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Reactive oxygen intermediates cause rapid release of the interleukin-1
decoy receptor from human myelomonocytic cells
P Sambo, EJ Fadlon, M Sironi, C Matteucci, M Introna, A Mantovani and F Colotta
Istituto de Ricerche Farmacologiche Mario Negri, Milano, Italy.
Free radicals play an important role in inflammation. We found that
reactive oxygen intermediates (ROI) inhibit interleukin-1beta (IL- 1beta)
binding on human myelomonocytes. Production of superoxide anion (O2-) by
Xanthine (X) and Xanthine-Oxidase (XO) or NADPH caused a reduction (48% +/-
15% in 25 experiments) in the IL-1beta binding of polymorphonuclear cells
(PMN) and monocytes that was inhibited by superoxide dismutase (SOD).
Hydrogen peroxide (H2O2) was only active on monocytes and this effect was
prevented by catalase. O2(-)-induced loss of IL-1beta binding on PMN
reached half maximum at 5 minutes and peaked after 30 minutes. The
reduction of IL-1beta binding was due to reduction of IL-1beta receptors
(R) on PMN surface without any change in affinity. ROI-induced reduction of
surface IL-1R was not caused by receptor internalization, but rather by the
release of a soluble form (45 kD) of the type II decoy R. The action of ROI
on IL-1 binding was selective because major histocompatibility complex
class I, CD18 and CD16 were unaffected. The O2(-)-induced release of IL-1
decoy R was not affected by protein synthesis inhibitors, but was partially
blocked by protease inhibitors. Release of the IL-1 type II decoy R might
represent one mechanism by which ROI antagonize and limit the
proinflammatory effects of IL-1.
Volume 87,
Issue 5,
pp. 1682-1686,
03/01/1996
Copyright © 1996 by The American Society of Hematology
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