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Cancer Research U.K. Growth Factor Group (N.U.-D., L.A.M., V.A.B., J.K.H.), School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom; and Nuffield Department of Obstetrics & Gynaecology (N.K., H.J.M.), University of Oxford, Women’s Centre, John Radcliffe Hospital, Headington, Oxford OX3 9DU, United Kingdom
Address all correspondence and requests for reprints to: Nicholas Underhill-Day, Cancer Research U.K. Growth Factor Group, School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom. E-mail: N.UnderhillDay{at}bham.ac.uk.
IL-11 is a member of the gp130 family of cytokines, which signal via assembly of multisubunit receptor complexes containing at least one molecule of the transmembrane signaling receptor gp130. IL-11 forms a high-affinity complex, thereby inducing gp130-dependent signaling. Previous studies have identified three distinct receptor binding sites, I, II, and III, crucial for the binding of murine IL-11 (mIL-11) to both the IL-11R and gp130. In this study, we have further characterized the role of the mIL-11 site III mutant W147A. We show that W147A is a high-affinity specific antagonist of mIL-11-mediated signaling in gp130/IL-11R-transfected Ba/F3 cells. The antagonistic action of W147A is due to its ability to competitively disrupt multimeric gp130/IL-11R signaling complex formation. We also show that W147A inhibits IL-11-mediated signaling in primary human endometrial cells, thus demonstrating the potential utility of W147A in suppressing IL-11 responses in vivo.
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