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Originally published In Press as doi:10.1074/jbc.M110011200 on November 15, 2001

J. Biol. Chem., Vol. 277, Issue 5, 3242-3246, February 1, 2002
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Interstitial Collagens I, III, and VI Sequester and Modulate the Multifunctional Cytokine Oncostatin M*

Rajan SomasundaramDagger §, Martin RuehlDagger §, Benjamin SchaeferDagger , Monika SchmidDagger , Renate AckermannDagger , E. O. RieckenDagger , Martin ZeitzDagger , and Detlef Schuppan||

From the Dagger  Medizinische Klinik I (Gastroenterology/Hepatology), Klinikum Benjamin Franklin, Freie Universität Berlin, Hindenbergdamm 30, 12280 Berlin and the  Medizinische Klinik I (Gastroenterology/Hepatology), University of Erlangen-Nuernberg, Krankenhausstrabeta e 12, Erlangen 91054, Germany

The binding of certain growth factors and cytokines to components of the extracellular matrix can regulate their local availability and modulate their biological activities. We show that oncostatin M (OSM), a profibrogenic cytokine and modulator of cancer cell proliferation, specifically binds to collagen types I, III, IV, and VI, immobilized on polystyrene or nitrocellulose. Single collagen chains inhibit these interactions in a dose-dependent manner. Cross-inhibition experiments of collagen-derived peptides point to a limited set of OSM-binding collagenous consensus sequences. Furthermore, this interaction is found for OSM but not for other interleukin-6 type cytokines. OSM binding to collagens is saturable, with dissociation constants around 10-8 M and estimated molar ratios of 1-3 molecules of OSM bound to one molecule of triple helical collagen. Furthermore, collagen-bound OSM is biologically active and able to inhibit proliferation of A375 melanoma cells. We conclude that abundant interstitial collagens dictate the spatial pattern of bioavailable OSM. This interaction could be exploited for devising collagenous peptide-antagonists that modulate OSM bioactivity in tumor growth and fibrotic disorders like rheumatoid arthritis and hepatic fibrosis.

* This study was supported by grants Schu 646/1-10 and SFB366 C5/C10 from the Deutsche Forschungsgemeinschaft and by a grant from the Interdisciplinary Center for Clinical Research (IZKF B18) at the University of Erlangen-Nuernberg.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.

§ Both authors contributed equally to this work.

|| To whom correspondence should be addressed: Medizinische Klinik I, University of Erlangen-Nürnberg, Krankenhausstr. 12, Erlangen 91054, Germany. Tel.: 49-131-85-33398 (Ext. 3386); Fax: 49-131-85-36003; E-mail: detlef.schuppan@med1.imed.uni-erlangen.de.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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