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Published on: June 7, 2018
Human neutrophil elastase abolishes interleukin-8 chemotactic activity
K J Leavell1, M W Peterson, T J Gross
1Department of Internal Medicine, University of Iowa College of Medicine, Iowa City 52242, USA.
Journal of Leukocyte Biology
|March 1, 1997
Summary
Human neutrophil elastase (HNE) degrades interleukin-8 (IL-8), a key inflammatory chemokine. This proteolysis inactivates IL-8, suggesting a novel mechanism to control inflammatory lung disease.
Area of Science:
- Immunology
- Molecular Biology
- Pulmonary Medicine
Background:
- Interleukin-8 (IL-8) is a critical chemokine in inflammatory lung diseases, attracting polymorphonuclear leukocytes.
- The fate and regulation of IL-8 at inflammatory sites are not well understood.
Purpose of the Study:
- To investigate the degradation of IL-8 by human neutrophil elastase (HNE).
- To determine if HNE affects IL-8's biological activity and structure.
Main Methods:
- Incubation of recombinant human IL-8 with purified HNE.
- Assays for IL-8 chemotactic activity and immunoreactivity.
- Western blot analysis to detect IL-8 fragments.
- Comparison with other serine proteases (urokinase, plasmin, thrombin, cathepsin G).
Main Results:
- HNE dose- and time-dependently abolished IL-8 chemotactic activity and immunoreactivity.
- Western blots showed IL-8 was proteolyzed into small fragments by HNE.
- HNE's effect was specific, as other proteases did not degrade IL-8.
- HNE also degraded IL-8 secreted by human monocytes.
Conclusions:
- Human neutrophil elastase specifically degrades and inactivates IL-8.
- HNE-mediated proteolysis represents a novel mechanism for down-regulating IL-8-driven inflammation.
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