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)

35S- as well as 3H-labeled glycosaminoglycans (GAG) produced by cultivated epithelium and fibroblasts of the rabbit cornea were treated with testicular hyaluronidase, leech hyaluronidase and chondroitinase-ABC or -AC. The fractionation-patterns of enzyme-treated GAG were compared with blanks not exposed to enzymes. The epithelial GAG revealed to be generally more resistant to the enzymatic degradation than the GAG synthesized by the fibroblasts, but--depending on the enzyme--in the GAG of both cell types the same fractions were attacked. The decline of the radioactivity in the fractions of enzyme-treated GAG allows the conclusions that both cell types produce relatively small amount of keratan sulfate but mainly chondroitin sulfates with a different degree of sulfation. In addition GAG, not present in the normal cornea, are synthesized: hyaluronic acid chiefly by fibroblasts and probably dermatan sulfate. The possible role of the fibroblastic and epithelial GAG in corneal wound repair is discussed.
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PMID:Biosynthesis of glycosaminoglycans by mammalian corneal epithelium and fibroblasts in vitro. II. Approach to specify the GAG from the two cell types. 12 25

The acidic glycosaminoglycans (AGAG) in normal human kidneys were fractionated on Dowex 1-X2 columns and analysed by electrophoretic separation in three buffers on cellulose acetate membranes and gel filtration on Sephadex G-100 columns, before and after digestion with chondroitinases and streptomyces hyaluronidase. Thin-layer chromatography was also performed to separate glucosamine from galactosamine moieties. Enzymatic digestion combined with electrophoretic characterization indicated that heparan sulfates exist as the main AGAG which accounted for two-fifths of the total AGAG. Hyaluronic acid and dermatan sulfates accounted for one-fourth and one-sixth of the total kidney AGAG, respectively. Chondroitin sulfate isomers (4-sulfate and 6-sulfate) consisted of the residual one-sixth of the total AGAG. An oversulfated chondroitin sulfate was detected in a small amount by demonstration of the unsaturated disulfated disaccharide after digestion with chondroitinase-ABC but not with chondroitinase-AC.
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PMID:Acidic glycosaminoglycans in human kidney tissue. 12 23

Chondroitin sulfate fractions were isolated from different animal cartilages, including whale, cattle, sheep, ray and shark, by Dowex 1 chromatography followed by ethanol fractionation. Although each preparation showed a single spot when electrophoresed on cellulose acetate, both 4- and 6-sulfated disaccharides were present in chondroitinase digests of each. In particular, the main fraction of bovine tracheal chondroitin sulfate (SO4/Ga1N = 1) gave both the disaccharides in nearly equal amounts, and its IR spectrum showed absorption bands at 820 and 850 cm-1. This fraction yielded three types of tetrasaccharides after digestion with testicular hyaluronidase. Structural studies on these tetrasaccharides, using P. vulgaris chondro-4-sulfatase followed by chondroitinase, showed that one of them is a hybrid consisting of the 4- and 6-sulfated residues. In the light of these facts, a nomenclature for chondroitin sulfates is discussed.
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PMID:Microheterogeneity of chondroitin sulfates from various cartilages. 12 31

Uterine slices obtained from the estrogen-treated rabbits were digested with pronase. Glycosaminoglycans and acidic glycopeptides were then isolated by Dowex 1 column chromatography and preparative electrophoresis on cellulose acetate membrane (Separax), in succession. Each subfraction thus obtained was identified by the mobility on Separax electrophoresis and the digestibility with mucopolysaccharidases (Streptomyces hyaluronidase, testicular hyaluronidase, chondroitinase AC, chondroitinase ABC and heparinase). The resulting data showed that each complex saccharide (hyaluronic acid, heparan sulfate, chondroitin sulfate A, chondroitin sulfate C, dermatan sulfate, sulfated glycopeptide and sialoglycopeptide) was separated into 2-5 fractions, indicating charge and/or molecular heterogeneity of each complex saccharide.
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PMID:Glycosaminoglycans and acidic glycoproteins in rabbit uterus under estrogenic conditions. 12

7 clinically uninvolved as well as 8 involved (6 moderately, 2 markedly) back or forearm skin specimens from 12 patients with systemic scleroderma were subjected to quantitative evaluation and to qualitative analysis of glycosaminoglycans (GAG) by one-dimensional and two-dimensional cellulose acetate electrophoresis. Skin specimens from the back, clinically uninvolved but histologically demonstrating the initial change, revealed increased amounts of hyaluronidase, chondroitinase-resistant GAG of varying electrophoretic mobilities, and one of them was chemically confirmed to be heparan sulfate variant, whereas involved skin specimens showed hardly this increase.
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PMID:Initial change of glycosaminoglycans in systemic scleroderma. 12 27

The extracellular sulfated glycosaminoglycans synthesized by explants of rabbit cornea and sclera, and by confluent cultures of corneal fibroblasts after incubation in medium containing 35S-sulfate were compared. The glycosaminoglycans isolated from corneal explants differed considerably from those obtained from confluent corneal fibroblast cultures and scleral explants. Only the corneal explants secreted into the nutrient medium a population of enzyme-resistant 35S-sulfate-labeled glycosaminoglycan that eluted from Dowex 1-X2 (Cl-) at a 3 M sodium chloride concentration, and which was resistant to testicular hyaluronidase, chondroitinase ABC, and nitrous acid degradation. With time, corneal explants gradually synthesized less of this fraction with these attributes of keratosulfate. If the corneal epithelium and endothelium remained on the corneal explants the total incorporated 35S-sulfate was approximately double that obtained when the cornea was striped of these cells.
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PMID:A comparative study of extracellular sulfated glycosaminoglycans synthesized by rabbit corneal fibroblasts in organ and confluent cultures. 13 75

Histological aspects of cervical ripening were studied on the human uterine cervix during pregnancy. Cervical specimens were taken from 25 cases of cervical laceration of primiparous women immediately after delivery, 8 primiparous women whose cervixes opened 2-3 cm, and 5 cesarean-sectioned women with unripeness of cervix. The following histochemical techniques were used: alcian blue, azure A, hyaluronidase digestion, and chondroitinase ABC digestion. The collagen bundles disintegrated into fine fibers and also underwent quantitative changes during the ripening process of the cervix. The number of connective tissue cells was increased during pregnancy, but that of mast cells was decreased. In late pregnancy, acid mucopolysaccharides in the cervical ground substance were found to increase.
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PMID:Histological aspects of cervical ripening. 13 67

Rat liver cells grown in primary cultures in the presence of [(35)S]sulphate synthesize a labelled heparan sulphate-like glycosaminoglycan. The characterization of the polysaccharide as heparan sulphate is based on its resistance to digestion with chondroitinase ABC or hyaluronidase and its susceptibility to HNO(2) treatment. The sulphate groups (including sulphamino and ester sulphate groups) are distributed along the polymer in the characteristic block fashion. In (3)H-labelled heparan sulphate, isolated after incubation of the cells with [(3)H]galactose, 40% of the radioactive uronic acid units are l-iduronic acid, the remainder being d-glucuronic acid. The location of heparan sulphate at the rat liver cell surface is demonstrated; part of the labelled polysaccharide can be removed from the cells by mild treatment with trypsin or heparitinase. Further, a purified plasma-membrane fraction isolated from rats previously injected with [(35)S]sulphate contains radioactively labelled heparan sulphate. A proteoglycan macromolecule composed of heparan sulphate chains attached to a protein core can be solubilized from the membrane fraction by extraction with 6m-guanidinium chloride. The proteoglycan structure is degraded by treatment with papain, Pronase or alkali. The production of heparan [(35)S]sulphate by rat liver cells incubated in the presence of [(35)S]sulphate was followed. Initially the amount of labelled polysaccharide increased with increasing incubation time. However, after 10h of incubation a steady state was reached where biosynthetic and degradative processes were in balance.
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PMID:Structure and metabolism of rat liver heparan sulphate. 14 28

Proteoglycans were extracted from bovine articular cartilage with guanidine-HCl and fractionated in cesium chloride density gradients by equilibrium ultracentrifugation. The acidic glycosaminoglycan (AGAG) components were then determined enzymatically with chondroitinase-ABC and streptomyces hyaluronidase. Under associative and dissociative conditions, the distribution of the AGAG components was as follows: the ratio of 4-sulfated disaccharide units to total AGAG increased with decreasing density gradients whereas that of 6-sulfated disaccharide units to total AGAG increased with increasing density gradients. The ratio of disulfated disaccharide units to total AGAG increased somewhat with decreasing density gradients whereas that of non-sulfated disaccharide units tended to decrease. Although the cartilage proteoglycan macromolecules were heterogeneous, a certain regularity was observed with respect to the distribution of sulfate and the degree of sulfation in the chondroitin sulfate chains of the proteoglycans.
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PMID:Constitutional heterogeneity of the glycosaminoglycans in articular cartilage proteoglycans. 14 4

Medullary tissue of the normal rat kidney was perfused with 3 percent glutaraldehyde (GA), incubated in 0.5 percent cetyl pyridinium chloride and postfixed in 1 percent OsO4. In comparison with the ordinary fixation with GA and OSO4, the medullary interstitium represented abundant matrical substance that is rich in acid mucopolysaccharides (AMPS) and morphologically represents a diffuse reticular structure consisting of 30 to 150 a thick microfibrils and granular structures of 300 to 500 A in diameter. When chondroitinase was applied before OsO4 treatment, the dense granes disappeared and the microfibrils were replaced by loosely textured 30 A thick microfilaments. After hyaluronidase treatment the microfibrils disappeared and most granules changed into a ring-shaped structure with an electronlucent central portion. These results suggest that the reticular structure consists of microfilaments of hyaluronates and amorphous masking substance of chondroitin sulfates. In the dense granule, hyaluronates become concentrated in the central portion and chondroitin sulfate in the peripheral zone. When perfused with a CPC-containing GA, the medullary interstitium was diffusely filled with a large amount of fine granular substances suggesting the presence of water soluble free AMPS filling the reticular space.
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PMID:Ultrastructure and histochemistry of the medullary interstitial matrix of rat kidney. 14 5


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