2.50
Hdl Handle:
http://hdl.handle.net/10541/95223
Title:
Specific binding of the chemokine platelet factor 4 to heparan sulfate.
Authors:
Stringer, Sally E; Gallagher, John T
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.
Affiliation:
Cancer Research Campaign, Manchester, M20 9BX, United Kingdom.
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
Issue Date:
15-Aug-1997
URI:
http://hdl.handle.net/10541/95223
DOI:
10.1074/jbc.272.33.20508
PubMed ID:
9252363
Type:
Article
Language:
en
ISSN:
0021-9258
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorStringer, Sally Een
dc.contributor.authorGallagher, John Ten
dc.date.accessioned2010-03-30T10:21:45Z-
dc.date.available2010-03-30T10:21:45Z-
dc.date.issued1997-08-15-
dc.identifier.citationSpecific binding of the chemokine platelet factor 4 to heparan sulfate. 1997, 272 (33):20508-14 J. Biol. Chem.en
dc.identifier.issn0021-9258-
dc.identifier.pmid9252363-
dc.identifier.doi10.1074/jbc.272.33.20508-
dc.identifier.urihttp://hdl.handle.net/10541/95223-
dc.description.abstractPlatelet 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.en
dc.language.isoenen
dc.subject.meshBinding Sites-
dc.subject.meshHeparin Lyase-
dc.subject.meshHeparitin Sulfate-
dc.subject.meshPlatelet Factor 4-
dc.subject.meshPolysaccharide-Lyases-
dc.titleSpecific binding of the chemokine platelet factor 4 to heparan sulfate.en
dc.typeArticleen
dc.contributor.departmentCancer Research Campaign, Manchester, M20 9BX, United Kingdom.en
dc.identifier.journalThe Journal of Biological Chemistryen

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