The IL-6 Signal Transducer, gp130: an Pncostatin M Receptor and Affinity Converter for the LIF Receptor

• DOI: 10.1126/science.1542794
• Publication Date: 2006-10-05T23:03:06Z
• Authors: David P. Gearing; Michael R. Comeau; Della J. Friend; Steven D. Gimpel; Catherine J. Thut; Jackie McGourty; Kelle K. Brasher; Julie A. King; Steven Gillis; Bruce Mosley; Steven F. Ziegler; David Cosman
• Keywords: Lymphokines; 0303 health sciences; Membrane Glycoproteins; Receptors, OSM-LIF; Interleukin-6; Oncostatin M; Transfection; Binding, Competitive; Leukemia Inhibitory Factor; Growth Inhibitors; Recombinant Proteins; Radioligand Assay; 03 medical and health sciences; Antigens, CD; Cytokine Receptor gp130; Animals; Receptors, Cytokine; Receptors, Immunologic; Peptides; Cell Line, Transformed

Leukemia inhibitory factor (LIF) and interleukin-6 (IL-6) are multifunctional cytokines with many similar activities. LIF is structurally and functionally related to another cytokine, Oncostatin M (OSM), that binds to the high-affinity LIF receptor but not to the low-affinity LIF receptor. A complementary DNA was isolated that encodes the high-affinity converting subunit of the LIF receptor. The converter conferred high-affinity binding of both LIF and OSM when expressed with the low-affinity LIF receptor and is identical to the signal transducing subunit of the IL-6 receptor, gp130. The gp130 subunit alone confers low-affinity binding of OSM when expressed in COS-7 cells. This receptor system resembles the high-affinity receptors for granulocyte-macrophage colony-stimulating factor, IL-3, and IL-5, which share a common subunit.