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1 Division of Pulmonary Sciences and Critical Care Medicine, University of Colorado Health Sciences Center, Denver, Colorado 80262; and 2 Laboratory of Biomedical Science, North Shore University Hospital, New York University School of Medicine, Manhasset, New York 11030
High
mobility group box 1 (HMGB1) protein, a DNA binding protein that
stabilizes nucleosomes and facilitates transcription, was recently
identified as a late mediator of endotoxin lethality. High serum HMGB1
levels in patients with sepsis are associated with increased mortality,
and administration of HMGB1 produces acute inflammation in animal
models of lung injury and endotoxemia. Neutrophils occupy a critical
role in mediating the development of endotoxemia-associated acute lung
injury, but previously it was not known whether HMGB1 could influence
neutrophil activation. In the present experiments, we demonstrate that
HMGB1 increases the nuclear translocation of NF-
B and enhances the
expression of proinflammatory cytokines in human neutrophils. These
proinflammatory effects of HMGB1 in neutrophils appear to involve the
p38 MAPK, phosphatidylinositol 3-kinase/Akt, and ERK1/2 pathways. The
mechanisms of HMGB1-induced neutrophil activation are distinct from
endotoxin-induced signals, because HMGB1 leads to a different profile
of gene expression, pattern of cytokine expression, and kinetics of p38
activation compared with LPS. These findings indicate that HMGB1 is an
effective stimulus of neutrophil activation that can contribute to
development of a proinflammatory phenotype in diseases characterized by
excessively high levels of HMGB1.
p38 mitogen-activated protein kinase; phosphatidylinositol
3-kinase; Akt; extracellular signal regulated kinase 1/2; nuclear
factor-B; inflammation
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