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Sorting of the specific granule protein, NGAL, during granulocytic
maturation of HL-60 cells
V Le Cabec, J Calafat and N Borregaard
Department of Hematology, Finsen Center, The National University Hospital,
Rigshospitalet, Copenhagen, Denmark.
The different types of human neutrophil granules (azurophil, specific, and
gelatinase granules) are formed sequentially during maturation of
neutrophils from the promyelocyte stage to the band cell stage. The
promyelocytic HL-60 cells can maturate to segmented granulocytes but are
incapable of activating the transcription of any known intragranular
protein, normally located in specific or gelatinase granules. To study the
sorting of granule proteins during maturation, we transfected HL-60 cells
with the specific granule protein NGAL, inserted under control of a
cytomegalovirus promoter. We previously showed that NGAL is sorted to
azurophil granules and colocalizes with myeloperoxidase in undifferentiated
HL-60 cells. We show here that, when such transfected HL-60 cells
differentiate into granulocytes, newly synthesized NGAL is not retained in
granules but is constitutively secreted. This indicates that highly
specific mechanisms must exist that are responsible for diverting transport
vesicles into storage granules, and that HL-60 cells not only lack the
ability to activate transcription of specific granule proteins, but also
lose the ability to form storage granules during maturation.
Volume 89,
Issue 6,
pp. 2113-2121,
03/15/1997
Copyright © 1997 by The American Society of Hematology
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