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Originally published In Press as doi:10.1074/jbc.M000313200 on June 7, 2000

J. Biol. Chem., Vol. 275, Issue 43, 33688-33696, October 27, 2000
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High Molecular Weight Kininogen Utilizes Heparan Sulfate Proteoglycans for Accumulation on Endothelial Cells*

Thomas Renné, Jürgen Dedio, Guido DavidDagger §, and Werner Müller-Esterl

From the Institute for Biochemistry II, Johann Wolfgang Goethe-University of Frankfurt, Theodor-Stern-Kai 7, D-60590 Frankfurt, Germany and the Dagger  Center for Human Genetics, University of Leuven and Flanders Interuniversity Institute for Biotechnology, B-3000 Leuven, Belgium

Kininogens, the high molecular weight precursor of vasoactive kinins, bind to a wide variety of cells in a specific, reversible, and saturable manner. The cell docking sites have been mapped to domains D3 and D5H of kininogens; however, the corresponding cellular acceptor sites are not fully established. To characterize the major cell binding sites for kininogens exposed by the endothelial cell line EA.hy926, we digested intact cells with trypsin and other proteases and found a time- and concentration-dependent loss of 125I-labeled high molecular weight kininogen (H-kininogen) binding capacity (up to 82%), indicating that proteins are crucially involved in kininogen cell attachment. Cell surface digestion with heparinases similarly reduced kininogen binding capacity (up to 78%), and the combined action of heparinases and trypsin almost eliminated kininogen binding (up to 85%), suggesting that proteoglycans of the heparan sulfate type are intimately involved. Consistently, inhibitors such as p-nitrophenyl-beta -D-xylopyranoside and chlorate interfering with heparan sulfate proteoglycan biosynthesis reduced the total number of kininogen binding sites in a time- and concentration-dependent manner (up to 67%). In vitro binding studies demonstrated that biotinylated H-kininogen binds to heparan sulfate glycosaminoglycans via domains D3 and D5H and that the presence of Zn2+ promotes this association. Cloning and over-expression of the major endothelial heparan sulfate-type proteoglycans syndecan-1, syndecan-2, syndecan-4, and glypican in HEK293t cells significantly increased total heparan sulfate at the cell surface and thus the number of kininogen binding sites (up to 3.3-fold). This gain in kininogen binding capacity was completely abolished by treating transfected cells with heparinases. We conclude that heparan sulfate proteoglycans on the surface of endothelial cells provide a platform for the local accumulation of kininogens on the vascular lining. This accumulation may allow the circumscribed release of short-lived kinins from their precursor molecules in close proximity to their sites of action.

* This work was supported in part by grants from the Deutsche Forschungsgemeinschaft (Mu598/5-3), and from the Fonds der Chemischen Industrie (to W. M. E.).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.

§ Supported by the Flanders Interuniversity Institute for Bio/Technology and the Fonds voor Wetenschappelijk Onderzoek-Vlaanderen.

To whom correspondence should be addressed. Tel.: 49-69-6301-5652; Fax: 49-69-6301-5577; E-mail: wme@biochem2.de.

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