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J. Biol. Chem., Vol. 275, Issue 43, 33688-33696, October 27, 2000
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From the Institute for Biochemistry II, Johann Wolfgang
Goethe-University of Frankfurt, Theodor-Stern-Kai 7, D-60590 Frankfurt,
Germany and the 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-
High Molecular Weight Kininogen Utilizes Heparan Sulfate
Proteoglycans for Accumulation on Endothelial Cells*
§, and Center for Human Genetics, University of
Leuven and Flanders Interuniversity Institute for Biotechnology, B-3000
Leuven, Belgium
-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.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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