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 Ca2+, 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.
Original language | English |
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Pages (from-to) | 91-98 |
Number of pages | 8 |
Journal | Journal of Neuroimmunology |
Volume | 88 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - Aug 1 1998 |
Externally published | Yes |
Bibliographical note
Funding Information:We thank Christine Moogk and J. Andrews for excellent technical assistance and Dr. S.J. Dixon (Dept. of Physiology, Univ. of Western Ontario) for assistance with fluorescence measurement of [Ca 2+ ] i . The authors also thank Mark DeVries for computer assistance. This work was supported by grants from the MRC, JDF-MRC, and Heart and Stroke of Canada.
ASJC Scopus Subject Areas
- Immunology and Allergy
- Immunology
- Neurology
- Clinical Neurology
PubMed: MeSH publication types
- Journal Article
- Research Support, Non-U.S. Gov't