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Activation of the NF-kappaB pathway by inflammatory stimuli in human
neutrophils
PP McDonald, A Bald and MA Cassatella
Department of General Pathology, University of Verona, Italy.
Activated neutrophils have the ability to upregulate the expression of many
genes, in particular those encoding cytokines and chemokines, and to
subsequently release the corresponding proteins. Although little is known
to date concerning the regulation of gene transcription in neutrophils, it
is noteworthy that many of these genes depend on the activation of
transcription factors, such as NF-kappaB, for inducible expression. We
therefore investigated whether NF-kappaB/Rel proteins are expressed in
human neutrophils, as well as their fate on cell activation. We now report
that dimers consisting of p50 NFkappaB1, p65 RelA, and/or c-Rel are present
in neutrophils and that the greater part of these protein complexes is
physically associated with cytoplasmic IkappaB-alpha in resting cells.
Following neutrophil stimulation with proinflammatory agonists (such as
lipopolysaccharide [LPS], tumor necrosis factor-alpha [TNF-alpha], and
fMet-Leu-Phe) that induce the production of cytokines and chemokines in
these cells, NF-kappaB/Rel proteins translocated to nuclear fractions,
resulting in a transient induction of NF-kappaB DNA binding activity, as
determined in gel mobility shift assays. The onset of both processes was
found to be closely paralleled by, and dependent on, IkappaB-alpha
degradation. Proinflammatory neutrophil stimuli also promoted the
accumulation of IkappaB-alpha mRNA transcripts, resulting in the
reexpression of the IkappaB-alpha protein. To our knowledge, this
constitutes the first indication that NF-kappaB activation may underlie the
action of proinflammatory stimuli towards human neutrophil gene expression
and, as such, adds a new facet to our understanding of neutrophil biology.
Volume 89,
Issue 9,
pp. 3421-3433,
05/01/1997
Copyright © 1997 by The American Society of Hematology
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