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    Specific binding of the chemokine platelet factor 4 to heparan sulfate.

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    Authors
    Stringer, Sally E
    Gallagher, John T
    Affiliation
    Cancer Research Campaign, Manchester, M20 9BX, United Kingdom.
    Issue Date
    1997-08-15
    
    Metadata
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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.
    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 Chemistry
    URI
    http://hdl.handle.net/10541/95223
    DOI
    10.1074/jbc.272.33.20508
    PubMed ID
    9252363
    Type
    Article
    Language
    en
    ISSN
    0021-9258
    ae974a485f413a2113503eed53cd6c53
    10.1074/jbc.272.33.20508
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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