010
Идентификатор DOI: 10.1515/BC.2010.066
Ключевые слова: antimicrobials, antiproteases, cleavage, microbial, proteases, transglutaminase
Аннотация: Elafin is a 6-kDa innate immune protein present at several epithelial surfaces including the pulmonary epithelium. It is a canonical protease inhibitor of two neutrophil serine proteases wneutrophil elastase (NE) and proteinase 3x with the capacity to covalently bind extracellular matrix proteins by transglutamination. In addition Показать полностьюto these properties, elafin also possesses antimicrobial and immunomodulatory activities. The aim of the present study was to investigate the effect of Pseudomonas aeruginosa proteases on elafin function. We found that P. aeruginosa PAO1-conditioned medium and two purified Pseudomonas metalloproteases, pseudolysin (elastase) and aeruginolysin (alkaline protease), are able to cleave recombinant elafin. Pseudolysin was shown to inactivate the anti-NE activity of elafin by cleaving its protease-binding loop. Interestingly, antibacterial properties of elafin against PAO1 were found to be unaffected after pseudolysin treatment. In contrast to pseudolysin, aeruginolysin failed to inactivate the inhibitory properties of elafin against NE. Aeruginolysin cleaves elafin at the amino-terminal Lys6- Gly7 peptide bond, resulting in a decreased ability to covalently bind purified fibronectin following transglutaminase activity. In conclusion, this study provides evidence that elafin is susceptible to proteolytic cleavage at alternative sites by P. aeruginosa metalloproteinases, which can affect different biological functions of elafin. © by Walter de Gruyter, Berlin, New York.
Журнал: Biological Chemistry
Выпуск журнала: Т. 391, № 6
Номера страниц: 705-716
ISSN журнала: 14316730
Издатель: Walter de Gruyter GmbH & Co. KG