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At least 19 recordsLinked to original sources
PubMed1986

Organization of glycosaminoglycan chains in a chondroitin sulfate-dermatan sulfate proteoglycan from bovine aorta.

A chondroitin sulfate-dermatan sulfate proteoglycan was isolated from bovine aorta intima by extraction of the tissue by 4 M guanidine hydrochloride. The proteoglycan was purified by CsCl isopycnic centrifugation followed by gel filtration and ion-exchange chromatography. The proteoglycan had 21.9% protein, 22.1% uronate, 21.4% hexosamine and 10.8% sulfate. Glycosaminoglycan chains obtained from the proteoglycan by beta-elimination were resolved by gel filtration into two fractions, one containing chondroitin 6-sulfate with an approximate molecular weight of 49 000 and the other containing chondroitin 4-sulfate and dermatan sulfate in a proportion of 2:1 with an approximate molecular weight of 37 000. Digestion of the proteoglycan by chondroitinase ABC or AC yielded a protein core with similar composition and behavior in gel filtration and SDS-polyacrylamide gel electrophoresis. An approximate molecular weight of 180 000 was estimated for the core protein. Dermatan sulfate chains with an approximate molecular weight of 10 000 were observed only in the digest of chondroitinase AC. Limited trypsin hydrolysis of the proteoglycan yielded three peptide fragments containing chondroitin 6-sulfate, chondroitin 4-sulfate and dermatan sulfate in varied proportions. A tentative structure for the proteoglycan was suggested.

Animals↗
PubMed1986

Immunocytochemical investigation on the distribution of small chondroitin sulfate-dermatan sulfate proteoglycan in the human.

Polyclonal antibodies against the core protein of the small chondroitin sulfate-dermatan sulfate proteoglycan from human skin fibroblast secretions were used, after affinity-purification, as a probe to study localization of crossreactive material in several human tissues by indirect immunocytochemistry. In contrast to skin, kidney, and the adventitial layer of aorta, positive staining of brain, liver, cartilage, and intimal and medial layers of aorta required pre-treatment of tissue sections with chondroitin ABC lyase. In all tissues investigated, antigenic material was present in the interstitial space. Filamentous structures were perpendicularly oriented towards basement membranes. In liver, specific staining was seen along the sinusoidal walls. Reticular fibers with or without focal condensations were seen in cerebral cortex and cerebellum. The results suggest a role of small chondroitin sulfate-dermatan sulfate proteoglycan in cell-matrix interactions.

Animals↗
PubMed1998

Highly sulfated dermatan sulfates from Ascidians. Structure versus anticoagulant activity of these glycosaminoglycans.

Dermatan sulfates with the same backbone structure [4-alpha-L-IdceA-1-->3-beta-D-GalNAc-1]n but with different patterns of sulfation substitutions have been isolated from the ascidian body. All the ascidian dermatan sulfates have a high content of 2-O-sulfated alpha-L-iduronic acid residues but differ in the pattern of sulfation of the N-acetyl-beta-D-galactosamine units. Styela plicata and Halocynthia pyriformis have 4-O-sulfated units, but in Ascidian nigra they are 6-O-sulfated. This collection of ascidian dermatan sulfates (together with native and oversulfated mammalian dermatan sulfate), where the extent and position of sulfate substitution have been fully characterized, were tested in anticoagulant assays. Dermatan sulfate from A. nigra has no discernible anticoagulant activity, which indicates that 4-O-sulfation of the N-acetyl-beta-D-galactosamine is essential for the anticoagulant activity of this glycosaminoglycan. In contrast dermatan sulfates from S. plicata and H. pyriformis are potent anticoagulants due to potentiation of thrombin inhibition by heparin cofactor II. These ascidian dermatan sulfates have approximately 10-fold and approximately 6-fold higher activity with heparin cofactor II than native and an oversulfated mammalian dermatan sulfate, respectively. They have no effect on thrombin or factor Xa inhibition by antithrombin. These naturally oversulfated ascidian dermatan sulfates are sulfated at selected sites required for interaction with heparin cofactor II and thus have specific and potent anticoagulant activity.

Acetylgalactosamine↗
PubMed1994

Tandem mass spectrometry for characterization of unsaturated disaccharides from chondroitin sulfate, dermatan sulfate and hyaluronan.

Fast atom bombardment tandem mass spectrometry has been used in the characterization of non-, mono-, di- and trisulfated disaccharides from chondroitin sulfate, dermatan sulfate and hyaluronan. The positional isomers of the sulfate group of mono- and disulfated disaccharides were distinguished from each other by both positive- and negative-ion fast atom bombardment tandem mass spectra, which gave sufficient information characteristic of the isomers. The anomeric isomers of nonsulfated disaccharides were characterized by the technique in the positive-ion mode. This fast atom bombardment collision induced dissociation mass spectrometry/mass spectrometry technique was also applied successfully to the characterization of trisulfated disaccharide.

Carbohydrate Conformation↗
PubMed1996

Synchronized order of appearance of hyaluronic acid (or acidic galactan) --> chondroitin C-6 sulfate --> chondroitin C-4/C-6 sulfate, heparan sulfate, dermatan sulfate --> heparin during morphogenesis, differentiation and development.

The synthesis of glycosaminoglycans and acidic polysaccharides during embryonic and fetal development in mammals and molluscs is briefly reviewed. A sequential order of appearance of each of the acidic polysaccharides was observed, coinciding with the major processes of the ontogeny. In mammals, hyaluronic acid is the first glycosaminoglycan synthesized at the beginning of morphogenesis. This glycosaminoglycan is then replaced by chondroitin 6-sulfate during the migration of the mesenchymal cells. Heparan sulfate, dermatan sulfate and chondroitin 4-sulfate are synthesized only during cell differentiation. The synthesis of heparin, on the other hand, is confined to mast cells in a few tissues and is a late event in the differentiation process. The same general pattern is also observed in molluscs except that hyaluronic acid is replaced by an acidic galactan in the morphogenetic process. The activity of the degrading enzymes responsible for the disappearance of hyaluronic acid, chondroitin sulfate and the acidic galactan in each phase of embryonic development is also reviewed.

Animals↗
PubMed1975

Studies on the chemistry of arterial wall, XVII. Metabolic characteristics of different types of chondroitin sulfate-dermatan sulfate hybrids in arterial tissue.

1) Chondroitin sulfate and dermatan sulfate of bovine arterial tissue exist as copolymers with a varying degree of hybridization between chondroitin and dermatan sulfates. A fraction rich in dermatan sulfate hybridized with 20% chondroitin sulfate (termed DS-rich hybrid) and a fraction rich in chondroitin sulfate containing 17% DS as copolymer constituent (CS-rich hybrid) can be isolated by the subfractionation of the arterial tissue CS-DS preparation. 2) When arterial tissue segments were preincubated with [14C]glucosamine, 95% of the radioactivity incorporated into the glycosaminoglycans was found to be present in the galactosamine moiety of all of the CS-DS subfractions, whereas the relative proportion of 14C radioactivity incorporated into the galactosamine and uronic acid components was 51:49 following preincubation with [14C]glucose. In both experiments the specific radioactivity of the DS-rich hybrids was twice as high as that of the CS-rich hybrids. 3) Enzymatic degradation of the hybrid CS-DS subfractions by chondroitin AC and ABC lyases revealed that the specific radioactivity of the CS and DS disaccharide units released from the DS-rich hybrids was twice as high as those isolated from the CS-rich hybrids, but within each hybrid fraction the galactosamine moieties of the CS and DS units and their glucuronic and iduronic acid components exhibited equal specific radioactivities. 4) The results strongly support the assumption that distinct compartments exist for the formation of hybrid CS-DS proteoglycans with different proportions of CS and DS.

Animals↗
PubMed1990

Isolation and some structure analyses of a copolymeric chondroitin sulfate-dermatan sulfate proteoglycan from post-burn, human hypertrophic scar.

A D-glucuronic acid rich, copolymeric chondroitin sulfate (CS)-dermatan sulfate (DS) proteoglycan (PG) from post-burn hypertrophic scar tissue (HSc) was obtained by DEAE-cellulose chromatography and differential ethanol fractionation, and further purified on a Sepharose CL-6B column. CS-DS-PG protein content was 14% (w/w). The amino-terminal amino acid sequence of the first ten residues was as follows: NH2-Asp-Glu-Ala-B-Gly-Ile-Gly-Pro-Glu-Val. This sequence is identical to that of human embryonic fibroblast cell (IMR-90) CS-DS-PG, as well as to human HSc-DS-PG. After chondroitinase ABC treatment, two peptides (Mr 22,000 and 16,000 daltons) were detected by sodium dodecyl sulfate-(polyacryl)amide gel electrophoresis (SDS-PAGE). ELISA analysis using rabbit antiserum raised against a synthetic peptide that contained 15 amino acids in the same sequence as the amino terminus of human fetal membrane PG showed significant reactivity with HSc CS-DS-PG. HSc CS-DS-PG had an apparent Mr of approximately 78,000 daltons, as determined by Sepharose CL-6B chromatography and SDS-PAGE. Alkaline borohydride treatment of CS-DS-PG liberated CS-DS glycosaminoglycan (GAG) chains having an Mr of 29,000 daltons. The conversion of xylose to xylitol indicated that the GAG chains are attached to the PG protein core at O-3 through a xylosyl-seryl linkage. CS-DS-PG also contained both N and O-linked oligosaccharides and did not aggregate with hyaluronic acid. These results, together with those reported previously, showed that HSc CS-DS-PG and DS-PG have the same A1-A15 amino acid sequence at the amino terminus but different protein cores. HSc CS-DS-PG was completely digested with chondroitinase AC and is, therefore, distinctly different from HSc DS-PG.

Aggrecans↗
PubMed1987

Binding of chondroitin sulfate, dermatan sulfate and fat-storing cell-derived proteoglycans to rat hepatocytes.

1. The interaction of isolated rat hepatocytes with exogenous 3H-labeled chondroitin-4-sulfate and dermatan sulfate and with biosynthetically 35S-labeled proteoglycans secreted by cultured rat liver fat-storing cells has been studied. 2. All ligands are bound by hepatocytes in a concentration-dependent manner. Scatchard-plot analysis of the data revealed the existence of high- and low-affinity binding modes. 3. The cell-bound exogenous [3H]glycosaminoglycans could be displaced by each unlabeled ligand and by heparin, whereas displacement of the endogenous material was less effective. 4. Binding of all ligands to hepatocytes increased with time. For the exogenous glycosaminoglycans the two- to threefold amount was retained at 37 degrees C as compared to 4 degrees C; it was markedly reduced by pretreatment of the cells with trypsin. 5. Degradation of the exogenous ligands could be detected neither for the cell-bound fraction nor for the free glycosaminoglycans in the culture medium. 6. The binding of the ligands to hepatocytes is viewed as a cell-matrix interaction. Its possible pathobiochemical relevance in liver fibrosis or neoplasia is discussed.

Adipose Tissue↗
PubMed1984

Heparan sulfate and dermatan sulfate inhibit the generation of thrombin activity in plasma by complementary pathways.

Heparan with a low affinity for antithrombin III has previously been demonstrated to inhibit thrombin generation in both normal plasma and plasma depleted of antithrombin III. In addition, standard heparin and heparin with a low affinity for antithrombin III have been demonstrated to have equivalent inhibitory actions on thrombin generation in plasma depleted of antithrombin III. These observations prompted the investigation of the effects of four normal vessel wall glycosaminoglycans (heparan sulfate, dermatan sulfate, chondroitin-4-sulfate, and chondroitin-6-sulfate) on the intrinsic pathway generation of thrombin and factor Xa and on the inactivation of thrombin and factor Xa in plasma. Heparan sulfate inhibited thrombin generation and accelerated the inactivation of added thrombin and factor Xa in normal plasma but not in antithrombin III-depleted plasma. In contrast, dermatan sulfate inhibited thrombin generation in both normal and antithrombin III-depleted plasma. In addition, heparan sulfate was an effective inhibitor of factor Xa generation, while dermatan sulfate was not. Neither chondroitin-4-sulfate nor chondroitin-6-sulfate inhibited the generation of thrombin or factor Xa nor did they accelerate the inactivation of factor Xa or thrombin by plasma. These results suggest that heparan sulfate acts primarily by potentiating antithrombin III, while dermatan sulfate acts by potentiating heparin cofactor II. The inhibition of thrombin generation by heparan sulfate and dermatan sulfate thus appears to occur by complementary pathways, both of which may contribute to the anticoagulation of blood in vivo.

Anticoagulants↗
PubMed1995

Fibrinogen inhibits the heparin cofactor II-mediated antithrombin activity of dermatan sulfate.

Dermatan sulfate is a naturally occurring antithrombotic glycosaminoglycan. The antithrombin activity of several dermatan sulfate preparations has been measured in whole human plasma and found to be -55% of that in purified systems. Kinetic studies under pseudo-first-order conditions indicated that the reduction in antithrombin activity of dermatan sulfate in plasma compared with that in buffer was due to noncompetitive inhibition with respect to dermatan sulfate. Analysis of the protein profile bound to immobilized dermatan sulphate showed that on a molar basis, histidine-rich glycoprotein and apolipoprotein E were the most abundant proteins specifically bound, together with significant amounts of fibrinogen and vitronectin. Addition of these proteins to the purified system showed that only fibrinogen inhibited the antithrombin activity of dermatan sulfate and that it did so in a concentration-dependent manner over the physiologic range of plasma fibrinogen levels. These results indicate that the anticoagulant activity of dermatan sulfate may be modulated in human plasma by fibrinogen.

Animals↗
PubMed1987

Ca2+-mediated association of human serum amyloid P component with heparan sulfate and dermatan sulfate.

The serum amyloid P component (SAP) is a precursor glycoprotein of amyloid P component found in all types of amyloid deposits. The binding of human SAP to heparan sulfate and dermatan sulfate was studied using Sepharose-immobilized SAP. The apparent dissociation constants of heparan sulfate and dermatan sulfate for immobilized-SAP were estimated to be approximately 2 X 10(-7) M in the presence of 2 mM CaCl2 at neutral pH and physiological ionic strength. Both the binding affinity of SAP for these glycosaminoglycans and the numbers of binding sites of SAP depended on calcium concentration. Cadmium partially substituted for calcium as an activator of glycosaminoglycan binding to SAP. No binding occurs in the absence of added metal, or in the presence of barium, copper, magnesium, manganese, and strontium. The calcium-dependent binding of [3H]heparan sulfate and [3H]dermatan sulfate to SAP was strongly inhibited by heparan sulfate, heparin, and dermatan sulfate. Chondroitin 6-sulfate was a moderate inhibitor, whereas hyaluronic acid, chondroitin 4-sulfate, and keratan sulfate were not potent inhibitors. The calcium-dependent binding of amyloid P component to heparan sulfate and/or dermatan sulfate may be a cause of the coexistence of the particular glycoprotein and these glycosaminoglycans in amyloid tissues.

Animals↗
PubMed1989

Plasma anticoagulant mechanisms of heparin, heparan sulfate, and dermatan sulfate.

The relationship between two anticoagulant actions of glycosaminoglycans (GAGs), namely the catalysis of thrombin inhibition (assessed by thrombin-antithrombin-III and thrombin-heparin-cofactor-II formation) and the inhibition of prothrombin activation, was explored by comparing the effects of heparin, heparan sulfate, and dermatan sulfate on the two reactions in plasma. Heparan sulfate and dermatan sulfate were also resulfated in vitro to yield products with sulfate/carboxylate ratios similar to those of heparin. Their effects on thrombin inhibition and the activation of prothrombin were also determined. The catalytic efficiency of the five GAGs on thrombin inhibition and their inhibitory effects on prothrombin activation decreased in the following order: heparin; resulfated dermatan sulfate; resulfated heparan sulfate; heparan sulfate = dermatan sulfate. These results suggest that the catalytic efficiency of a glycosaminoglycan on thrombin inhibition translates to its inhibitory effect on prothrombin activation, since catalysis of thrombin inhibition results in the inhibition of the thrombin-dependent positive feedback reactions of coagulation which facilitate prothrombinase formation.

Antithrombin III↗
PubMed1992

Distribution of chondroitin sulfate and dermatan sulfate in normal and inflamed human gingivae.

The effect of inflammation on the distribution of chondroitin sulfate and dermatan sulfate proteoglycans was assessed after normal and inflamed human gingivae were stained with monoclonal antibodies against these extracellular matrix macromolecules. The tissues were obtained following periodontal surgery and reacted with specific antibodies after pre-treatment with chondroitinase ACII or chondroitinase ABC, and staining was visualized by the immunoperoxidase technique. The results indicated that these two proteoglycans were present in both the 4-sulfated and 6-sulfated isomeric forms. While chondroitin sulfate appeared to be uniformly distributed throughout the connective tissue, dermatan sulfate showed greater intensity of staining in the areas immediately subjacent to the epithelium. Positive staining for chondroitin sulfate was noted in the intercellular spaces of the epithelium. In inflamed tissues, there was significant staining associated with 4-sulfated dermatan sulfate and chondroitin sulfate, but this had lost the structured pattern of staining noted in normal sections. The 6-sulfated isomeric forms were greatly reduced in inflamed tissues and tended to show a predilection to be localized within the perivascular tissues. In the inflamed tissues, there was intense staining for chondroitin sulfate associated with the infiltrating inflammatory cells. These findings corroborate earlier biochemical studies on normal and inflamed gingival tissues. The specific tissue localization of dermatan sulfate and chondroitin sulfate in tissues damaged by inflammation indicates that, as opposed to the large loss of collagenous material noted during inflammation, there is not a corresponding large loss of proteoglycan. Indeed, at specific inflammatory foci, the intensity of staining for these macromolecules may intensify.

Adult↗
PubMed1985

A high-performance liquid chromatography for constituent disaccharides of chondroitin sulfate and dermatan sulfate isomers.

An improved high-performance liquid chromatography for unsaturated disaccharides prepared from chondroitin sulfate and dermatan sulfate isomers was developed using an ion-exchange resin made from a sulfonized styrene-divinylbenzene copolymer. By this newly devised method, it was found that the retention times of representative unsaturated disaccharides are very unique and appear in the following order: unsaturated 6-sulfated, nonsulfated, and 4-sulfated disaccharides. The content of the individual unsaturated disaccharides could be measured at similar sensitivities with ultraviolet absorbance. Sensitive and unique retention times as well as good resolution were found for various unsaturated disulfated disaccharides. The new microassay method by HPLC can be used to determine chondroitin sulfate and dermatan sulfate isomers in amounts as small as 100 ng to 8 micrograms. The practicality of this method was verified by application to the separation and quantitation of chondroitin sulfate and dermatan sulfate isomers from human coronary arteries.

Adult↗