Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2168032 | Cellular Immunology | 2007 | 7 Pages |
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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Authors
Peter Lemansky, Eva Smolenova, Christian Wrocklage, Andrej Hasilik,