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Morphological and Compositional Analysis of Neutrophil Extracellular Traps Induced by Microbial and Chemical Stimuli
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Neutrophil proteases degrade autoepitopes of NET-associated proteins
C M de Bont1, N Eerden1, W C Boelens1
1Department of Biomolecular Chemistry, Institute of Molecules and Materials (IMM), Radboud University, Nijmegen, the Netherlands.
Clinical and Experimental Immunology
|October 30, 2019
Summary
Neutrophil proteases alter neutrophil extracellular traps (NETs) by degrading proteins. This process may reduce autoimmune reactions to NET components in conditions like lupus and rheumatoid arthritis.
Area of Science:
- Immunology
- Cell Biology
- Biochemistry
Background:
- Neutrophils form neutrophil extracellular traps (NETs) to trap and clear microbes.
- NETs are composed of decondensed chromatin and antimicrobial proteins.
- NETs are implicated in autoimmune diseases.
Purpose of the Study:
- To investigate the impact of neutrophil proteases on the protein composition of NETs.
- To determine how proteolytic degradation affects NET-associated autoantigens.
Main Methods:
- Analysis of NET protein content after incubation with neutrophil serine proteases.
- Quantification of protein degradation and identification of affected proteins.
Main Results:
- Neutrophil serine proteases significantly degrade various proteins within NETs.
- Antimicrobial proteins like myeloperoxidase and neutrophil elastase (NE) show relative resistance to degradation compared to actin and MNDA.
- Proteolytic activity removes numerous autoepitopes recognized by autoantibodies in systemic lupus erythematosus (SLE) and rheumatoid arthritis (RA) patients.
Conclusions:
- Neutrophil serine proteases substantially modify the NET proteome.
- Proteolytic modification of NETs may serve as a mechanism to mitigate autoimmune responses against NET components.
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