Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.6.4 (chondroitinase)
2,039 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Isolated rabbit glomeruli were incubated in vitro with 35SO4 in order to analyze the proteoglycans synthesized. Proteoglycans extracted with 4 M guanidine HCl from whole isolated glomeruli and from purified glomerular basement membrane (GBM) were analyzed by gel filtration chromatography. Two types of sulfated proteoglycans were found to be synthesized by rabbit glomeruli and these contained either heparan sulfate or chondroitin/dermatan sulfate glycosaminoglycan chains. These glycosaminoglycans were characterized by their sensitivity to selective degradation by nitrous acid or chondroitinase ABC, respectively. The major proteoglycan extracted from the whole glomeruli was a chondroitin/dermatan sulfate species (75%), while purified GBM contained mostly heparan sulfate (70%). The glycosaminoglycan chains were estimated to be about 12,000 molecular weight which is consistent with previous estimates for similar molecules extracted from the rat GBM.
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PMID:Biosynthesis of proteoglycans by isolated rabbit glomeruli. 662 17

A glycopeptide fraction containing glucuronic acid as a component sugar was extracted and purified from squid cartilage to give a single band migrating much slower than hyaluronic acid in cellulose acetate electrophoresis. The molecular weight of the glycopeptide was fairly large since its Kav value in Sephadex G-200 chromatography was 0.18; however, it was soluble in 66% ethanol. This glycopeptide contained glucuronic acid, glucosamine, galactosamine, galactose, and fucose. The total amino acid content was 1.87 mumol of amino acid per mg of the glycopeptide. Threonine, serine and proline represented 80% of the amino acids. Digestion with chondroitinase ABC or reaction with nitrous acid did not result in degradation of the glycopeptide; however, it was completely degraded by reaction with 0.5 M KOH at 37 degrees C. Two hexasaccharides were separated from the alkaline degradation products, and they both contained glucuronic acid, fucose, galactosamine, and reducing terminal glucosamine in the molar ratio, 2:1:2:1. These results indicated that the glycopeptide contains glucuronic acid-containing sugar chains that are distinct from any known glycosaminoglycan.
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PMID:Glucuronic acid-containing glycopeptide from squid cartilage. 662 77

Platelet factor 4, a unique peptide released during platelet aggregation, can bind to natural sulfated glycosaminoglycans from human renal cortex. The glycosaminoglycan isolate contained components sensitive to hyaluronidase, chondroitinase ABC and nitrous acid. Binding was demonstrated by the change in electrophoretic mobility of platelet factor 4 applied in combination with glycosaminoglycan compared to either applied alone. This effect, which occurred at physiologic pH but not at acidic pH or with high ionic strength, was preserved in samples subjected to prior hyaluronidase and chondroitinase digestion. Further demonstration that platelet factor 4 can interact with heparan sulfate anionic sites in the glomerular microvascular matrix was obtained by incubating radiolabeled platelet factor 4 with isolated rat glomeruli, and with purified human and rat glomerular basement membrane, followed by displacement with heparin. Total binding and heparin-released binding were decreased in glomerular basement membrane prepared from diabetic patients and from rats with streptozotocin-diabetes compared to control samples. These findings implicate platelet factor 4 in the pathogenesis of the altered capillary integrity associated with diabetes, and provide novel evidence that heparan sulfate anionic sites in glomerular basement membrane are diminished in human and experimental diabetes.
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PMID:Platelet factor 4 binding to glomerular microvascular matrix. 669 9

Ruthenium red and toluidine blue O precipitates were described associated with lathyritic elastic fibers in aortas of chickens treated with beta-aminopropionitrile fumarate (I. Pasquali-Ronchetti, C. Fornieri, I. Castellani, G. M. Bressan, and D. Volpin (1981). Alterations of the connective tissue components induced by beta-aminopropionitrile. Exp. Mol. Pathol. 35, 42-56). In this report evidence is given that these precipitates reveal the presence of proteoglycans, as they are completely removed by 5 M guanidine-HCl incubation and by specific enzymatic digestions. In particular, proteoglycans associated with the poorly cross-linked lathyritic elastin can be removed by testicular hyaluronidase, chondroitinase ABC, heparitinase, and nitrous acid treatments, whereas they are rather resistant to streptococcal hyaluronidase and chondroitinase AC. On the contrary, proteoglycans of the matrix or associated with collagen fibers are particularly sensitive to these latter enzymatic treatments. The conclusion is reached that glycosaminoglycans associated with beta-aminopropionitrile-induced lathyritic elastin (i) are different from those of the matrix or associated with collagen, and (ii) include mainly dermatan and heparan sulfates.
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PMID:Elastin fiber-associated glycosaminoglycans in beta-aminopropionitrile-induced lathyrism. 670 93

Arterial basement membrane-like material was prepared by a sonication-differential centrifugation technique from cultures of rabbit aortic myomedial cells after metabolic labelling with [35S]sulphate and [3H]glucosamine. Labelled glycosaminoglycans were obtained from isolated basement membrane-like material by proteinase digestion and gel filtration. Glycosaminoglycans were identified by a combination of Sephadex G-50 chromatography and sequential degradation with nitrous acid, Streptomyces hyaluronidase, testicular hyaluronidase and chondroitinase ABC. The data showed that heparan sulphate and chondroitin sulphate were the predominant glycosaminoglycans of myomedial basement membrane-like material. Heparan sulphate accounted for about 55% of [3H]glucosamine-labelled glycosaminoglycans. In addition small amounts of hyaluronic acid was present. Only trace amounts of dermatan sulphate was found. The glycosaminoglycans were analysed by DEAE-cellulose chromatography. Two major peaks were found in the chromatogram consistent with the predominance of heparan sulphate and chondroitin sulphate.
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PMID:Glycosaminoglycans of arterial basement membrane-like material from cultured rabbit aortic myomedial cells. 671 91

The effect of sodium butyrate on the cellular glycosaminoglycans of cultured mastocytoma p-815-4 cells was investigated using enzymic digestion, electrophoresis, nitrous acid degradation, and sequential partition fractionation. The average cellular glycosaminoglycan content of mastocytoma p-815-4 cells grown in the presence of 2 mM sodium butyrate was ten times as much as that of the control p-815-4 cells. Approximately 90% of the glycosaminoglycans isolated from the control cells and 70% from the butyrate-treated cells were found to be chondroitin 4-sulfate by enzymic digestion. The remainders were chondroitinase ABC-resistant. Hyaluronic acid and dermatan sulfate were not detected in either control cells or butyrate-treated cells. The chondroitinase ABC-resistant fraction of glycosaminoglycans from butyrate-treated cells showed a molar ratio of sulfate to uronic acid of more than 2.0, and provided some physicochemical properties characteristic to reference bovine lung heparin.
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PMID:Changes in the cellular glycosaminoglycans of cultured mastocytoma cells induced by sodium butyrate. 676 27

Glycosaminoglycans in urine from patients representing the major different mucopolysaccharidoses were separated and measured by use of a procedure that requires only 2 mL of urine. The compounds were resolved by two-dimensional electrophoresis on cellulose acetate plates and made visible by staining with Alcian Blue. They were identified by co-migration with standard glycosaminoglycans, by digestion with specific glycosidases, and by specific degradation with HNO2. They were quantitated by comparing the absorbance of eluates of the stained spots to appropriate standard curves for each glycosaminoglycan. This study revealed additional findings. About half of the patients excreted small amounts of heparin. Further, the keratan sulfate in samples from Morquio's disease patients migrated differently from authentic keratan sulfate unless digested with chondroitinase ABC. Our results for these diseases are in harmony with earlier reports.
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PMID:Direct quantitation of glycosaminoglycans in 2 mL of urine from patients with mucopolysaccharidoses. 677 34

Kidneys were perfused with [35S]sulfate at 4 h in vitro to radiolabel sulfated proteoglycans. Glomeruli were isolated from the labeled kidneys, and purified fractions of glomerular basement membrane (GBM) were prepared therefrom. Proteoglycans were extracted from GBM fractions by use of 4 M guanidine-HCl at 4 degrees C in the presence of protease inhibitors. The efficiency of extraction was approximately 55% based on 35S radioactivity. The extracted proteoglycans were characterized by gel-filtration chromatography (before and after degradative treatments) and by their behavior in dissociative CsCl gradients. A single peak of proteoglycans with an Mr of 130,000 (based on cartilage proteoglycan standards) was obtained on Sepharose CL-4B or CL-6B. Approximately 85% of the total proteoglycans were susceptible to nitrous acid oxidation (which degrades heparan sulfates), and approximately 15% were susceptible to digestion with chondroitinase ABC (degrades chondroitin-4 and -6 sulfates and dermatan sulfate). The released glycosaminoglycan (GAG) chains had an Mr of approximately 26,000. Density gradient centrifugation resulted in the partial separation of the extracted proteoglycans into two types with different densities: a heparan sulfate proteoglycan that was enriched in the heavier fraction (p greater than 1.43 g/ml), and a chondroitin sulfate proteoglycan that was concentrated in the lighter fractions (p less than 1.41). The results indicate that two types of proteoglycans are synthesized and incorporated into the GBM that are similar in size and consist of four to five GAG chains (based on cartilage proteoglycan standards). The chromatographic behavior of the extracted proteoglycans and the derived GAG, together with the fact that the two types of proteoglycans can be partially separated into the density gradient, suggest that the heparan sulfate and chondroitin sulfate(s) are located on different core proteins.
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PMID:Partial characterization of newly synthesized proteoglycans isolated from the glomerular basement membrane. 679 99

Colon wall from pig, stripped of most of the mucosal layer to leave material largely composed of muscle, basement membrane, and extracellular matrix, was subjected to procedures for isolation of glycosaminoglycans. A total ethanol precipitate from a papain digest was fractionated by selective ethanol precipitation in the presence of Ca2+. Glycosaminoglycan fractions, freed proteolytically from a high molecular weight glycoprotein component, were further purified by Sepharose CL-6B gel-filtration or DE-52 anion-exchange chromatography. Glycosaminoglycans were identified by chemical composition, 13C-NMR spectroscopy and response to chondroitinase and nitrous acid degradations. The content of glycosaminoglycan in the tissue is low (0.05% dry weight) being comprised of dermatan sulphate (38%), heparin (34%), heparan sulphate (18%) and chondroitin sulphates (10%) as a percentage of total glycosaminoglycan content. Hyaluronic acid and keratan sulphate have not been detected. The composition is generally typical of a high muscle content tissue.
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PMID:The glycosaminoglycans of pig colonic wall connective tissue. 684 74

Monocytes isolated from human blood were maintained in vitro on plastic culture dishes. After 3-4 days, adherent cells displayed morphological changes previously attributed to differentiation of the cells into histiocytes. 35S-labelled glycosaminoglycans were isolated after incubation of the cells with inorganic [35S]sulphate. Polysaccharide recovered from the culture medium after labelling from day 0 to day 2 or from day 5 to day 7 in vitro was approximately 90% galactosaminoglycan (resistant to deamination by HNO2), irrespective of labelling period. Whereas day-0-2 material was extensively degraded to disaccharide on incubation with the bacterial eliminase chondroitinase AC, a significant portion, about 30%, of the day-5-7 material resisted degradation under the same conditions. The resistant portion was readily depolymerized by treatment with chondroitinase ABC and may be dermatan sulphate. Paper electrophoresis and paper chromatography of the disaccharides obtained by eliminase digestion identified the day-0-2 labelled galactosaminoglycan as chondroitin 4-sulphate. In contrast, the corresponding day-5-7 material yielded approximately 20% disulphated disaccharide, both on digestion with chondroitinase AC and on subsequent enzymic degradation of the chondroitinase AC-resistant fraction. Further treatment of the disulphated disaccharide with chondro-4-sulphatase and chondro-6-sulphatase indicated that both sulphate groups were located on the N-acetylgalactosamine residue. In accordance with these findings, the day-5-7 polysaccharide showed a higher negative charge density than the day-0-2 material on ion-exchange chromatography. It is concluded that the novel properties acquired by the monocyte during prolonged culturing on plastic include the ability to synthesize glycosaminoglycan(s) containing 4,6-disulphated N-acetylgalactosamine units.
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PMID:Changes in glycosaminoglycan biosynthesis during differentiation in vitro of human monocytes. 687 Aug 1


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