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The differentiation and maturation mediator for human myeloid leukemia
cells shares homology with neuroleukin or phosphoglucose isomerase
W Xu, K Seiter, E Feldman, T Ahmed and JW Chiao
Department of Medicine, New York Medical College, Valhalla 10595, USA.
The identity of the maturation inducer capable of mediating the
differentiation of human myeloid leukemic HL-60 calls to terminal monocytic
cells was investigated. One of such inducers from T cells was purified as a
54.3-kD peptide. The amino acid sequence of a tryptic peptide and the
enzyme cleavage sites revealed 100% homology to neuroleukin or
phosphoglucose isomerase (PGI). Neuroleukin mediates differentiation of
neurons and is homologous to PGI, which catalyzes the interconversion of
glucose-6-phosphate and fructose-6-phosphate. The 54.3-kD inducer was shown
to have PGI enzymatic activity. Separately purified PGI by
substrate-elution exhibited identical specificity as the maturation inducer
for HL-60 cell differentiation. They mediated a reduction of proliferating
S and G2M cells, and the mature monocytic calls acquired complement
receptors, phagocytic capacity, and adherence morphology. The magnitude of
differentiation was dosage dependent on the inducer, with a bell-shaped
curve. At the excess dose range cells did not undergo differentiation and
remained in a proliferating cycle. Abnormally elevated PGI enzyme
activities were detected in the plasma of acute myelogenous leukemia
patients. Whether they represent an excess of the differentiation regulator
in patients and are important in leukemogenesis remain to be investigated.
Volume 87,
Issue 11,
pp. 4502-4506,
06/01/1996
Copyright © 1996 by The American Society of Hematology
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