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J. Biol. Chem., Vol. 277, Issue 7, 5082-5089, February 15, 2002
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From the Department of Internal Medicine, The Ohio State
University, Columbus, Ohio 43210 and § INSERM U.255, 75270 Paris Cedex 06, Paris, France
Human monocytes/macrophages express three classes
of receptors for IgG: Fc
Regulated Expression and Inhibitory Function of Fc
RIIb in
Human Monocytic Cells*
,
RI, FcRII, and FcRIII. The expression
and function of these receptors has been extensively studied with the
exception of one, FcRIIb. While the mRNA for FcRIIb has been
detected in human monocytes, the protein has remained elusive. Studies in mouse models indicated that the macrophage FcRIIb serves to down-regulate FcR-mediated phagocytosis and immune complex-induced inflammation. FcRIIb has also been shown to modulate the action of
cytotoxic antibodies against tumors in mouse models. Hence, an
understanding of how FcRIIb expression is regulated is of great
importance. Here we demonstrate for the first time FcRIIb protein
expression and function in human monocytes. We also report that the
expression of FcRIIb is highly up-regulated by interleukin-4, a Th2 cytokine, and that the up-regulation of FcRIIb results in a
decrease in the phagocytic efficiency of interleukin-4-treated THP-1
cells. Furthermore co-clustering FcRIIb with FcRIIa resulted in
enhanced phosphorylation of the inositol phosphatase SHIP, association
of SHIP with Shc, and phosphorylation of additional proteins around 120 and 60-65 kDa, with a concomitant attenuation of Akt activation. We,
therefore, propose that FcRIIb serves to inhibit
FcRI/IIa-mediated macrophage activation using SHIP as its effector.
*
This work was supported by National Institutes of Health
Grants CA44983, HD35121, and HO38764.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Fellow of the Leukemia and Lymphoma Society (formerly Leukemia
Society of America).
¶
To whom correspondence should be addressed: The Ohio State
University College of Medicine, Rm. 430, Heart & Lung Research Institute (HLRI), 473 West Twelfth Ave., Columbus, OH 43210. Tel.: 614-247-7650; Fax: 614-247-7669; E-mail: anderson.48@osu.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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