Abstract
Secretoneurin (SN) is a 33-amino acid peptide derived from secretogranin II (chromogranin C) which induces chemotaxis of monocytes but not neutrophils. In this study, we found that SN interacted with specific cell surface binding sites on human monocytes. The chemoattractants MCP-1, MCP-2 or fMLP could not compete for SN binding sites suggesting SN may bind to a novel chemotactic receptor. Additional studies showed that neither SN nor MCP-2 induced a rise in cytosolic Ca 2+, and chemotaxis to SN was inhibited by cholera toxin (CT) and pertussis toxin (PT). Chemotactic desensitization studies demonstrated that fMLP, MCP-1, SN, and MCP-2 could all desensitize monocytes to subsequent SN stimulation. Our results indicate that SN binds to a cell surface receptor expressed on monocytes and activates signaling pathways which are sensitive to CT and PT.
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