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Blood, 15 June 2001, Vol. 97, No. 12, pp. 3941-3950
PHAGOCYTES
Plasmin-induced expression of cytokines and tissue factor in
human monocytes involves AP-1 and IKK -mediated NF- B
activation
Tatiana Syrovets,
Marina Jendrach,
Angela Rohwedder,
Almut Schüle, and
Thomas Simmet
From the Department of Pharmacology of Natural Products
and Clinical Pharmacology, University of Ulm, Germany; and the
Department of Virology, University of Bochum, Germany.
It was previously shown that plasmin activates human peripheral
monocytes in terms of lipid mediator release and chemotactic migration.
Here it is demonstrated that plasmin induces proinflammatory cytokine
release and tissue factor (TF) expression by monocytes. Plasmin 0.043 to 1.43 CTA U/mL, but not active site-blocked plasmin, triggered concentration-dependent expression of mRNA for
interleukin-1 (IL-1), IL-1 , tumor necrosis factor-
(TNF-), and TF with maximum responses after 4 hours.
Plasmin-mediated mRNA expression was inhibited in a
concentration-dependent manner by the lysine analogue trans-4-(aminomethyl)cyclohexane-1-carboxylic acid
(t-AMCA). Increases in mRNA levels were followed by concentration- and
time-dependent release of IL-1, IL-1 and TNF- and by TF
expression on monocyte surfaces. Neither cytokines nor TF could be
detected when monocytes were preincubated with actinomycin D or
cycloheximide. Electrophoretic mobility shift assays indicated
plasmin-induced activation of NF- B; DNA-binding complexes were
composed of p50, p65, and c-Rel, as shown by supershift experiments.
Nuclear translocation of NF-B/Rel proteins coincided with IB
degradation. At variance with endotoxic lipopolysaccharide, plasmin
elicited the rapid degradation of another cytoplasmic NF-B
inhibitor, p105. Proteolysis of NF-B inhibitors was apparently due
to transient activation of IB kinase (IKK) that reached maximum
activity at 1 hour after plasmin stimulation. In addition, AP-1 binding
was increased in plasmin-treated monocytes, with most complexes
composed of JunD, c-Fos, and FosB. These findings further substantiate
the role of plasmin as a proinflammatory activator of human monocytes
and reveal an important new link between the plasminogen-plasmin system
and inflammation.
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