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Secretoneurin, a Novel Neuropeptide, Is a Potent Chemoattractant
for Human Eosinophils
Stefan Dunzendorfer,
Peter Schratzberger,
Norbert Reinisch,
Christian M. Kähler, and
Christian J. Wiedermann
From the Laboratory of Intensive Care Medicine, the Division of
General Internal Medicine, the Department of Medicine, University of
Innsbruck, Innsbruck, Austria.
Secretoneurin (SN), a 33-amino acid neuropeptide, is derived from
secretogranin II that is released from sensory afferent C-fibers by
capsaicin. Described functions of secretoneurin include chemotaxis of
monocytes and endothelial cells, and inhibition of endothelial cell
proliferation. Inhibition of monocyte chemotaxis by staurosporine
indicated involvement of specific signaling pathways. We have tested
effects of SN, substance P (SP), and interleukin-8 (IL-8) on eosinophil
migration in modified Boyden chambers including signaling mechanisms of
neuropeptide and cytokine stimulation of human eosinophils. Experiments
showed SN as eosinophil chemoattractant comparable in its potency to
IL-8. Checkerboard analysis, usage of a specific anti-SN-antibody, and
receptor desensitization experiments confirmed the chemotactic
activity. Preincubation of the cells with effective concentrations of
staurosporine or tyrphostin-23 showed no effect, whereas treatment with
wortmannin (WTN) or 3-isobutyl-1-methylxantin (IBMX) completely blocked
SN-induced migration. Additionally, experiments ruled out
tyrphostin-23- and WTN-sensitive signaling pathways for
SP-induced chemotaxis of eosinophils. We conclude that
SN-stimulated human eosinophil chemotaxis is mediated via a unique and
specific signal transduction pathway that involves activation of
phosphodiesterases and WTN-sensitive enzymes, ie, phospholipase D and
phosphatidylinositol-3-kinase. In contrast, we report that activation
of the latter and tyrosine kinases is required for
SP-induced chemotaxis of eosinophils.
Blood, Vol. 91 No. 5 (March 1), 1998:
pp. 1527-1532
© 1998 by The American Society of Hematology.
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