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Published online before print February 9, 2005
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receptors in human monocytes
Research Division, Hospital for Special Surgery and Department of Medicine and Graduate Program in Immunology, Weill Medical College of Cornell University, New York, New York
1 Correspondence: Hospital for Special Surgery, Weill Medical College of Cornell University, 535 East 70th Street, New York, NY 10021. E-mail: PRICOPL{at}HSS.EDU
Fc
receptors (FcR) trigger inflammatory reactions in response to immunoglobulin-opsonized pathogens and antigen-antibody complexes. The coordinate expression of activating and inhibitory FcR ensures the homeostasis of immune complex-driven inflammatory responses. In this study, we used antibodies with preferential binding for activating FcRIIa and inhibitory FcRIIb receptors to investigate the expression and regulation of FcRII isoforms in human monocytes. Cross-linking of FcRIIa triggered phagocytosis and cytokine production. Cross-linking of FcRIIb was associated with phosphorylation of the immunoreceptor tyrosine-based inhibitory motif and with a marked reduction in monocyte effector functions. Our study revealed that tumor necrosis factor 
(TNF-), interleukin (IL)-10, and IL-13 altered the transcriptional activity of the FcRIIB promoter in transfected cell lines and skewed the balance of activating versus inhibitory FcR in human monocytes. TNF- decreased the expression of inhibitory FcRIIb. IL-10 up-regulated all classes of FcR and induced alternative activation in monocytes, an effect that was synergistic with that of TNF-. In contrast, IL-4 and IL-13, in combination with TNF-, decreased the expression of activating FcR and markedly down-regulated FcR-mediated function. Our findings suggest that the cytokine milieu can induce changes in the relative expression of FcR with opposing function and thus, may regulate the amplitude of FcR-mediated uptake and inflammation.
Key Words: phagocytes • hypersensitivity • inflammation
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