Neutrophil elastase is a serine protease stored in granules of neutrophils. Its ability to cleave proteins can alter structures outside or within the cell, depending on where the active enzyme is located. A particularly illuminating example connects proteolysis to organization of chromatin.[ref]
In a 2010 study, activation caused neutrophil elastase to reach the cell nucleus, where it partly degraded particular histones. Experiments with isolated nuclei and purified enzyme connected that cleavage to chromatin decondensation; Western blot measurements followed the protein changes. The study also found defective neutrophil extracellular trap formation in mice lacking the enzyme in its tested infection model.[ref]
Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps by Venizelos Papayannopoulos and others. Abstract and Fig. 1E–I, histone processing, purified enzyme and nuclear decondensation
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