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Papers In Press, published online ahead of print June 28, 2004
Department of Biochemistry, Kobe Pharmaceutical University, Kobe, Hyogo 658-8558
Corresponding Author: k-sugar{at}kobepharma-u.ac.jp
A comparative analysis was carried out of heparan sulfate (HS) and chondroitin sulfate (CS) chains of the ectodomains of hybrid type transmembrane proteoglycans, syndecan-1 and -4, synthesized simultaneously by normal murine mammary gland epithelial cells. While the HS chains were structurally indistinguishable, intriguingly the CS chains were structurally and functionally distinct, probably reflecting the differential regulation of sulfotransferases involved in the synthesis of HS and CS. The CS chains of the two syndecans were comprised of nonsulfated, 4-O-, 6-O- and 4,6-O-disulfated GalNAc-containing disaccharide units and were significantly different, with a higher degree of sulfation for syndecan-4. Functional analysis using a BIAcore system showed that basic fibroblast growth factor (bFGF) specifically bound only to the HS chains of both syndecans, whereas midkine (MK) and pleiotrophin (PTN) bound not only to the HS but also to the CS chains. Stronger binding of MK and PTN to the CS chains of syndecan-4 than those of syndecan-1 was revealed, supporting the structural and functional differences. Intriguingly, removal of the CS chains decreased the association and dissociation rate constants of MK, PTN and bFGF for both syndecans, suggesting the simultaneous binding of these growth factors to both types of chains, producing a ternary complex that transfers the growth factors to the corresponding cell surface receptors more efficiently as compared with the HS chains alone. The involvement of the core protein was also shown in the binding of MK and PTN to syndecan-1, suggesting the possibility of co-operation with the HS and/or CS chains in the binding of these growth factors and their delivery to the cell surface receptors.
J. Biol. Chem, 10.1074/jbc.M403031200
Submitted on March 18, 2004
Revised on June 21, 2004
Accepted on June 28, 2004
Chondroitin sulfate chains on syndecan-1 and syndecan-4 from normal murine mammary gland epithelial cells are structurally and functionally distinct, and co-operate with heparan sulfate chains to bind growth factors: A novel function to control binding of midkine, pleiotrophin and basic fibroblast growth factor
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