Secretoneurin and chemoattractant receptor interactions
| Autor: | Ross D. Feldman, Bhagirath Singh, Luoling Xu, C Kong, B. M. Gill, Sushil K. Mahata, David J. Kelvin, Laurent Taupenot, R. Rahimpour, Q Xiao, Daniel T. O'Connor, T.J McDonald |
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| Rok vydání: | 1998 |
| Předmět: |
Cholera Toxin
Receptors Peptide Immunology Biology Pertussis toxin medicine.disease_cause Monocytes Cell surface receptor medicine Immunology and Allergy Chemokine CCL8 Humans Virulence Factors Bordetella Receptors Immunologic Receptor Chemokine CCL2 G protein-coupled receptor Binding Sites Secretoneurin Cholera toxin Neuropeptides Chemotaxis Intracellular Membranes Molecular biology Receptors Formyl Peptide Monocyte Chemoattractant Proteins N-Formylmethionine Leucyl-Phenylalanine Chemotaxis Leukocyte Neurology Biochemistry Pertussis Toxin Secretogranin II Calcium Neurology (clinical) Signal transduction |
| Zdroj: | Journal of neuroimmunology. 88(1-2) |
| ISSN: | 0165-5728 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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