Structure of Pig Skin Dermatan Suflate

Fransson, Lars‐Âke; Malmström, Anders

doi:10.1111/j.1432-1033.1971.tb01259.x

Cited by 44 publications

(12 citation statements)

References 21 publications

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“…Thus, the low-charged preparation HS2 was obtained between 0.4 and 0.6 M NaCl and the high-charged HS6 between 1.2 and 2.1 M NaCl. The DS was obtained and characterized by methods described by Fransson and Malmström [1971] and by Fransson et al [1979]. Chemical data are summarized in Table I.…”

Section: Methods Materialsmentioning

confidence: 99%

Binding, internalization, and degradation of antiproliferative heparan sulfate by human embryonic lung fibroblasts

et al. 1997

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Binding, internalization, and degradation of 125I-labeled, antiproliferative, or nonantiproliferative heparan sulfate by human embryonic lung fibroblasts was investigated. Both L-iduronate-rich, antiproliferative heparan sulfate species as well as L-iduronate-poor, inactive ones were bound to trypsin-releasable, cell-surface sites. Both heparan sulfate types were bound with approximately the same affinity to one high-affinity site (Kd approximately 10(-8) M) and to one low-affinity site (Kd approximately 10(-6) M), respectively. Results of Hill-plot analysis suggested that the two sites are independent. Competition experiments with unlabeled glycosaminoglycans indicated that the binding sites had a selective specificity for sulfated, L-iduronate-rich heparan sulfate. Dermatan sulfate, which is also antiproliferative, was weakly bound to the cells. The antiproliferative effects of heparan and dermatan sulfate appeared to be additive. Hence, the two glycosaminoglycans probably exert their effect through different mechanisms. At concentrations above 5 micrograms/ml (approximately 10(-7) M), heparan sulfate was taken up by human embryonic lung fibroblasts, suggesting that the low-affinity site represents an endocytosis receptor. The antiproliferative effect of L-iduronate-rich heparan sulfate species was also exerted at the same concentrations. The antiproliferative species was taken up to a greater degree than the inactive one, suggesting a requirement for internalization. However, competition experiments with dextran sulfate suggested that both the high-affinity and the low-affinity sites are involved in mediating the antiproliferative effect. Structural analysis of the inactive and active heparan sulphate preparations indicated that although sulphated L-iduronate appears essential for antiproliferative activity, it is not absolutely required for binding to the cells. Degradation of internalized heparan sulfate was analyzed by polyacrylamide gel electrophoresis using a sensitive detection technique. The inactive species was partially degraded, whereas the antiproliferative one was only marginally affected.

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Section: Methods Materialsmentioning

confidence: 99%

Binding, internalization, and degradation of antiproliferative heparan sulfate by human embryonic lung fibroblasts

et al. 1997

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“…DS (iduronic acid content of 95%) was purified from porcine skin (known as DS-18) (Fransson and Malmström, 1971), and CS was purified from horse nasal septum (known as CS-4) (Rodén et al, 1972).…”

Section: Methodsmentioning

confidence: 99%

Biglycan and decorin induce morphological and cytoskeletal changes involving signalling by the small GTPases RhoA and Rac1 resulting in lung fibroblast migration

Tufvesson

Westergren‐Thorsson

2003

Journal of Cell Science

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Biglycan and decorin are small chondroitin/dermatan sulphate proteoglycans in the extracellular matrix of connective tissue that belong to the family of structurally related proteoglycans called small leucine-rich repeat proteins. We show for the first time that biglycan and decorin induce morphological and cytoskeletal changes in fibroblasts, resulting in an increase in migration. Biglycan changed the cell shape of fibroblasts with formation of long protruding filamentous processes. This was also seen for decorin but to a lesser extent. Using fluorescence staining of F-actin fibres it was possible to show that these long filamentous processes were supported by long thick bundles of actin, together with an induced formation of stress fibres after stimulation with biglycan and decorin. Moreover, a reorganisation of α-smooth muscle actin was clearly seen in these cultures. Decorin also stimulated α-smooth muscle actin expression in the cells. Using cDNA Atlas Arrays we were also able to show that the mRNA level of a number of the intracellular regulators and effectors involved in cell migration were increased. For example, the focal adhesion proteins paxillin and zyxin, and some of the small Rho GTPases such as RhoA, Rac1 and Cdc42 were upregulated. After treatment with biglycan or decorin, additional results showed an increased activation of RhoA (1.8- and 1.5-fold, respectively) and Rac1 (1.8- and 1.5-fold, respectively) after 15 minutes. These factors are known to be involved in fibroblast migration, and as expected a 1.3- to 1.6-fold increase in migration could be observed after stimulation with biglycan or decorin. This induced migration was caused by the core protein, as treatment with glycosaminoglycan chains alone did not have any effect. In summary, these data indicate that biglycan- and decorin-induced fibroblast cytoskeletal and signalling changes result in an increased cell migration, and demonstrate their potential role in the remodelling process.

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“…Enzymes and carbohydrates have been listed in the preceding paper [6]. Hyaluronidase-degraded dermatan sulfate from pig skin was the same preparation as described by Fransson [7].…”

Section: Methodsmentioning

confidence: 99%

“…The analytical methos for determination of hexosamine, uronic acid and sulfate were those used in the preceding paper [6].…”

Section: Methodsmentioning

confidence: 99%

Structure of Pig Skin Dermatan Sulfate

Malmström

Fransson

1971

European Journal of Biochemistry

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The presence of sulfated uronic acid residues in dermatan sulfate has been known for some time. I n view of the copolymeric nature of pig skin dermatan sulfate, it was of interest to see whether the extra sulfate groups were attached to iduronic acid or glucuronic acid residues.Hyaluronidase-degraded dermatan sulfate was fractionated on Dowex-1 to yield fractions of varying sulfate content. It was observed that the degree of sulfation was inversely proportional to the glucuronic acid content. Oversulfated dermatan sulfate was subsequently treated with chondroitinase-AC to yield a completely glucuronic acid-free polymeric product still bearing all the extra sulfate groups. More direct evidence for the presence of sulfated iduronic acid moieties was obtained by Smith degradation of oversulfated, chondroitinase-AC treated dermatan sulfate. A fast-moving component isolated by preparative electrophoresis had the molar ratio sulfate : hexosamine 1.8 : 1 and contained exclusively L-iduronic acid.The sulfate groups of acidic glycosaminoglycans are generally attached to the hexosamine moieties. However, sulfated uronic acid residues have also been demonstrated ; besides heparin, a number of galactosaminoglycans from various sources have been found to contain uronosyl-sulfate units (for references see [l]). So-called oversulfated dermatan sulfates have thus been isolated from skin of elasmobranches [Z] and urines of Hurler patients [3]. Furthermore, even dermatan sulfate preparations with equimolar proportions of sulfate and hexosamine contain disaccharide units bearing two sulfate residues ; unsaturated dissaccharides with sulfated uronic acid moieties were thus isolated from a chondroitinase digest of dermatan sulfate [l, 41. Although the configurational difference between iduronic and glucuronic acid is eliminated in the unsaturated disaccharides it was suggested that part of the sulfate residues would be located to glucuronic acid moieties [I].During studies on the copolymeric nature of pig skin dermatan sulfate it was observed that polysaccharide fragments reisolated after hyaluronidase degradation were significantly oversulfated [ 5 ] . Since the oligosaccharide fragments containing the bulk of the glucuronic acid residues of the polymer did not show an oversulfation [5] it seems reasonable to suggest that the extra sulfate groups are located to iduronic acid residues.Enzyme. Chondroitinase or chondroitin sulfate glycanohydrolase (EC 3.2.1.34).

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Structure of Pig Skin Dermatan Suflate

Cited by 44 publications

References 21 publications

Binding, internalization, and degradation of antiproliferative heparan sulfate by human embryonic lung fibroblasts

Binding, internalization, and degradation of antiproliferative heparan sulfate by human embryonic lung fibroblasts

Biglycan and decorin induce morphological and cytoskeletal changes involving signalling by the small GTPases RhoA and Rac1 resulting in lung fibroblast migration

Structure of Pig Skin Dermatan Sulfate

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