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Interleukin-1 induces interleukin-8 secretion from endothelial cells by a
juxtacrine mechanism
G Kaplanski, C Farnarier, S Kaplanski, R Porat, L Shapiro, P Bongrand and CA Dinarello
Department of Medicine, Tufts University, Boston, MA.
Inflammation is characterized by migration of neutrophils through the
endothelium, and the chemokine interleukin-8 (IL-8) appears to be involved.
We asked whether adherence of cells bearing a membrane-form of interleukin
1 (IL-1) induces IL-8 secretion from human umbilical vein endothelial cells
(HUVEC) and fibroblasts. Human peripheral blood mononuclear cells (PBMC)
were stimulated with endotoxin for 12 hours and then fixed for 4 hours with
paraformaldehyde. When these cells were added to HUVEC or fibroblasts, IL-8
production was induced. This stimulation by fixed PBMC was attributed to
IL-1, because pretreatment of HUVEC or fibroblasts with IL-1 receptor
antagonist (IL-1Ra) reduced the induction by 95% and 80%, respectively, P
< .005. Using anti-IL-1 alpha monoclonal antibodies, reduction was
complete, whereas anti-IL-1 beta had no effect. IL-1 alpha was shown on the
surface of monocytes by fluorescence-activated cell sorter (FACS) analysis.
Blockade of IL-1 receptors on PBMC did not affect the activity of
membrane-associated IL- 1 alpha, indicating that IL-1 is not anchored to
the membrane through its receptors. However, PBMC treated with D-mannose
before fixation resulted in a loss of activity; this loss of activity was
associated with release of IL-1 alpha, not IL-1 beta, into the supernatant.
Thus, anchoring of IL-1 alpha to the membrane may be via a lectin or
mannose receptor-like interaction. Blockade of membrane IL-1 alpha required
a 30-fold and fivefold excess of IL-1Ra compared with the amount required
to block soluble IL-1 beta and IL-1 alpha, respectively. We conclude that
the fixed PBMC IL-8 inducing activity is almost entirely caused by IL-1,
that this represents IL-1 alpha bound to a surface lectin or mannose
receptor on the monocyte, and that it functions in inflammation via
juxtacrine interactions.
Volume 84,
Issue 12,
pp. 4242-4248,
12/15/1994
Copyright © 1994 by The American Society of Hematology
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