A new electrophoretic method for the separation of disaccharides obtained by digestion of chondroitin sulfates and dermatan sulfate with chondroitinases

1981 ◽  
Vol 110 (1) ◽  
pp. 39-42 ◽  
Author(s):  
Itaru Miyamoto ◽  
Hitoshi Watanabe ◽  
Sumi Nagase
Keyword(s):  
Dermatan Sulfate ◽  
Electrophoretic Method ◽  
Chondroitin Sulfates

Glycosaminoglycan biosynthesis in the isolated perfused rat lung

1984 ◽  
Vol 57 (6) ◽  
pp. 1648-1654 ◽  
Author(s):  
P. M. Sampson ◽  
R. B. Boyd ◽  
G. G. Pietra ◽  
A. P. Fishman
Keyword(s):  
Hyaluronic Acid ◽  
Heparan Sulfate ◽  
Dermatan Sulfate ◽  
Rat Lung ◽  
Electron Microscopic ◽  
Chondroitin Sulfates ◽  
Isolated Lung ◽  
Microscopic Studies

The suitability of an isolated lung, perfused under carefully monitored conditions, for the study of the biosynthesis of glycosaminoglycans was examined for the rat lung using either [35S]-sulfate or [6-3H]glucosamine. Metabolic and electron-microscopic studies after 3 h of perfusion showed that under the conditions of this study the isolated lung showed no anatomical or metabolic derangements. All glycosaminoglycans normally synthesized in the intact lung were identified. The predominant glycosaminoglycan was heparan sulfate (40% of total). Approximately 14% of the glucosamine incorporated into the glycosaminoglycans was found in hyaluronic acid. Less than 5% of either label was in heparin. The remainder of the synthesized glycosaminoglycans, with the exception of 10% which could not be identified, consisted of the chondroitin sulfates and dermatan sulfate. The relative proportions of the newly synthesized glycosaminoglycans, including the low amounts of heparin, are similar to those found in isolation of endogenous lung glycosaminoglycans. The isolated perfused rat lung appears to be a useful model for the study of glycosaminoglycan biosynthesis by the intact lung.

Resolution-enhanced 1H-n.m.r. spectra of dermatan sulfate and chondroitin sulfates: conformation of the uronic acid residues

1979 ◽  
Vol 68 (1) ◽  
pp. C3-C7 ◽  
Author(s):  
Giuseppe Gatti ◽  
Benito Casu ◽  
Giangiacomo Torri ◽  
John R. Vercellotti
Keyword(s):  
Uronic Acid ◽  
Dermatan Sulfate ◽  
Chondroitin Sulfates

scholarly journals Phagocytosis of gelatin-latex particles by a murine macrophage line is dependent on fibronectin and heparin.

1981 ◽  
Vol 90 (1) ◽  
pp. 32-39 ◽  
Author(s):  
L van de Water ◽  
S Schroeder ◽  
E B Crenshaw ◽  
R O Hynes
Keyword(s):  
Dermatan Sulfate ◽  
Keratan Sulfate ◽  
Reticuloendothelial System ◽  
Murine Macrophage ◽  
Temperature Dependent ◽  
Opsonic Activity ◽  
Latex Particles ◽  
Chondroitin Sulfates ◽  
Rapid Assays

It has been suggested that fibronectin plays a role in clearing particles from the circulation by promoting binding to phagocytes of the reticuloendothelial system. By use of a well-defined system to investigate the possible opsonic role of fibronectin, we have studied the uptake of gelatin-coated latex particles by a murine macrophage cell line (P388D1). Fibronectin promotes binding of gelatin-coated beads to these cells in both suspension and monolayer cultures. In both cases there is a requirement for heparin as a cofactor. Other glycosaminoglycans (chondroitin sulfates A and C, dermatan sulfate, and keratan sulfate) were inactive, whereas heparan sulfate was somewhat active. Proof that beads were actually endocytosed was obtained by electron microscopy, which showed beads internalized in membrane-bounded vesicles, and by immunofluorescence analyses, using antibodies to fibronectin to stain external beads. Two rapid assays for the opsonic activity of fibronectin were developed based on differential centrifugation of cell-associated beads and on the immunofluorescence procedure. Binding and endocytosis were time- and temperature-dependent and varied with the amount of gelatin on the beads and with the concentrations of fibronectin and heparin added, and could be inhibited by F(ab')2 antifibronectin. These studies provide a sound basis for a detailed analysis of the interaction of fibronectin with the cell surface and of its involvement in endocytosis.

Sulfated polysaccharides inhibit leukocyte rolling in rabbit mesentery venules

1991 ◽  
Vol 260 (5) ◽  
pp. H1667-H1673 ◽  
Author(s):  
K. Ley ◽  
M. Cerrito ◽  
K. E. Arfors
Keyword(s):  
Heparan Sulfate ◽  
Dextran Sulfate ◽  
Dermatan Sulfate ◽  
Leukocyte Adhesion ◽  
Keratan Sulfate ◽  
Mean Value ◽  
Sulfated Polysaccharides ◽  
Leukocyte Rolling ◽  
Chondroitin Sulfates ◽  
Wide Range

Before firm adhesion, leukocytes roll slowly along the walls of small venules at velocities ranging from 0.7 to 36% of mean blood flow velocity. To investigate the nature of the adhesive process underlying leukocyte rolling, synthetic (dextran sulfate) and naturally occurring sulfated polysaccharides (heparin, chondroitin sulfates, keratan sulfate, and heparan sulfate) were infused via glass micropipettes into the lumen of small venules (20–60 microns diam) of the rabbit mesentery. Leukocyte rolling was observed and quantified using both transmitted light and incident fluorescence intravital microscopy. Rolling leukocytes accounted for 27–80% of total leukocyte flux, exhibiting a wide range of individual velocities (0.01–0.84 mm/s) with a mean value of 4% of centerline velocity. Dextran sulfate (Mr 500,000) inhibited leukocyte rolling very effectively [half-effective concentration (ED50) approximately 10 micrograms/ml] and was able to almost completely abolish rolling at 500 micrograms/ml. Heparin (ED50 approximately 50 micrograms/ml), chondroitin 6-sulfate C (ED50 approximately 500 micrograms/ml), and heparan sulfate (ED50 approximately 5 mg/ml) also reduced leukocyte rolling. At 5 mg/ml, chondroitin 4-sulfate B (dermatan sulfate) was marginally effective, but chondroitin 4-sulfate A and keratan sulfate were ineffective. The present data suggest that an adhesion receptor-ligand system distinct from the leukocyte integrins may be underlying transient leukocyte adhesion (rolling). Endothelial glycoproteins or proteoglycans containing sulfated side chains may be involved in mediating this adhesive process.

scholarly journals Systemic Glycosaminoglycan Clearance by HARE/Stabilin-2 Activates Intracellular Signaling

Cells ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 2366
Author(s):  
Paul H. Weigel
Keyword(s):  
Intracellular Signaling ◽  
Dermatan Sulfate ◽  
Specific Binding ◽  
Target Surface ◽  
Cell Types ◽  
Scavenger Receptors ◽  
Extracellular Signal Regulated Kinase ◽  
Chondroitin Sulfates ◽  
Extracellular Signal ◽  
Receptor Purification

Scavenger receptors perform essential functions, critical to maintaining mammalian physiologic homeostasis by continuously clearing vast numbers of biomolecules from blood, interstitial fluid and lymph. Stabilin-2 (Stab2) and the Hyaluronic Acid Receptor for Endocytosis (HARE), a proteolytic isoform of Stab2, are important scavenger receptors responsible for the specific binding and internalization (leading to degradation) of 22 discrete molecules, macromolecular complexes and cell types. One-third of these ligands are glycosaminoglycans (GAGs). Full-length Stab2, but not HARE, mediates efficient phagocytosis of apoptotic cells and bacteria via binding to target surface ligands. HARE, the C-terminal half of Stab2, mediates endocytosis of all the known soluble ligands. HA was the first ligand identified, in 1981, prior to receptor purification or cloning. Seven other GAG ligands were subsequently identified: heparin, dermatan sulfate, chondroitin and chondroitin sulfates A, C, D and E. Synthetic dextran sulfate is also a GAG mimic and ligand. HARE signaling during HA endocytosis was first discovered in 2008, and we now know that activation of HARE/Stab2 signaling is stimulated by receptor-mediated endocytosis or phagocytosis of many, but not all, of its ligands. This review focuses on the HARE-mediated GAG activation of intracellular signaling, particularly the Extracellular Signal-Regulated Kinase 1/2 pathway.

The effect of glycosaminoglycans with acetaldehyde on the activation of prothrombin

2005 ◽  
Vol 83 (5) ◽  
pp. 431-438 ◽  
Author(s):  
Arthur S Brecher ◽  
Mohammed T Adamu
Keyword(s):  
Dermatan Sulfate ◽  
Anticoagulant Activity ◽  
Statistical Significance ◽  
Coagulation Factors ◽  
Additive Effect ◽  
Anticoagulant Effect ◽  
Ethanol Metabolism ◽  
Chondroitin Sulfates ◽  
Factor Ii ◽  
Aptt Reagent

Heparin17–19k, (25, 50, and 100 ng), heparin6k(50 and 100 ng), heparin3k(50, 100, and 200 µg), chondroitin sulfates B (dermatan sulfate) (0.25, 0.5, and 1.0 µg), C (1 and 10 µg), and A (1 and 10 µg) each prolong the activated partial thromboplastin time (APTT) when preincubated with prothrombin to a greater extent than when preincubated with Factor II-deficient plasma prior to their mixing and subsequent additions of APTT reagent and Ca2+. In all cases statistical significance (p ≤ 0.05) was observed except with the 2 lower levels of heparin3k. These results suggest that the glycosaminoglycans (GAGs) may exert a direct effect upon prothrombin (FII) in their anticoagulant activity. Pre mix tures of [(FII/25 ng H17–19k) + 447 mmol acetaldehyde (AcH)/L] as well as [(AcH/H) + FII] and [(FII/AcH) + H] each exert a synergistic anticoagulant effect upon APTT. At low AcH concentrations (44.7 mmol/L), neither a synergistic nor an additive effect is seen. H6kand H3k, on premixing with 447 mmol AcH/L, exhibit an additive effect on APTT prolongation but no synergism. Similarly, premixtures of CSB/447 mmol AcH/L/FII show a greater anticoagulant effect than do [(CSB/AcH) + FII] or [(FII/AcH) + CSB] premixtures. CSC–AcH and CSA–AcH patterns are analogous to those of CSB (DS). These data suggest the possibility that AcH, the primary product of ethanol metabolism, may serve as a crosslinking adduct with proteins, in this case, prothrombin, as well as GAGs. Thus ternary complexes between the zymogen form of coagulation factors, GAGs, and AcH are possible, further influencing coagulopathy.Key words: prothrombin, alcoholism, acetaldehyde, glycosaminoglycans, heparins, chondroitin sulfates.

Aortic glycosaminoglycans in atheroma and alloxan diabetes

1968 ◽  
Vol 46 (3) ◽  
pp. 249-260 ◽  
Author(s):  
Tokuro Ichida ◽  
Norman Kalant
Keyword(s):  
Hyaluronic Acid ◽  
Sialic Acid ◽  
Lipid Accumulation ◽  
Dermatan Sulfate ◽  
Surrounding Tissue ◽  
High Cholesterol Diet ◽  
High Cholesterol ◽  
High Fat ◽  
Fractional Rate ◽  
Chondroitin Sulfates

(1) Rabbits and rats were fed a high-fat, high-cholesterol diet to produce lipid deposition in the wall of the aorta. The intima and inner media were examined for their content of lipids, protein-bound carbohydrates, and individual glycosaminoglycans. In addition, the rate of uptake of 35S from sulfate into the sulfated glycosaminoglycans was measured in some animals.(2) In the rat, lipid accumulation was minimal; there were increases in the protein-bound hexosamine and sialic acid and decreases in all the glycosaminoglycans (hyaluronic acid, heparan sulfate, chondroitin-4-sulfate, chondroitin-6-sulfate, and dermatan sulfate).(3) In the rabbit, lipid accumulation was marked in the normal appearing tissue and still greater in the "fatty streaks". There were associated increases in protein-bound hexosamine and hexose and, in the fatty streaks, of sialic acid also. The concentrations of all sulfated glycosaminoglycans were higher in the fatty streaks than in the surrounding tissue.(4) In the rat, the rate of synthesis of chondroitin sulfates, as reflected in sulfate-35S incorporation, was not increased, but the turnover of chondroitin sulfates as reflected in the fractional rate of 35S incorporation was increased; this is taken as evidence that the fall in concentration was due to an increase in the rate of removal. In the rabbit, both synthesis and turnover of chondroitin sulfates were greatly increased in the fatty streaks; the change in synthesis was greater and led to the increase in the concentrations of these substances.(5) The concentration of hyaluronic acid was increased in the aortae of alloxan diabetic animals. Sulfate incorporation was reduced, indicating decreased synthesis of sulfated glycosaminoglycans. Despite this, the aortae of diabetic animals had virtually the same composition (except for hyaluronic acid) as those of non-diabetics given the same diet.

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