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Synthesis of eosinophil-associated enzymes in HL-60 promyelocytic leukemia
cells
SA Fischkoff, GE Brown and A Pollak
Eosinophils derived from HL-60 cells share many of the abnormalities of
granule histochemistry and morphology frequently seen in eosinophils of
patients with certain malignancies, especially those seen in acute
myelomonocytic leukemia with abnormal eosinophils (FAB class M4eo). In
order to understand the pathogenesis of these abnormalities, four enzymes,
characteristic of the eosinophil, were studied in HL-60 promyelocytic
leukemia cells at various stages of eosinophilic differentiation. Using
biochemical and ultrahistochemical techniques, the following differences
from normal eosinophil development were demonstrated. First, both
myeloperoxidase and eosinophil peroxidase coexisted in the population of
maturing HL-60 eosinophils. Second, the granules formed from the
condensation of material in vacuoles which were derived from dilated
segments of the endoplasmic reticulum; the role of the Golgi apparatus in
processing of peroxidase appeared minimal. Third, low levels of
lysophospholipase and arylsulfatase were present in the cells compared to
normal eosinophils. Finally, crystallizations resembling precursor
structures of Auer rods appeared in the granules of about 5% of the cells.
These findings suggest that several disorders of the control of protein
synthesis and processing exist in HL-60 eosinophils which may be
responsible for the abnormal granule morphology and histochemistry.
Volume 68,
Issue 1,
pp. 185-192,
07/01/1986
Copyright © 1986 by The American Society of Hematology
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