Abstract
We have previously shown that free granulocyte elastase (GE) is present for prolonged periods in CF bronchial secretions and that this enzyme may contribute to microbial persistence by proteolysis of opsonins (J.Infect.Dis. 1984, 1986). α1-PI, one of the most important inhibitors of GE was found to be present in an inactive state. In this study, we asked the question whether in CF bronchial secretions α1-PI is inactivated by 1) complex formation with enzyme, 2) oxidation and/or the proteolytic activity of pseudomonas (p) elastase, a protease secreted by strains of P isolated from CF bronchial secretions. α1-PI in 20 CF bronchial secretions was assessed by tandem crossed immunoelectrophoresis and by immunoblots and its migration pattern compared to 1) purified α1-PI inactivated by oxidation, 2) purified α1-PI inactivated by P elastase and 3) purified α1-PI incubated with purified GE. In CF bronchial secretions, we found α1-PI migrating identically to α1-PI fragments generated by PA elastase and those generated by incubation of α1-PI with GE, but not like α1-PI inactivated by oxidation. We conclude that in CF bronchial secretions α1-PI is not inactivated by oxidation, but rather by P elastase and/or GE and that this contributes to the imbalance between proteases and antiproteases.
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Suter, S., Chevallier, I. α1 PROTEINASE INHIBITOR P(α1-PI) IN BRONCHIAL SECRETIONS FROM CYSTIC FIBROSIS (CF) PATIENTS IS NOT INACT TIVATED BY OXIDATION. Pediatr Res 21 (Suppl 4), 336 (1987). https://doi.org/10.1203/00006450-198704010-01012
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DOI: https://doi.org/10.1203/00006450-198704010-01012