Specific binding of the chemokine platelet factor 4 to heparan sulfate.
Affiliation
Cancer Research Campaign, Manchester, M20 9BX, United Kingdom.Issue Date
1997-08-15
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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.Citation
Specific binding of the chemokine platelet factor 4 to heparan sulfate. 1997, 272 (33):20508-14 J. Biol. Chem.Journal
The Journal of Biological ChemistryDOI
10.1074/jbc.272.33.20508PubMed ID
9252363Type
ArticleLanguage
enISSN
0021-9258ae974a485f413a2113503eed53cd6c53
10.1074/jbc.272.33.20508
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