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Lactoferrin biosynthesis during granulocytopoiesis
TA Rado, J Bollekens, G St. Laurent, L Parker and EJ Benz
We examined the synthesis of lactoferrin, an iron binding protein that,
among hematopoietic cells, is restricted to secondary granules of
polymorphonuclear leukocytes. Lactoferrin biosynthesis was absent from
leukemic myeloblasts and promyelocytes but abundant in normal bone marrow
and both the bone marrow and peripheral blood of patients with chronic
myelogenous leukemia (CGL) if the samples contained substantial numbers of
myelocytes and metamyelocytes. Lactoferrin was present in the steady state
in normal or CGL bands and polymorphonuclear leukocytes, but no lactoferrin
biosynthesis was detectable in these samples. Taken together, these results
suggest that lactoferrin accumulation begins with the onset of biosynthesis
at the myelocyte stage and is largely complete by the beginning of the band
stage of maturation. HL-60 cells, a permanent promyelocytic leukemia cell
line, synthesized no lactoferrin. Translation of messenger RNA in Xenopus
laevis oocytes revealed that mRNA from patients with chronic myelogenous
leukemia and abundant myelocytes and metamyelocytes directed the synthesis
of readily detectable amounts of lactoferrin, whereas HL-60 cells contained
no translatable lactoferrin mRNA. We thus hypothesize that lactoferrin is a
useful marker of gene expression restricted to the terminal stages of
granulocyte maturation. Biosynthesis of this protein appears to be mediated
by appearance of translatable mRNA at the myelocyte stage, coincident with
development of secondary granules. Absence of lactoferrin production by
HL-60 cells is due to absence of translatable lactoferrin mRNA, either
because of lineage infidelity of these transformed cells or because of
arrest before the developmental stage at which secondary granules appear.
Volume 64,
Issue 5,
pp. 1103-1109,
11/01/1984
Copyright © 1984 by The American Society of Hematology
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