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

David P. Gearing(Research & Development Corporation), Michael R. Comeau(Research & Development Corporation), Della Friend(Research & Development Corporation), Steven D. Gimpel(Research & Development Corporation), Catherine J. Thut(Research & Development Corporation), Jackie McGourty(Research & Development Corporation), Kelle K. Brasher(Research & Development Corporation), Julie A. King(Research & Development Corporation), Steven Gillis(Research & Development Corporation), Bruce Mosley(Research & Development Corporation), Steven F. Ziegler(Research & Development Corporation), David Cosman(Research & Development Corporation)
Science
March 13, 1992
Cited by 897

Abstract

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.


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