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Query: UMLS:C1852044 (HS3)
 171 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ability of fibroblast heparan sulphate to aggregate was examined by affinity chromatography on agarose gels substituted with heparan sulphate variants from beef-lung tissue (designated HS2-A, HS3-A, and HS4-A) having different tendencies for association. Fibroblast heparan sulphate bound only to HS4-A agarose. The cell-derived material was subdivided into low-, medium-, and high-affinity species by affinity chromatography on HS4-A-agarose. High-affinity variants contained a larger proportion of chains of high molecular weight. Degradation of heparan sulphate by selective periodate-oxidation of glucuronate in regions rich in 2-acetamido-2-deoxyglucose followed by scission in alkali produced fragments comprising the highly irregular, iduronate-rich and N-sulphate-rich domains. The latter were slightly larger in the high-affinity form. By re-oxidation of the irregular domains, the location of glucuronate residues was identified. The degradation pattern, i.e., the distribution of iduronate-containing repeats, was markedly similar in the high-affinity variant and in the HS4-A chains that were used as affinity ligands. It is suggested that the strength and specificity of heparan sulphate self-association is dependent on complementary and co-operative associations between a number of contact zones.
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PMID:Chemical features of aggregatable heparan sulphates from human-lung fibroblasts. 621 7

1. Heparan sulphates from normal 3T3 fibroblasts are association-prone as indicated by their affinity for agarose gels substituted with cognate heparan sulphate species. Heparan sulphates from SV40-transformed or polyoma-virus-transformed cells have no affinity for the same gels. 2. Heparan sulphates from the medium, the pericellular and intracellular pools of normal, SV40-transformed and polyoma-transformed 3T3 cells were separated into four subfractions (HS1-HS4) by ion-exchange chromatography. In general, HS1-HS3 were found in cell-derived heparan sulphates, whereas HS3-HS4 were present in the medium. The heparan sulphates from transformed cells were more heterogeneous and of lower charge density than those from the normal counterpart. 3. Degradations via periodate oxidation/alkaline elimination yielded the oligomers glucosamine-(hexuronate-glucosamine)(n)-R with n=1-5 and a large proportion of N-sulphate groups. There was a large contribution of fragments n=4-5 from heparan sulphates of normal cells. These fragments were less common in low-sulphated heparan sulphates of transformed cells. In the case of medium-drived heparan sulphates all species had a low content of fragments n=4-5. 4. The size distribution of (glucuronate-N-acetylglucosamine)(n) regions was assessed after deaminative cleavage. It was broad and ranged from n=1-10 for all heparan sulphate species. In the case of medium-derived heparan sulphates there were distinct differences between normal and transformed cells. In the latter chains the N-acetyl-rich segments were both shorter and longer than in the normal case. The shape of the disaccharide peak was consistent with a lower content of O-sulphate in the heparan sulphates from transformed cells. 5. It was concluded that heparan sulphates from medium or transformed cells exhibit the greatest structural deviation from the normal case. The finding of lower proportions of extended, iduronate/glucuronate-bearing, N-sulphate-rich segments in heparan sulphates of transformed cells was particularly interesting in view of the fact that these elements have been associated with ability to self-interact.
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PMID:Co-polymeric glycosaminoglycans in transformed cells. Transformation-dependent changes in the co-polymeric structure of heparan sulphate. 628 59

We have developed an affinity chromatography procedure which measures binding of heparan sulfate species to agarose gels substituted with different heparan sulfates. Three major subfractions of bovine lung heparan sulfate (HS2, HS3, and HS4) which differ in sulfate content and hexuronate composition have been used. Association-prone variants of these species (HS2-A, HS3-A, and HS4-A) were prepared by gel chromatography. Free heparan sulfate chains were applied to columns of various heparan sulfate-agaroses which were eluted with a linear guanidine gradient and binding was assessed by measuring the hexuronate content of the effluent. Associating heparan sulfate of a particular subfraction was chiefly bound to gels that were substituted with chains of the same kind, i.e. HS2-A to HS2-A-agarose, HS3-A and HS4-A to HS3-A-agarose, and HS4-A to HS4-A-agarose. N-Desulfation and N-acetylation of HS2-A markedly reduced binding to HS2-A-agarose and periodate oxidation of glucuronate in HS3-A completely abolished binding to HS3-A-agarose. Partially oxidized HS2-A was separated into bound and unbound material by affinity chromatography on HS2-A-agarose. Gel chromatography of these fractions indicated that unbound chains were significantly smaller than bound ones. It is concluded that association between heparan sulfate chains may be quite specific and that the strength of binding is dependent on co-operative interactions between a number of contact zones. The latter may correspond to the N-sulfated and iduronate- and glucuronate-containing segments.
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PMID:Self-association of heparan sulfate. Demonstration of binding by affinity chromatography of free chains on heparan sulfate-substituted agarose gels. 645 8