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Oncostatin M and Leukemia Inhibitory Factor Do Not Use the Same Functional Receptor in Mice
Masatoshi Ichihara,
Takahiko Hara,
Heejung Kim,
Takashi Murate, and
Atsushi Miyajima
From First Department of Internal Medicine, Nagoya University School of Medicine, Nagoya, Japan; DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA; and Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo, Japan.
Oncostatin M (OSM) and leukemia inhibitory factor (LIF ) are members of the interleukin-6 (IL-6) subfamily of cytokines that use a common signal transducer gp130. Human OSM (hOSM) and LIF share a functional high-affinity receptor that is composed of gp130 and LIF receptor  subunit (LIFR). A second high-affinity receptor for hOSM was recently found to be formed by gp130 and the hOSM receptor subunit. However, the nature of murine OSM (mOSM) and its receptors has remained unknown. Using the recently cloned mOSM cDNA, we produced recombinant mOSM and studied its biological activity and receptor structure. Murine hematopoietic cell lines M1 and DA1.a, an embryonic stem cell line CCE, and Ba/F3 transfectants expressing gp130 and LIFR responded to murine LIF (mLIF ) and hOSM equally well, while these cells responded to mOSM only at a 30-fold to 100-fold higher concentration than those of mLIF and hOSM. In contrast, NIH3T3 cells responded to mOSM, but not to mLIF and hOSM. Scatchard plot analyses showed that mOSM bound to gp130 with low-affinity (kd = 2.8 to 4.2 nmol/L) and that the binding affinity did not increase in the presence of LIFR. However, mOSM bound to NIH3T3 cells with high-affinity (kd = 660 pmol/L), whereas mLIF did not bind to NIH3T3 cells at all. These results indicate that unlike hOSM, mOSM and mLIF do not share the same functional receptor, and mOSM delivers signals only through its specific receptor complex. Further studies in mice will define the physiological roles of OSM.
Blood, Vol. 90 No. 1 (July 1), 1997:
pp. 165-173
© 1997 by The American Society of Hematology.
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