Abstract
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-α 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-α 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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 3717-3723 |
| Number of pages | 7 |
| Journal | Journal of Immunology |
| Volume | 170 |
| Issue number | 7 |
| State | Published - Apr 1 2003 |
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ASJC Scopus subject areas
- Immunology
Cite this
Transactivation of gp130 in myeloma cells. / French, Jena D.; Walters, Denise K.; Jelinek, Diane F.
In: Journal of Immunology, Vol. 170, No. 7, 01.04.2003, p. 3717-3723.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Transactivation of gp130 in myeloma cells
AU - French, Jena D.
AU - Walters, Denise K.
AU - Jelinek, Diane F
PY - 2003/4/1
Y1 - 2003/4/1
N2 - 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-α 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-α 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.
AB - 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-α 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-α 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0037379269&partnerID=8YFLogxK
M3 - Article
C2 - 12646637
AN - SCOPUS:0037379269
VL - 170
SP - 3717
EP - 3723
JO - Journal of Immunology
JF - Journal of Immunology
SN - 0022-1767
IS - 7
ER -