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Sputum sol neutrophil elastase activity in bronchiectasis: differential modulation by syndecan-1
Stanley C H Chan1, Daisy K Y Shum, Mary S M Ip
1Department of Biochemistry, University of Hong Kong, 21 Sassoon Road, Hong Kong, China. shumdkhk@hkucc.hku.hk
American Journal of Respiratory and Critical Care Medicine
|April 19, 2003
Summary
Neutrophil elastase in bronchiectasis secretions binds to heparan sulfate/syndecan-1, hindering natural inhibitors. Targeting this complex may improve treatment for this lung disease.
Area of Science:
- Pulmonary Medicine
- Biochemistry
- Cell Biology
Background:
- Neutrophil elastase (NE) activity in bronchial secretions contributes to bronchiectasis pathogenesis.
- Antielastases normally regulate NE, but their efficacy is compromised in this condition.
Purpose of the Study:
- To investigate how bronchial secretion components interact with NE.
- To understand the impact of these interactions on antielastase function.
Main Methods:
- Zymographic and Western blot analyses of sputum from bronchiectasis patients.
- Density gradient ultracentrifugation and heparin displacement assays.
Main Results:
- NE was found complexed with heparan sulfate/syndecan-1 and endogenous antielastases (SLPI, A1AT) in sputum.
- NE dissociation from heparan sulfate/syndecan-1 restored full inhibition by antielastases.
- Exogenous SLPI inhibited NE, while A1AT showed limited efficacy.
Conclusions:
- Heparan sulfate/syndecan-1 complexation of NE in secretions impairs antielastase activity.
- Targeting the NE-heparan sulfate/syndecan-1 complex offers a potential therapeutic strategy for bronchiectasis.