Molecular attributes of bovine aortic endothelial cell heparan sulfate.

2.50
Hdl Handle:
http://hdl.handle.net/10541/99264
Title:
Molecular attributes of bovine aortic endothelial cell heparan sulfate.
Authors:
Pye, David A; Kumar, Shant
Abstract:
Heparan sulfate (HS) secreted into the medium of bovine aortic endothelial cell (BAEC) cultures was subjected to chemical and enzymatic degradation followed by analysis using gel-filtration and ion-exchange chromatography. Treatment with HNO2 showed that 41% of the disaccharides were N-sulfated. Degradation by Heparin lyases I (Hep I) showed that 8-9% of the disaccharides contained IdoA(2S) residues. Heparin lyase III (Hep III) degradation produced mainly disaccharides with 67% of the molecules glycosidic linkages susceptible to cleavage. Further degradation of Hep III-resistant fragments with Hep I showed that IdoA(2S) residues were predominantly positioned centrally within the repeating GlcNSO3(+/- 6S)alpha 1-4IdoA containing domains. Digestion with a mixture of Heparin lyases I, II and III degraded the molecule almost entirely to disaccharides, with small amounts of tetrasaccharides containing resistant linkages, suggesting the presence of 3-O sulfated GlcNSO3. Further analysis of the disaccharide products by ion-exchange chromatography and comparison with the data from single enzymatic digestion, allowed an estimate of the disaccharide composition to be made. The results suggest an ordered arrangement of structural domains; however, variations in the structure of these domains results in a heterogeneous population of HS chains. It is suggested that biosynthetic differences in HS structure may act as a regulator of bFGF induced cellular responses.
Affiliation:
Department of Clinical Research, Christie Hospital, Manchester, United Kingdom.
Citation:
Molecular attributes of bovine aortic endothelial cell heparan sulfate. 1995, 1266 (3):235-44 Biochim. Biophys. Acta
Journal:
Biochimica et Biophysica Acta
Issue Date:
12-May-1995
URI:
http://hdl.handle.net/10541/99264
DOI:
10.1016/0167-4889(95)00012-H
PubMed ID:
7766709
Type:
Article
Language:
en
ISSN:
0006-3002
Appears in Collections:
All Christie Publications

Full metadata record

DC FieldValue Language
dc.contributor.authorPye, David Aen
dc.contributor.authorKumar, Shanten
dc.date.accessioned2010-05-19T10:06:02Z-
dc.date.available2010-05-19T10:06:02Z-
dc.date.issued1995-05-12-
dc.identifier.citationMolecular attributes of bovine aortic endothelial cell heparan sulfate. 1995, 1266 (3):235-44 Biochim. Biophys. Actaen
dc.identifier.issn0006-3002-
dc.identifier.pmid7766709-
dc.identifier.doi10.1016/0167-4889(95)00012-H-
dc.identifier.urihttp://hdl.handle.net/10541/99264-
dc.description.abstractHeparan sulfate (HS) secreted into the medium of bovine aortic endothelial cell (BAEC) cultures was subjected to chemical and enzymatic degradation followed by analysis using gel-filtration and ion-exchange chromatography. Treatment with HNO2 showed that 41% of the disaccharides were N-sulfated. Degradation by Heparin lyases I (Hep I) showed that 8-9% of the disaccharides contained IdoA(2S) residues. Heparin lyase III (Hep III) degradation produced mainly disaccharides with 67% of the molecules glycosidic linkages susceptible to cleavage. Further degradation of Hep III-resistant fragments with Hep I showed that IdoA(2S) residues were predominantly positioned centrally within the repeating GlcNSO3(+/- 6S)alpha 1-4IdoA containing domains. Digestion with a mixture of Heparin lyases I, II and III degraded the molecule almost entirely to disaccharides, with small amounts of tetrasaccharides containing resistant linkages, suggesting the presence of 3-O sulfated GlcNSO3. Further analysis of the disaccharide products by ion-exchange chromatography and comparison with the data from single enzymatic digestion, allowed an estimate of the disaccharide composition to be made. The results suggest an ordered arrangement of structural domains; however, variations in the structure of these domains results in a heterogeneous population of HS chains. It is suggested that biosynthetic differences in HS structure may act as a regulator of bFGF induced cellular responses.en
dc.language.isoenen
dc.subject.meshAnimals-
dc.subject.meshAorta-
dc.subject.meshCarbohydrate Sequence-
dc.subject.meshCattle-
dc.subject.meshCells, Cultured-
dc.subject.meshChromatography, Gel-
dc.subject.meshChromatography, Ion Exchange-
dc.subject.meshDisaccharides-
dc.subject.meshEndothelium, Vascular-
dc.subject.meshHeparin Lyase-
dc.subject.meshHeparitin Sulfate-
dc.subject.meshIduronic Acid-
dc.subject.meshMolecular Sequence Data-
dc.subject.meshOligosaccharides-
dc.subject.meshPolysaccharide-Lyases-
dc.titleMolecular attributes of bovine aortic endothelial cell heparan sulfate.en
dc.typeArticleen
dc.contributor.departmentDepartment of Clinical Research, Christie Hospital, Manchester, United Kingdom.en
dc.identifier.journalBiochimica et Biophysica Actaen
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