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C-Reactive Protein Induces Signaling Through FcRIIa on HL-60 Granulocytes^{1 ,2}

Maoyen Chi^*, Susheela Tridandapani, Wangjian Zhong^*, K. Mark Coggeshall and Richard F. Mortensen^3,*

Departments of ^* Microbiology and Internal Medicine, Ohio State University, Columbus, OH 43210; and Immunobiology and Cancer Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104

Human C-reactive protein (CRP) at acute phase levels of 10–200 µg/ml triggered the phosphorylation of FcRIIa, Syk kinase, and phospholipase C2 in granulocytic HL-60 cells. CRP also stimulated translocation to the membrane of both phospholipase C2 and phosphatidylinositol-3-kinase. The signaling response triggered by CRP was a rapid, early event with kinetics similar to the response elicited by human IgG. Both soluble-aggregated CRP and monomeric CRP cross-linked FcRII to generate a signal of the same intensity. The results are consistent with signaling through the intrinsic immunoreceptor tyrosine-based activation motif of the cytoplasmic domain of FcRIIa, the major CRP-receptor on monocytes and neutrophils that is responsible for CRP-mediated phagocytosis. The signaling events driven by CRP have the potential to regulate infiltrating neutrophil activities.

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