| Literature DB >> 1542794 |
D P Gearing1, M R Comeau, D J Friend, S D Gimpel, C J Thut, J McGourty, K K Brasher, J A King, S Gillis, B Mosley.
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.Entities:
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Year: 1992 PMID： 1542794 DOI： 10.1126/science.1542794
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728