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and TNF Regulate Macrophage Expression of the Chemotactic S100 Protein S100A81
Cytokine Research Unit, School of Pathology, Faculty of Medicine, University of New South Wales, Sydney, Australia
The murine calcium-binding protein S100A8 is a potent
chemoattractant for neutrophils and monocytes in vivo and in vitro but
may also play a protective role. We show that the kinetics of induction
of S100A8 mRNA in elicited murine macrophages (Mac) by LPS, IFN-
,
and TNF were distinct from the C-C chemokines monocyte chemoattractant
protein-1 (MCP-1), macrophage-inflammatory protein-1
(MIP-1), and
RANTES. Monomeric S100A8 was predominantly secreted. IFN substantially
increased S100A8 mRNA levels after 1 h with optimal induction
after 12 h; induction by TNF was slower and more sustained. TNF
did not up-regulate MCP-1 and MIP-1 mRNA in these cells. Luciferase
reporter assays confirmed that LPS and IFN induce S100A8 gene
transcription and mRNA in LPS-treated Mac showed little decay over
16 h, whereas transcripts induced by IFN and TNF were markedly
less stable. Newly synthesized proteins may be required for mRNA
transcription and stabilization in response to LPS. S100A9 associates
with A8 in neutrophils, but was not coinduced with S100A8. S100A8 gene
induction in Mac stimulated with LPS and IFN may be modulated by
mobilization of intracellular Ca2+ concentration from
distinct intracellular stores and/or the extracellular compartment and
by distinct pathways involving protein kinase C and leading to
activation of mitogen-activated protein kinase.
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