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J. Biol. Chem., Vol. 282, Issue 33, 24083-24091, August 17, 2007

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Soluble CD23 Monomers Inhibit and Oligomers Stimulate IGE Synthesis in Human B Cells^*

Natalie McCloskey¹², James Hunt, Rebecca L. Beavil, Mark R. Jutton, Gabrielle J. Grundy, Enrico Girardi, Stella M. Fabiane¹, David J. Fear, Daniel H. Conrad^¶, Brian J. Sutton, and Hannah J. Gould

From the Medical Research Council Asthma UK Centre in Allergic Mechanisms of Asthma and the Randall Division of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, United Kingdom, the Laboratory of Molecular Biology, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, and the ^¶Department of Microbiology and Immunology, Virginia Commonwealth University, Richmond, Virginia 23298

The low affinity IgE receptor, CD23, is implicated in IgE regulation and the pathogenesis of allergic disease. CD23 is a type II integral membrane protein, comprising a lectin "head," N-terminal "stalk," and C-terminal "tail" in the extracellular sequence. Endogenous proteases cleave CD23 in the stalk and the tail to release soluble fragments that either stimulate or inhibit IgE synthesis in human B cells. The molecular basis of these paradoxical activities is not understood. We have characterized three fragments of CD23, monomeric derCD23, monomeric exCD23, and oligomeric lzCD23. We show that the monomers inhibit and the oligomer stimulates IgE synthesis in human B cells after heavy chain switching to IgE. CD23 fragments could be targets for therapeutic intervention in allergic disease.

Received for publication, April 16, 2007 , and in revised form, May 31, 2007.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Supported by Wellcome Trust Programme Grant 076343.

² To whom correspondence should be addressed: Randall Division of Cell and Molecular Biophysics, King's College London, New Hunt's House, St. Thomas' St., London SE1 1UL, United Kingdom. Tel.: 44-207-848-6458; Fax: 44-207-848-6435; E-mail: natalie.mccloskey{at}kcl.ac.uk.

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