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Originally published In Press as doi:10.1074/jbc.M002296200 on June 14, 2000

J. Biol. Chem., Vol. 275, Issue 33, 25273-25285, August 18, 2000
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Receptor Subunit-specific Action of Oncostatin M in Hepatic Cells and Its Modulation by Leukemia Inhibitory Factor*

Yanping WangDagger , Olivier RobledoDagger §, Erin KinzieDagger , Frédéric BlanchardDagger , Carl Richards, Atsushi Miyajima||, and Heinz BaumannDagger **

From the Dagger  Roswell Park Cancer Institute, Department of Molecular and Cellular Biology, Buffalo, New York 14263, the  Department of Pathology, McMaster University, Hamilton, Ontario L8N 3Z5, Canada, and the || Institute of Molecular and Cellular Bioscience, The University of Tokyo, Tokyo 113-0032, Japan

The related cytokines, interleukin-6 (IL-6), oncostatin M (OSM), and leukemia inhibitory factor (LIF) direct the formation of specific heteromeric receptor complexes to achieve signaling. Each complex includes the common signal-transducing subunit gp130. OSM and LIF also recruit the signaling competent, but structurally distinct OSMRbeta and LIFRalpha subunits, respectively. To test the hypothesis that the particularly prominent cell regulation by OSM is due to signals contributed by OSMRbeta , we introduced stable expression of human or mouse OSMRbeta in rat hepatoma cells which have endogenous receptors for IL-6 and LIF, but not OSM. Both mouse and human OSM engaged gp130 with their respective OSMRbeta subunits, but only human OSM also acted through LIFR. Signaling by OSMRbeta -containing receptors was characterized by highest activation of STAT5 and ERK, recruitment of the insulin receptor substrate and Jun-N-terminal kinase pathways, and induction of a characteristic pattern of acute phase proteins. Since LIF together with LIFRalpha appear to form a more stable complex with gp130 than OSM with gp130 and OSMRbeta , co-activation of LIFR and OSMR resulted in a predominant LIF-like response. These results suggest that signaling by IL-6 cytokines is not identical, and that a hierarchical order of cytokine receptor action exists in which LIFR ranks as dominant member.

* This work was supported by National Institutes of Health Grants CA 26122 and DK 38866 (to H. B.) and Roswell Park Grant CA16056.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Present address: Université du Québec, INRS, Laval QC, H7V 1B7 Canada.

** To whom correspondence should be addressed: Roswell Park Cancer Institute, Dept. of Molecular and Cellular Biology, Elm and Carlton Sts., Buffalo, NY 14263. Tel.: 716-845-4587; Fax: 716-845-8389; E-mail: baumann@sc3101.med.buffalo.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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