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C-Reactive Protein Binding to Murine Leukocytes Requires Fc Receptors¹

Mary-Pat Stein^*,, Carolyn Mold and Terry W. Du Clos^2,*,

^* Veterans Affairs Medical Center, Albuquerque, NM 87108; and Departments of Medicine and Molecular Genetics and Microbiology, University of New Mexico School of Medicine, Albuquerque, NM 87131

Human C-reactive protein (CRP) is an acute phase protein that binds to receptors on human and mouse leukocytes. We have recently determined that the high and low affinity receptors for CRP on human leukocytes are FcRIIa and FcRI, respectively. Previous work by others suggested that CRP receptors on mouse macrophages are distinct from FcR. We have taken advantage of the availability of mice deficient in one or more FcR to reexamine the role of FcR in CRP binding to mouse leukocytes. Three strains of FcR-deficient mice were examined: -chain-deficient mice that lack FcRI and FcRIII, FcRII-deficient mice, and mice deficient in both -chain and FcRII that lack all FcR. No binding of CRP was detected to leukocytes from double-deficient mice, indicating that FcR are required for CRP binding. CRP binding to leukocytes from -chain-deficient and FcRII-deficient mice was reduced compared with binding to leukocytes from wild-type mice. Further analysis of CRP binding to macrophages, neutrophils, and lymphocytes provides direct evidence that FcRIIb1, FcRIIb2, and FcRI are the receptors for CRP on mouse leukocytes. These findings may have important implications in understanding the physiological function of CRP.

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