Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Cell Line
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Enzyme Activation
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Growth Inhibitors / metabolism*
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Humans
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Interleukin-6*
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Leukemia Inhibitory Factor
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Leukemia Inhibitory Factor Receptor alpha Subunit
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Lymphokines / metabolism*
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Mitogen-Activated Protein Kinase 1
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Molecular Sequence Data
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Oncostatin M
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Peptides / metabolism*
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Phosphorylation
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Protein Serine-Threonine Kinases / metabolism
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Protein-Tyrosine Kinases / metabolism
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Receptors, Cytokine / metabolism*
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Receptors, OSM-LIF
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Receptors, Oncostatin M
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Signal Transduction*
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Tumor Cells, Cultured
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Tyrosine / metabolism
Substances
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Growth Inhibitors
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Interleukin-6
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LIF protein, human
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LIFR protein, human
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Leukemia Inhibitory Factor
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Leukemia Inhibitory Factor Receptor alpha Subunit
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Lymphokines
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OSM protein, human
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Peptides
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Receptors, Cytokine
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Receptors, OSM-LIF
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Receptors, Oncostatin M
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Oncostatin M
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Tyrosine
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Protein-Tyrosine Kinases
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Protein Serine-Threonine Kinases
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Mitogen-Activated Protein Kinase 1