The IL-6 Signal Transducer, gp130: an Pncostatin M Receptor and Affinity Converter for the LIF Receptor
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 complem...
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Published in | Science (American Association for the Advancement of Science) Vol. 255; no. 5050; pp. 1434 - 1437 |
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Main Authors | , , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
13.03.1992
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Online Access | Get full text |
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Summary: | 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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ISSN: | 0036-8075 1095-9203 |
DOI: | 10.1126/science.1542794 |