The copolymeric structure of pig skin dermatan sulphate. Isolation and characterization of <scp>l</scp>-idurono-sulphate-containing oligosaccharides from copolymeric chains

Fransson, Lars‐Âke; Cöster, L; Havsmark, Birgitta; Malmström, Anders; Sjöberg, Ingrid

doi:10.1042/bj1430379

Cited by 33 publications

(28 citation statements)

References 9 publications

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“…It should be added that approximately 10-15% of the repeating units in hyaluronidase-degraded dermatan sulphate were obtained in oligosaccharide form after chondroitinase-ABC digestion. On the basis of indirect evidence it was previously proposed that the chondroitinase-ABC-and periodate-insensitive oligosaccharides contained IdUA(-S04)-GalNAc units (Fransson et al, 1974b). The present results further suggest that these oligosaccharides also contain IdUA(-SO4.-GalNAc(-S04) and IdUA-GalNAc repeating units.…”

Section: Resultssupporting

confidence: 78%

“…GalNAc4(IdUA-GalNAc).-GlcUA-GalNAc I SO4 (Fransson et al, 1974b) This finding indicates that repeating units containing L-iduronic acid sulphate may be intercalated between D-glucuronic acid-and L-iduronic acidcontaining block regions. To investigate whether this was a common arrangement the following experiment was performed.…”

Section: Resultsmentioning

confidence: 96%

“…The enzymes chondroitinase-AC, chondroitinase-ABC and testicular hyaluronidase were the same preparations as described previously (Fransson & Malmstr6m, 1971;Fransson et al, 1974a). Both chondroitinase-AC and -ABC cleave linkages between N-acetylgalactosamine and D-glucuronic acid.…”

Section: Experimental Materialsmentioning

confidence: 99%

“…To study the distribution of L-iduronic acid sulphate residues, methods for a selective periodate oxidation of dermatan sulphate were developed (Fransson, 1974;Fransson & Carlstedt, 1974). Oxidation of unsubstituted L-iduronosyl residues at low pH values was followed by reduction-hydrolysis or alkaline elimination to yield oligosaccharides containing D-glucuronic acid or O-sulpho-L-iduronic acid as hexuronic acid components (Fransson et al, 1974a). Copolymeric oligosaccharides containing both D-glucuronic acid and O-sulpho-L-iduronic acid in the same chain were also demonstrated.…”

mentioning

confidence: 99%

“…Copolymeric oligosaccharides containing both D-glucuronic acid and O-sulpho-L-iduronic acid in the same chain were also demonstrated. These sequences were particularly prominent in polysaccharide fragments derived from peripheral portions of the original chain (Fransson et al, 1974b). Further analysis of these oligosaccharides indicated that the GlcUA-GalNAc units occupied the reducing terminal end in the following manner:…”

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confidence: 99%

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The co-polymeric structure of pig skin dermatan sulphate. Distribution of L-iduronic acid sulphate residues in co-polymeric chains

Cöster

Malmström

Sjöberg

et al. 1975

Biochemical Journal

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1. Pig skin dermatan sulphate was degraded by periodate oxidation followed by alkaline elimination or by chondroitinase-ABC to quantify irregular repeating units, i.e. those containing D-GlcUA (D-glucuronic acid) and L-IdUA-SO4 (sulphated iduronic acid). 2. Previous results of periodate oxidation (Fransson, 1974) indicated repeating sequences in pig skin dermatan sulphate containing, on average, 3D-GlcUA, 9 L-IdUA-SO4 or 28 L-IdUA units in addition to N-acetylgalactosamine sulphate. However, complete digestion with chondroitinase-ABC yielded, at the most, 3-4 disulphated disaccharides/ chain. Consequently, more than one-half of the L-IdUA-SO4 residues were present in monosulphated periods, i.e. IdUA-(SO4)-GalNAc. 3. To determine the location of L-IdUA-S04 residues along the copolymeric chain dermatan sulphate was digested with testicular hyaluronidase. (This enzyme cleaves GalNAc-GlcUA bonds within block regions containing D-GlcUA.) By NaB3H4 reduction GalNAc residues located in the reducing end of the fragments were converted into [3H]GalNAcOH (N-acetylgalactosaminitol). Finally, the radioactive product was fragmented by periodate oxidation followed by alkaline elimination. The bulk of the radioactivity was associated with periodate-resistant oligosaccharides indicating that clusters of GlcUA-GalNAc-SO4 periods are often adjacent to a varying number (n = 1-4) of L-IdUA-SO4-containing periods. 4. To study the distribution of L-IdUA-SO4-containing periods in relation to blocks of IdUA-GaINAc-SO4 periods different fractions of hyaluronidase-degraded dermatan sulphate were degraded separately. In all types of fragments (mol.wts. 1500-10000) L-IdUA-SO4-containing periods were demonstrated. In short fragments reducing terminal was found confirming that these sequences were joined to relatively long D-GlcUA-containing block sequences via GalNAc-6-SO4. Moreover, low-molecular-weight oligosaccharides composed of alternating sequences were encountered. An octasaccharide derived from the carbohydrate sequence -GalNAc ---GlcUA-GaINAc-IdUA-GaINAc-GlcUA-GalNAcIdUA-GalNAc---GlcUA-GalNAc (---indicates the position of cleavage by hyaluronidase) was identified.

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Section: Resultssupporting

confidence: 78%

Section: Resultsmentioning

confidence: 96%

Section: Experimental Materialsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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The co-polymeric structure of pig skin dermatan sulphate. Distribution of L-iduronic acid sulphate residues in co-polymeric chains

Cöster

Malmström

Sjöberg

et al. 1975

Biochemical Journal

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Carbohydrate‐Carbohydrate Interactions

Spillmann

Burger

Ernst

et al. 2000

Carbohydrates in Chemistry and Biology

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Cell recognition and adhesion are important events in the formation and maintenance of functional tissues. These processes must be selective and flexible in order to guarantee proper development as in embryogenesis, during the development of the nervous system, for continuous activity of the lymphoid system, but can also be misused by parasitic intruders or aberrant cells like tumor cells. How are glycans involved in these recognition and adhesion phenomena so important for all living organisms?Carbohydrates are the most ubiquitous and prominently exposed molecules on the surface of living cells. The combination of a few building blocks in a seemingly countless array of structures is a principle characteristic of carbohydrate chains that distinguishes carbohydrate sequences from all other biomolecules whether nucleic acids or peptides. Such, these chains offer simultaneously flexible, ordered and easily modulatable motives for cellular interactions. The specific arrangement of individual carbohydrate sequences on surfaces and within matrices creates yet another dimension of diversity: Well defined structures or patches of carbohydrate motives can be created within linear stretches of glycans and glycosaminoglycans (GAG), attached to core protein backbones or located on freely movable lipid anchors for interaction with other molecules [ 1, 21. Glycans are therefore predestined to serve as crucial molecules for recognition and attachment at the moment of cell encounter,Carbohydrates have been recognized as interaction sites in many different instances. Many of these processes are mediated by lectin-or lectin-like molecules that recognise specific carbohydrate motifs. Lymphocyte homing is a multistep process with increasing interaction strengths. A first rolling stage of circulating lymphocytes is dependent on recognition of glycan ligands by protein receptors, the selectins, on the endothelium as well as on the lymphocytes [2, 31. Neuronal development depends on reversible cell extensions and connections followed by disruption which requires the proper interaction with cells, extracellular matrix and solu- Carbohydrates in Chemistry

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Mammalian glycosaminoglycans and proteoglycans

Kennedy

White

1982

Brit. Poly. J.

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The copolymeric structure of pig skin dermatan sulphate. Isolation and characterization of l-idurono-sulphate-containing oligosaccharides from copolymeric chains

Cited by 33 publications

References 9 publications

The co-polymeric structure of pig skin dermatan sulphate. Distribution of L-iduronic acid sulphate residues in co-polymeric chains

The co-polymeric structure of pig skin dermatan sulphate. Distribution of L-iduronic acid sulphate residues in co-polymeric chains

Carbohydrate‐Carbohydrate Interactions

Mammalian glycosaminoglycans and proteoglycans

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