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Originally published In Press as doi:10.1074/jbc.M202335200 on April 24, 2002

J. Biol. Chem., Vol. 277, Issue 30, 26872-26878, July 26, 2002
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The Epithelial Mitogen Keratinocyte Growth Factor Binds to Collagens via the Consensus Sequence Glycine-Proline-Hydroxyproline*

Martin RuehlDagger , Rajan SomasundaramDagger , Ines Schoenfelder, Richard W. Farndale§, C. Graham Knight§, Monika Schmid, Renate Ackermann, Ernst Otto Riecken, Martin Zeitz, and Detlef Schuppan||

From the Department of Medicine I, Klinikum Benjamin Franklin, Free University of Berlin, Hindenburgdamm 30, 12200 Berlin, Germany, the § Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom, and the  Department of Medicine I, University of Erlangen-Nuernberg, Ulmenweg 18, 91054 Erlangen, 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 mesenchymal cell-derived keratinocyte growth factor (KGF), a key stimulator of epithelial cell proliferation during wound healing, preferentially binds to collagens I, III, and VI. Binding is inhibited in a dose-dependent manner by denatured single collagen chains and collagen cyanogen bromide peptides. This interaction is saturable with dissociation constants of ~ 10-8 to 10-9 M and estimated molar ratios of up to three molecules of KGF bound to one molecule of triple helical collagen. Furthermore, collagen-bound KGF stimulated the proliferation of transformed keratinocyte or HaCaT cells. Ligand blotting of collagen-derived peptides points to a limited set of collagenous consensus sequences that bind KGF. By using synthetic collagen peptides, we defined the consensus sequence (Gly-Pro-Hyp)n as the collagen binding motif. We conclude that the preferential binding of KGF to the abundant collagens leads to a spatial pattern of bioavailable KGF that is dictated by the local organization of the collagenous extracellular matrix. The defined collagenous consensus peptide or its analogue may be useful in wound healing by increasing KGF bioactivity and thus modulating local epithelial remodeling and regeneration.

* This study was supported in part by Grants Schu 646/1-10 and SFB366 C5/C10 from the Deutsche Forschungsgemeinschaft, a grant from the Interdisciplinary Center for Clinical Research by the University of Erlangen-Nuernberg, and by a program grant from the Medical Research Council (to C. G. K. and R. W. F.).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.

Dagger Both authors contributed equally to this work.

|| Recipient of a Hermann-and-Lilly-Schilling Professorship. To whom correspondence should be addressed: Medizinische Klinik I, University of Erlangen-Nürnberg Krankenhausstrasse 12, 91054 Erlangen, Germany. Tel.: 09131-853-3398/3386; Fax: 09131-853-6003; 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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