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Inducible production of interleukin-6 by human polymorphonuclear
neutrophils: role of granulocyte-macrophage colony-stimulating factor and
tumor necrosis factor-alpha
NA Cicco, A Lindemann, J Content, P Vandenbussche, M Lubbert, J Gauss, R Mertelsmann and F Herrmann
Department of Hematology and Oncology, University of Freiburg, FRG.
The recent demonstration of the ability of human polymorphonuclear
neutrophils (PMN) to secrete various cytokines in response to the
granulocyte activator granulocyte-macrophage colony-stimulating factor
(GM-CSF) but not to other cytokines, has led to the identification of PMN
as biosynthetically active cells. In this study we have investigated the
ability of PMN to secrete interleukin-6 (IL-6), a molecule known to be
involved in inflammatory reactions. Using RNA blotting analysis and
bioassays, we show that PMN could be induced to synthesize transcripts
specific for IL-6, indistinguishable in size from IL-6 mRNA produced by
activated human macrophages. Consequently, PMN released IL-6-like activity
into their culture supernatants that could be neutralized by monospecific
anti-IL-6 antibody. Interleukin-6 secretion by PMN, however, required
previous stimulation with GM-CSF or tumor necrosis factor-alpha
(TNF-alpha), whereas other cytokines, including interleukin-3 (IL-3),
granulocyte-CSF (G-CSF), macrophage-CSF (M-CSF), interferon gamma
(IFN-gamma), and lymphotoxin (LT), failed to induce IL-6 mRNA accumulation
and protein secretion by PMN. Similar to GM-CSF and TNF-alpha, other
compounds, including the inhibitor of protein synthesis cyclohexemide
(CHX), endotoxin (Escherichia coli- derived lipopolysaccharide), and
phorbol myristate acetate (PMA) (but not the chemoattractant
N-formyl-methionyl-leucyl-phenylalanine [FMLP]), induced detectable levels
of IL-6 transcripts in PMN.
Volume 75,
Issue 10,
pp. 2049-2052,
05/15/1990
Copyright © 1990 by The American Society of Hematology
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