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Regulation of interleukin-6 expression in cultured human blood monocytes
and monocyte-derived macrophages
J Bauer, U Ganter, T Geiger, U Jacobshagen, T Hirano, T Matsuda, T Kishimoto, T Andus, G Acs and W Gerok
Medizinische Klinik, Universitat Freiburg, FRG.
A culture system that allows human blood monocytes to differentiate into
macrophages in vitro was used to study B-cell stimulatory factor-
2/interleukin-6 (interferon-beta 2/26 kd protein) expression in mononuclear
phagocytes. Using B-cell stimulatory factor-2 (BSF-2) cDNA and a
polyclonal, monospecific antibody directed against human BSF-2, we find
that strong interleukin-6 (IL-6) expression is initiated in cultured
monocytes on stimulation with endotoxin. Maximally induced monocytic
BSF-2/IL-6 synthesis (1% to 2% of total proteins secreted by monocytes) is
more than ten times stronger than in terminally differentiated macrophages
(approximately 0.1% of total secretory proteins). BSF-2/IL-6 mRNA was
detectable as early as one hour after stimulation with endotoxin, reaching
maximum levels three hours after stimulus. Interleukin-1 (IL-1) was able to
stimulate IL-6 synthesis in monocytes, but not in macrophages. Tumor
necrosis factor, interferon- gamma and interleukin-2 (IL-2) had no effect
on IL-6 synthesis in monocytes or macrophages. We found five molecular
weight forms of BSF- 2/IL-6 to be secreted by monocytes of 21.5 kd, 23.5
kd, 24 kd, 26 kd, and 28 kd apparent molecular weight. The 26 kd and 28 kd
forms were found to represent N-glycosylated molecules, which were not
detectable on treatment of the cells with the N-glycosylation inhibitor
tunicamycin. The 21.5 kd, 23.5 kd, and 24 kd BSF-2/IL-6 forms were
unaffected by tunicamycin treatment. We conclude from our data that cells
of the mononuclear phagocyte lineage are one of the main sites of
BSF-2/IL-6 (interferon-beta 2/26 kd protein/HSF) synthesis.
Volume 72,
Issue 4,
pp. 1134-1140,
10/01/1988
Copyright © 1988 by The American Society of Hematology
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