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Updated: Jul 13, 2026

Monitoring Neutrophil Elastase and Cathepsin G Activity in Human Sputum Samples
Published on: May 21, 2021
Neutrophil elastase is associated with serglycin on its way to lysosomes in U937 cells
Peter Lemansky1, Eva Smolenova, Christian Wrocklage
1Institute of Physiological Chemistry, Philipps-University Marburg, Karl-von-Frisch-Str. 1, 35033 Marburg/Lahn, Germany. lemansky@staff.uni-marburg.de
Abstract:
Mutations in the neutrophil elastase (NE) gene have been postulated to interfere with normal intracellular trafficking of NE as an AP3-interacting membrane integrated protein and to cause severe congenital or cyclic neutropenia in humans. Here, we show that in U937 promonocytes NE is synthesized as a predominantly soluble proenzyme and is completely secreted in the presence of phorbol esters similarly to serglycin. Using chemical cross-linking NE is shown to be associated with serglycin as 34 kDa proenzyme in the trans-Golgi region of these cells indicating that it is delivered to lysosomes associated with serglycin.
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