Syndecan-1 and -4 synthesized simultaneously by mouse mammary gland epithelial cells bear heparan sulfate chains that are apparently structurally indistinguishable.

2.50
Hdl Handle:
http://hdl.handle.net/10541/82318
Title:
Syndecan-1 and -4 synthesized simultaneously by mouse mammary gland epithelial cells bear heparan sulfate chains that are apparently structurally indistinguishable.
Authors:
Zako, Masahiro; Dong, Jianying; Goldberger, Olga; Bernfield, Merton; Gallagher, John T; Deakin, Jon A
Abstract:
Many 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.
Affiliation:
Division of Newborn Medicine, Children's Hospital, Harvard Medical School, Boston, Massachusetts 02215, USA. zako@aichi-med.ac.jp
Citation:
Syndecan-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.
Journal:
The Journal of Biological Chemistry
Issue Date:
11-Apr-2003
URI:
http://hdl.handle.net/10541/82318
DOI:
10.1074/jbc.M209658200
PubMed ID:
12571251
Type:
Article
Language:
en
ISSN:
0021-9258
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
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.en
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
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