Molecular attributes of bovine aortic endothelial cell heparan sulfate.
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Department of Clinical Research, Christie Hospital, Manchester, United Kingdom.Issue Date
1995-05-12
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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.Citation
Molecular attributes of bovine aortic endothelial cell heparan sulfate. 1995, 1266 (3):235-44 Biochim. Biophys. ActaJournal
Biochimica et Biophysica ActaDOI
10.1016/0167-4889(95)00012-HPubMed ID
7766709Type
ArticleLanguage
enISSN
0006-3002ae974a485f413a2113503eed53cd6c53
10.1016/0167-4889(95)00012-H
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