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* Lung Inflammatory Group, Center for Inflammation Research, University of Edinburgh, Edinburgh, United Kingdom; and
Respiratory Medicine Division, Department of Medicine, University of Cambridge School of Clinical Medicine, Addenbrooke’s and Papworth Hospitals, Cambridge, United Kingdom
Neutrophils are a vital component of the early acute inflammatory
response, but can cause profound tissue damage when activated to excess
or prevented from undergoing apoptosis. However, much remains unknown
about the intracellular signaling pathways regulating neutrophil
activity. The structurally diverse neutrophil-priming agents
platelet-activating factor, TNF-
, and the substance P analog
[D-Arg6,
D-Trp7,9,NmePhe8]-substance
P(6–11) (SP-G) stimulated a rapid increase in sphingosine kinase
activity in freshly isolated human neutrophils. This activity was
blocked by preincubation with the sphingosine kinase inhibitor
N,N-dimethylsphingosine (DMS). DMS also inhibited the
increase in intracellular calcium concentration stimulated by
platelet-activating factor, fMLP, and SP-G. This suggests that the
increase in intracellular calcium concentration by these agents is
dependent on sphingosine kinase activation and the generation of
sphingosine-1-phosphate. Changes in cell polarization and the
augmentation of the fMLP-induced superoxide anion generation, by all
priming agents were also inhibited by DMS, while only the superoxide
anion release was blocked by the phosphatidylinositol 3-kinase
inhibitor LY294002. Moreover, SP-G and GM-CSF inhibited constitutive
neutrophil apoptosis which was completely blocked by DMS. These results
suggest a novel role for sphingosine kinase in the regulation of
neutrophil priming.
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