Specific binding of the chemokine platelet factor 4 to heparan sulfate.
Stringer, Sally E Gallagher, John T
Stringer, Sally E
Gallagher, John T
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Abstract
Platelet factor 4 is a tetrameric heparin binding chemokine released from the alpha-granules of activated platelets. In this study we show that platelet factor 4 binds with high affinity and specificity to an approximately 9-kDa sequence in heparan sulfate, which it protects from degradation by heparinase enzymes. This protected fragment is enriched in N-sulfated disaccharides and iduronate 2-O-sulfate residues, the latter being important for binding to platelet factor 4. The major structural motif of the fragment appears to consist of a pair of sulfated domains positioned at both ends separated by a central mainly N-acetylated region. On the basis of these findings, we propose a model in which the heparan sulfate fragment wraps around the ring of positive charges on platelet factor 4 with the iduronate 2-O-sulfates within the sulfated domains binding strongly to lysine clusters on opposite faces of the tetramer.
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1997-08-15
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Specific binding of the chemokine platelet factor 4 to heparan sulfate. 1997, 272 (33):20508-14 J. Biol. Chem.