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dc.contributor.authorHampson, Ian Nen
dc.contributor.authorKumar, Shanten
dc.contributor.authorGallagher, John Ten
dc.date.accessioned2011-03-08T12:38:08Z
dc.date.available2011-03-08T12:38:08Z
dc.date.issued1984-09-28
dc.identifier.citationHeterogeneity of cell-associated and secretory heparan sulphate proteoglycans produced by cultured human neuroblastoma cells. 1984, 801 (2):306-13 Biochim Biophys Actaen
dc.identifier.issn0006-3002
dc.identifier.pmid6236854
dc.identifier.doi10.1016/0304-4165(84)90081-3
dc.identifier.urihttp://hdl.handle.net/10541/123876
dc.description.abstractBiosynthetically radiolabelled heparan sulphate proteoglycans have been isolated from the growth medium and the cell lysate of a human neuroblastoma cell line (CHP100). Chromatography on Sepharose CL-4B identified two heparan sulphate proteoglycans in the medium (Kav 0.220 and 0.389), whereas in the cell lysate the major proteoglycan species were more heterogenous and of a smaller overall molecular size (Kav 0.407) than the medium-derived counterparts. Chromatography on Sepharose CL-6B of free heparan sulphate glycosaminoglycan chains showed that the majority of cell-layer-derived material heparan sulphate 2, Kav = 0.509) was smaller than medium heparan sulphates (heparan sulphate 1 and heparan sulphate 2, Kav 0.230 and 0.317). Analysis of the patterns of polymer sulphation by nitrous acid treatment, gel chromatography and high-voltage electrophoresis established that in each heparan sulphate fraction there was on average 1.1 sulphate residues per disaccharide with an N:O sulphate ratio of 1.1. Heparan sulphate in the medium had a high proportion of di-O-sulphated disaccharides in regions of the chain with repeat disaccharide sequences of structure GlcA-GlcNSO3, whereas cell-associated material was enriched in di-O-sulphated tetrasaccharides of alternating sequences GlcA-GlcNAc-GlcA-GlcNSO3. The identification of several populations of heparan sulphate proteoglycans differing in molecular size and glycosaminoglycan fine structure may reflect the functional diversity of this family of macromolecules in the nervous system.
dc.language.isoenen
dc.subject.meshCell Line
dc.subject.meshCentrifugation, Density Gradient
dc.subject.meshChondroitin Sulfate Proteoglycans
dc.subject.meshChromatography, Gel
dc.subject.meshGlucosamine
dc.subject.meshGlycosaminoglycans
dc.subject.meshHeparan Sulfate Proteoglycans
dc.subject.meshHeparitin Sulfate
dc.subject.meshHumans
dc.subject.meshNeuroblastoma
dc.subject.meshProteoglycans
dc.subject.meshSulfates
dc.subject.meshSulfur Radioisotopes
dc.subject.meshTritium
dc.titleHeterogeneity of cell-associated and secretory heparan sulphate proteoglycans produced by cultured human neuroblastoma cells.en
dc.typeArticleen
dc.contributor.departmentDepartment of Clinical Research, U.K.en
dc.identifier.journalBiochimica et Biophysica Actaen
html.description.abstractBiosynthetically radiolabelled heparan sulphate proteoglycans have been isolated from the growth medium and the cell lysate of a human neuroblastoma cell line (CHP100). Chromatography on Sepharose CL-4B identified two heparan sulphate proteoglycans in the medium (Kav 0.220 and 0.389), whereas in the cell lysate the major proteoglycan species were more heterogenous and of a smaller overall molecular size (Kav 0.407) than the medium-derived counterparts. Chromatography on Sepharose CL-6B of free heparan sulphate glycosaminoglycan chains showed that the majority of cell-layer-derived material heparan sulphate 2, Kav = 0.509) was smaller than medium heparan sulphates (heparan sulphate 1 and heparan sulphate 2, Kav 0.230 and 0.317). Analysis of the patterns of polymer sulphation by nitrous acid treatment, gel chromatography and high-voltage electrophoresis established that in each heparan sulphate fraction there was on average 1.1 sulphate residues per disaccharide with an N:O sulphate ratio of 1.1. Heparan sulphate in the medium had a high proportion of di-O-sulphated disaccharides in regions of the chain with repeat disaccharide sequences of structure GlcA-GlcNSO3, whereas cell-associated material was enriched in di-O-sulphated tetrasaccharides of alternating sequences GlcA-GlcNAc-GlcA-GlcNSO3. The identification of several populations of heparan sulphate proteoglycans differing in molecular size and glycosaminoglycan fine structure may reflect the functional diversity of this family of macromolecules in the nervous system.


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