Recombinant soluble interleukin-11 (IL-11) receptor alpha-chain can act as an IL-11 antagonist
- Author(s)
- Curtis, DJ; Hilton, DJ; Roberts, B; Murray, L; Nicola, N; Begley, CG;
- Details
- Publication Year 1997-12-01,Volume 90,Issue #11,Page 4403-4412
- Journal Title
- BLOOD
- Publication Type
- Journal Article
- Abstract
- We have expressed a soluble N-glycosylated form of the murine interleukin-ll (IL-ll) receptor alpha-chain (sIL-11R) and examined signaling in cells expressing the gp130 molecule. In the presence of gp130 but not the transmembrane IL-11R, the sIL-11R mediated IL-ll-dependent differentiation of M1 leukemic cells and proliferation in Ba/F3 cells, Early intracellular events stimulated by the sIL-11R including phosphorylation of gp130, STAT 3, and SHP-2 were similar to signaling through the transmembrane IL-11R, IL-ll bound to sIL-11R with low affinity (kd 10 to 50 nmol/L). Binding of sIL-11R to gp130 was IL-ll dependent with intermediate affinity (kd 1.5 to 3.0 nmol/L), However, the concentration of IL-ll required for signaling through the sIL-11R was 10- to 20-fold greater than that required for cells expressing the transmembrane IL-11R and gp130 in the absence of sIL-11R. Furthermore, the sIL-11R was capable of antagonizing the activity of IL-ll when tested on cells expressing the transmembrane IL-11R and gp130, We propose that the observed IL-ll antagonism by the sIL-11R may depend on limiting numbers of gp130 molecules on cells already expressing the transmembrane IL-11R. (C) 1997 by The American Society of Hematology.
- Publisher
- W B SAUNDERS CO
- Keywords
- LEUKEMIA-INHIBITORY FACTOR; SIGNAL TRANSDUCER; ONCOSTATIN-M; CYTOKINE RECEPTORS; MOLECULAR-CLONING; GP130; BINDING; MURINE; EXPRESSION; COMPLEX
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Creation Date: 1997-12-01 12:00:00