Identification, purification, and characterization of a soluble interleukin (IL)-13-binding protein - Evidence that it is distinct from the cloned IL-13 receptor and IL-4 receptor alpha-chains
- Author(s)
- Zhang, JG; Hilton, DJ; Willson, TA; McFarlane, C; Roberts, BA; Moritz, RL; Simpson, RJ; Alexander, WS; Metcalf, D; Nicola, NA;
- Details
- Publication Year 1997-04-04,Volume 272,Issue #14,Page 9474-9480
- Journal Title
- JOURNAL OF BIOLOGICAL CHEMISTRY
- Publication Type
- Journal Article
- Abstract
- Interleukin-4 (IL-4) and interleukin-13 (IL-13) are structurally and functionally related cytokines which play an important role in the regulation of the immune response to infection, The functional similarity of IL-4 and IL-13 can be explained, at least in part, by the common components that form their cell surface receptors, namely the IL-4 receptor alpha-chain (IL-4R alpha) and the IL-13 receptor alpha-chain (IL-13R alpha), Soluble forms of the IL-4R alpha have also been described and implicated in modulating the effect of IL-4. In this paper we describe the presence of a 45,000-50,000 M(r) IL-13-binding protein (IL-13BP) in the serum and urine of mice, This protein binds IL-13 with a 100-300-fold higher affinity (K-D = 20-90 pM) than does the cloned IL-13R alpha (K-D = 3-10 nM). In addition to this functional difference, the IL-13BP appears to be structurally and antigenically distinct from the IL-13R alpha. Finally, unlike the cloned receptor, the IL-13BP acts as a potent inhibitor of IL-13 binding to its cell surface receptor, raising the possibility that it may be used to modulate the effects of IL-13 in vivo.
- Publisher
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
- Keywords
- LEUKEMIA INHIBITORY FACTOR; GAMMA-CHAIN; SIGNAL-TRANSDUCTION; BINDING-PROTEIN; B-CELLS; SUBUNIT; EXPRESSION; COMPONENT; RESPONSES; MECHANISM
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Creation Date: 1997-04-04 12:00:00