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Biosynthesis and processing of cathepsin G and neutrophil elastase in the
leukemic myeloid cell line U-937
A Lindmark, AM Persson and I Olsson
Department of Medicine, Lund Hospital, Sweden.
The processing of the neutral proteases cathepsin G and neutrophil
elastase, normally synthesized in myeloid precursor cells and stored in
azurophil granules, were investigated by biosynthetic labeling with 14C-
leucine of the monoblastic cell line U-937. The proteases were precipitated
with specific antibodies and the immunoprecipitates were analyzed by sodium
dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) followed by
fluorography. The transfer to lysosomes of newly synthesized proteases was
demonstrated in pulse-chase labeling experiments followed by centrifugation
of cell homogenates in a Percoll gradient. The presence of a closely spaced
polypeptide band-doublet at intermediate gradient density suggested
cleavage of the specific aminoterminal pro dipeptide extension before
storage in lysosomes. The molecular heterogeneity observed for cathepsin G
and neutrophil elastase seemed to be due to modifications occurring after
sorting into lysosomes, most likely because of C-terminal processing.
Modifications of the secreted enzymes were not detectable by SDS-PAGE. In
contrast to other lysosomal enzymes, no phosphorylation was demonstrated.
Newly synthesized cathepsin G and neutrophil elastase rapidly became
resistant to endoglycosidase H, indicating transport through the medial and
trans cisternae of the Golgi complex and conversion to "complex"
oligosaccharide side chains. This conversion was inhibited by an agent
swainsonine, but translocation from the Golgi complex and secretion were
unaffected. The processing described may play a role in activation of the
proteases.
Volume 76,
Issue 11,
pp. 2374-2380,
12/01/1990
Copyright © 1990 by The American Society of Hematology
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