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dc.contributor.authorZako, Masahiro
dc.contributor.authorDong, Jianying
dc.contributor.authorGoldberger, Olga
dc.contributor.authorBernfield, Merton
dc.contributor.authorGallagher, John T
dc.contributor.authorDeakin, Jon A
dc.date.accessioned2009-09-23T11:53:35Z
dc.date.available2009-09-23T11:53:35Z
dc.date.issued2003-04-11
dc.identifier.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.en
dc.identifier.issn0021-9258
dc.identifier.pmid12571251
dc.identifier.doi10.1074/jbc.M209658200
dc.identifier.urihttp://hdl.handle.net/10541/82318
dc.description.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.
dc.language.isoenen
dc.subject.meshAnimals
dc.subject.meshCell Line
dc.subject.meshChromatography, Gel
dc.subject.meshChromatography, High Pressure Liquid
dc.subject.meshCollagen
dc.subject.meshDisaccharides
dc.subject.meshEpithelial Cells
dc.subject.meshFemale
dc.subject.meshHeparin Lyase
dc.subject.meshHeparitin Sulfate
dc.subject.meshMammary Glands, Animal
dc.subject.meshMembrane Glycoproteins
dc.subject.meshMice
dc.subject.meshProteoglycans
dc.subject.meshSulfates
dc.subject.meshSulfur Radioisotopes
dc.subject.meshSyndecan-1
dc.subject.meshSyndecan-4
dc.subject.meshSyndecans
dc.titleSyndecan-1 and -4 synthesized simultaneously by mouse mammary gland epithelial cells bear heparan sulfate chains that are apparently structurally indistinguishable.en
dc.typeArticleen
dc.contributor.departmentDivision of Newborn Medicine, Children's Hospital, Harvard Medical School, Boston, Massachusetts 02215, USA. zako@aichi-med.ac.jpen
dc.identifier.journalThe Journal of Biological Chemistryen
html.description.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.


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