Oncostatin M and leukemia inhibitory factor trigger overlapping and different signals through partially shared receptor complexes
| Autor: | B, Thoma, T A, Bird, D J, Friend, D P, Gearing, S K, Dower |
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| Rok vydání: | 1994 |
| Předmět: |
Mitogen-Activated Protein Kinase 1
Lymphokines Leukemia Inhibitory Factor Receptor alpha Subunit Receptors OSM-LIF Interleukin-6 Molecular Sequence Data Receptors Oncostatin M Oncostatin M Protein Serine-Threonine Kinases Protein-Tyrosine Kinases Leukemia Inhibitory Factor Growth Inhibitors Cell Line Enzyme Activation Tumor Cells Cultured Humans Tyrosine Amino Acid Sequence Phosphorylation Receptors Cytokine Peptides Signal Transduction |
| Zdroj: | The Journal of biological chemistry. 269(8) |
| ISSN: | 0021-9258 |
| Popis: | Leukemia inhibitory factor (LIF) and oncostatin M (OSM) both bind to the same receptor with high affinity and thus mediate an overlapping spectrum of biological activities, the signal transduction mechanisms for which are unclear. We show that mitogen-activated protein kinases are involved in both the LIF and OSM signal transduction pathways. However, we found that OSM is a much more potent inducer of both mitogen-activated protein kinase activity and biological response, both of which correlate with the expression of a second OSM receptor that does not bind LIF. In addition, different patterns of tyrosine-phosphorylated proteins were stimulated by OSM and LIF. We therefore suggest that the two receptors for OSM can be coupled to different signal transduction events. |
| Databáze: | OpenAIRE |
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