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The Journal of Immunology, 1998, 161: 2533-2540.
Copyright © 1998 by The American Association of Immunologists

Effect of Human C-Reactive Protein on Chemokine and Chemotactic Factor-Induced Neutrophil Chemotaxis and Signaling1

Wangjian Zhong, Qin Zen2, Julie Tebo3, Klaus Schlottmann, Mark Coggeshall and Richard F. Mortensen4

Department of Microbiology and Comprehensive Cancer Center, Ohio State University, Columbus, OH 43210

C-reactive protein (CRP) is a unique serum pentraxin and the prototype acute phase reactant. CRP is a ligand for specific receptors on phagocytic leukocytes, and mediates activation reactions of monocytes/macrophages, but inhibits the respiratory burst of neutrophils (PMN). Since CRP selectively accumulates at inflammatory sites in which IL-8 is also produced, we tested the effects of CRP on the responsiveness of PMN to IL-8 and the bacterial chemotactic peptide, FMLP-phenylalanine (FMLPP). Purified human CRP inhibited the chemotactic response of PMN to IL-8 and FMLPP. A mouse IgM mAb that was generated against the leukocyte CRP receptor (CRP-R) also inhibited the chemotactic response. Incubation of purified CRP with activated PMN generated CRP-derived peptides that also inhibited chemotaxis. A synthetic CRP peptide (residues 27–38) that binds to the CRP-R had weak chemotactic activity, whereas two other CRP synthetic peptides (residues 174–185 and 191–205) inhibited chemotaxis of PMNs to both IL-8 and FMLPP. CRP did not alter receptor-specific binding of IL-8, but exerted its effect at the level of signaling. CRP augmented both IL-8- and FMLPP-induced mitogen-activated protein kinase (extracellular signal-regulated kinase-2) activity. CRP at acute phase levels increased both agonist-induced and noninduced phosphatidylinositol-3 kinase activity. The results suggest a role for CRP as a regulator of leukocyte infiltration at inflammatory sites.




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