Transactivation of gp130 in Myeloma Cells

Receptor transactivation, i.e., interaction between unrelated receptor systems, is a growing theme in cytokine and growth factor signaling. In this study we reveal for the first time the ability of IFN-alpha to transactivate gp130 in myeloma cells. An epidermal growth factor receptor/gp130 chimeric...

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Bibliographic Details
Published in:The Journal of immunology (1950) 2003-04, Vol.170 (7), p.3717-3723
Main Authors: French, Jena D, Walters, Denise K, Jelinek, Diane F
Format: Article
Language:English
Subjects:
Antigens, CD - genetics
Antigens, CD - metabolism
Antigens, CD - physiology
Cell Membrane - genetics
Cell Membrane - immunology
Cell Membrane - metabolism
Cytokine Receptor gp130
ErbB Receptors - genetics
ErbB Receptors - physiology
Extracellular Space - genetics
Extracellular Space - immunology
Extracellular Space - metabolism
Humans
Interferon-alpha - physiology
Janus Kinase 1
Janus Kinase 2
Ligands
Membrane Glycoproteins - genetics
Membrane Glycoproteins - metabolism
Membrane Glycoproteins - physiology
Multiple Myeloma - immunology
Multiple Myeloma - metabolism
Phosphorylation
Protein Structure, Tertiary
Protein-Tyrosine Kinases - metabolism
Protein-Tyrosine Kinases - physiology
Proteins - metabolism
Proto-Oncogene Proteins
Receptor Cross-Talk - immunology
Receptor, Interferon alpha-beta
Receptors, Interferon - metabolism
Receptors, Interferon - physiology
Receptors, Interleukin-6 - metabolism
Receptors, Interleukin-6 - physiology
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - physiology
Signal Transduction - genetics
Signal Transduction - immunology
Transcriptional Activation - immunology
Transfection
Tumor Cells, Cultured
TYK2 Kinase
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Summary:Receptor transactivation, i.e., interaction between unrelated receptor systems, is a growing theme in cytokine and growth factor signaling. In this study we reveal for the first time the ability of IFN-alpha to transactivate gp130 in myeloma cells. An epidermal growth factor receptor/gp130 chimeric receptor previously shown by us to transactivate endogenous gp130, provided a complementary tool to study the underlying mechanisms of receptor cross-talk. Further analysis revealed that transactivation of gp130 by IFN-alpha did not require the extracellular or trans-membrane domain of gp130. Moreover, transactivation of gp130 was critically dependent upon Janus kinase activation by the initiating receptor and correlated with rapid and sustained Janus kinase 1 and tyrosine kinase (Tyk) 2 tyrosine phosphorylation. Finally, transactivation of gp130 may be a common theme in myeloma cells, perhaps providing a mechanism for enhanced or qualitatively distinct cellular responses to specific stimuli.
ISSN:0022-1767
1550-6606
DOI:10.4049/jimmunol.170.7.3717