| Autor: |
Gearing DP; Immunex Research and Development Corporation, Seattle, WA 98101., Comeau MR, Friend DJ, Gimpel SD, Thut CJ, McGourty J, Brasher KK, King JA, Gillis S, Mosley B, et. al. |
| Jazyk: |
angličtina |
| Zdroj: |
Science (New York, N.Y.) [Science] 1992 Mar 13; Vol. 255 (5050), pp. 1434-7. |
| DOI: |
10.1126/science.1542794 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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