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A more recent version of this article appeared on March 15, 2002
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M108109200v1
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Papers In Press, published online ahead of print January 10, 2002
J. Biol. Chem, 10.1074/jbc.M108109200
Submitted on August 22, 2001
Revised on December 9, 2001
Accepted on January 9, 2002

A novel mechanism by which interferon-gamma can regulate IL-13 responses: Evidence for intracellular stores of IL-13 receptor alpha 2 and their rapid mobilization by interferon-gamma

Michael O. Daines and Gurjit K. Khurana Hershey

Pediatrics, Children's Hospital Medical Center, Cincinnati, Ohio 45229

Corresponding Author: Gurjit.Hershey{at}chmcc.org

IL-13 mediates its activities via a complex receptor system. IL-13Ra1 binds IL-13 with low affinity, but does not signal. However, when IL-13Ra1 combines with IL-4 receptor alpha (IL-4Ra), a signaling high affinity receptor complex for IL-13 is generated. In contrast, IL-13Ra2 alone binds IL-13 with high affinity, but does not signal and has been postulated to be a decoy receptor. Herein, we investigated the cellular localization of IL-13Ra2 and the regulation of its expression by confocal microscopy and flow cytometry in primary and cultured cells. Our results demonstrate that IL-13Ra2 is largely an intracellular molecule, which is rapidly mobilized from intracellular stores following treatment with IFN-g. Upregulation of IL-13Ra2 surface expression in response to IFN-g was rapid, did not require protein synthesis, and resulted in diminished IL-13 signaling. These results provide the first evidence that the IL-13Ra2 is predominantly an intracellular molecule and demonstrate a novel mechanism by which IFN-g can regulate IL-13 responses.


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