The sensory neuropeptide secretoneurin (SN) triggers chemotactic migration of monocytes. We have investigated the possibility that SN, like other chemoattractants such as formyl-Met-Leu-Phe and chemokines, might stimulate migration of monocytes by G protein and protein kinase C (PKC) activation and induce Ca(i)2+release. We report that preincubation of monocytes with pertussis toxin inhibited SN chemotaxis. Staurosporine, an inhibitor of PKC, significantly decreased SN-induced chemotaxis of monocytes, suggesting that PKC may be involved in the signaling. Tyrphostin-23, which inhibits tyrosin kinase, did not affect SN-induced chemotaxis of monocytes. This suggests that SN uses a signaling mechanism that is coupled to pertussis toxin-sensitive G proteins. Involvement of phospholipase Cβ as a result of PKC activation is suggested by a SN-induced increase of intracellular Ca2+concentration in monocytes.
Schratzberger, P., Wöll, E., Reinisch, N., Kähler, C. M., & Wiedermann, C. J. (1996). Secretoneurin-induced in vitro chemotaxis of human monocytes is inhibited by pertussis toxin and an inhibitor of protein kinase C. Neuroscience Letters, 214(2–3), 208–210. https://doi.org/10.1016/0304-3940(96)12947-5