Syndecan-1 and -4 synthesized simultaneously by mouse mammary gland epithelial cells bear heparan sulfate chains that are apparently structurally indistinguishable.
AffiliationDivision of Newborn Medicine, Children's Hospital, Harvard Medical School, Boston, Massachusetts 02215, USA. email@example.com
MetadataShow full item record
AbstractMany of the biological functions attributed to cell surface heparan sulfate (HS) proteoglycans, including the Syndecan family, are elicited through the interaction of their HS chains with soluble extracellular molecules. Tightly controlled, cell-specific sulfation and epimerization of HS precursors endows these chains with highly sulfated, iduronate-rich regions, which are major determinants of cytokine and matrix-protein binding and which are interspersed by N-acetylated, poorly sulfated regions. Until this study, there have been no comprehensive structural comparisons made on HS chains decorating simultaneously expressed, but different, syndecan core proteins. In this paper we demonstrate that the HS chains on affinity-purified syndecan-1 and -4 from murine mammary gland cells are essentially identical by a number of parameters. Size determination, disaccharide analyses, enzymatic and chemical scission methods, and affinity co-electrophoresis all failed to reveal any significant differences in fine structure, domain organization, or ligand-binding properties of these HS species. These findings lead us to suggest that the imposition of the fine structure onto HS occurs independently of the core protein to which it is attached and that these core proteins, in addition to the HS chains, may play a pivotal role in the various biological functions ascribed to these macromolecules.
CitationSyndecan-1 and -4 synthesized simultaneously by mouse mammary gland epithelial cells bear heparan sulfate chains that are apparently structurally indistinguishable. 2003, 278 (15):13561-9 J. Biol. Chem.
JournalThe Journal of Biological Chemistry
- Cell surface syndecan-1 on distinct cell types differs in fine structure and ligand binding of its heparan sulfate chains.
- Authors: Kato M, Wang H, Bernfield M, Gallagher JT, Turnbull JE
- Issue date: 1994 Jul 22
- Structural characterization of heparan sulfate and chondroitin sulfate of syndecan-1 purified from normal murine mammary gland epithelial cells. Common phosphorylation of xylose and differential sulfation of galactose in the protein linkage region tetrasaccharide sequence.
- Authors: Ueno M, Yamada S, Zako M, Bernfield M, Sugahara K
- Issue date: 2001 Aug 3
- Chondroitin sulfate chains on syndecan-1 and syndecan-4 from normal murine mammary gland epithelial cells are structurally and functionally distinct and cooperate with heparan sulfate chains to bind growth factors. A novel function to control binding of midkine, pleiotrophin, and basic fibroblast growth factor.
- Authors: Deepa SS, Yamada S, Zako M, Goldberger O, Sugahara K
- Issue date: 2004 Sep 3
- Heparan sulfate chains from glypican and syndecans bind the Hep II domain of fibronectin similarly despite minor structural differences.
- Authors: Tumova S, Woods A, Couchman JR
- Issue date: 2000 Mar 31
- Core protein structure and sequence determine the site and presence of heparan sulfate and chondroitin sulfate on syndecan-1.
- Authors: Kokenyesi R, Bernfield M
- Issue date: 1994 Apr 22