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)

Proteoglycan monomer (D1) and aggregate (A1) preparations were isolated from 4 M guanidinium chloride extracts of the Swarm rat chondrosarcoma. When EDTA, 6-aminohexanoic acid, and benzamidine were present in the solutions, the D1 preparation contained a single component (SO = 23 S), and the A1 preparation contained 30% monomer (SO = 23 S) and 70 percent aggregate (SO = 111 S). In the absence of EDTA, 6-aminohexanoic acid, and benzamidine, the A1 preparations contained only small proteoglycan fragments, indicating that extensive enzymatic degradation had occurred. The composition of the proteoglycan monomer was different from that of proteoglycan monomer preparations from normal hyaline cartilages in that it did not contain keratan sulfate and chondroitin 6-sulfate; only chondroitin 4-sulfate was found. The A1 preparation from the chondrosarcoma contained only one link protein, which was like the smaller (molecular weight of 40,000) of the two link proteins present in A1 preparations from bovine nasal cartilage. When the A1 preparation from the chondrosarcoma was treated with chondroitinase ABC and trypsin and the digest was chromatographed on Sepharose 2B, a complex was isolated which contained the link protein and the segments of the protein core from the hyaluronic acid-binding region of the proteoglycan molecules.
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PMID:Isolation and characterization of proteoglycans from the swarm rat chondrosarcoma. 12 82

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

Chick limb bud mesenchyme cells from stage 23-24 embryos were isolated and grown in culture under conditions facilitating chondrogenic development. Dissociative extraction methods were used to isolate proteoglycans from Day 8 cultures, at which time the incorporation of [35S]sulfate into these macromolecules occurred at maximal rates. The monomer (D1) fraction contained 85 to 90% of the proteoglycans originally present in the matrix of the cultures. The composition of this fraction was approximately 7 to 8% protein, 7% keratan sulfate, and 85% chondroitin sulfate. The proportions of nonsulfated, 4-sulfated, and 6-sulfated disaccharides in chondroitinase digests were about 11%, 31%, and 58%, respectively. The D1 fraction exhibited a single, polydisperse component on Sepharose 2B chromatography and in the ultracentrifuge (so = 19 S). In associative density gradients about 35% of the proteoglycans were recovered in a gel at the top of the gradient. The remainder were recovered at the bottom of the gradient in the aggregate (A1) fraction. The A1 fraction exhibited two components, aggregate (about 70% of the total) and monomer, upon Sepharose 2B chromatography and in the ultracentrifuge (so = 120 S for aggregate; 18 S for monomer). The aggregate preparation contained only one of the two link proteins (molecular weight of about 45,000) which occur in proteoglycan preparations from many hyaline cartilages.
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PMID:Isolation and characterization of proteoglycans from chick limb bud chondrocytes grown in vitro. 13 38

Incorporation of sulfate into alcian blue-precipitable glycosaminoglycan of 12-day-old chick embryo sterna is stimulated by addition, separately or together, of normal human serum and physiological concentrations of thyroid hormones (Audhya, T.K., and Gibson, K.D. (1975) Proc. Natl. Acad, Sci. U. S. A. 72, 604--608). We present evidence that this stimulation is due to increased synthesis of at least one proteoglycan, with minor alterations in the size and chemical composition of the glycosaminoglycans. Pulse-chase experiments showed no detectable loss of label during the chase, in control sterna or sterna incubated with serum and L-3,5,3'-triiodothyronine; thus, all incorporation was the result of synthesis of glycosaminoglycans. In double-label experiments, with 35SO4(2-) and [3H]acetate, the molar ratio of 3H and 35S incorporated into glycosaminoglycans was changed little, if at all, by addition of serum or triiodothyronine or both, at concentrations which increased incorporation up to 2-fold. Glycosaminoglycans isolated from these and other incubations gave similar elution patterns from agarose columns, and identical electrophoretic patterns on cellulose acetate. Digestion with chondroitinase ABC (chondroitin ABC lyase; EC 4.2.2.4.) showed that incorporation was into chondroitin sulfate and possibly hyaluronic acid, and that the proportions of non-sulfated, 4-sulfated, and 6-sulfated disaccharide units differed little between stimulated and unstimulated sterna. Incorporation of [3H]serine into glycosaminoglycans from papain digest of sterna paralleled incorporation of 35SO4(2-), and indicated a number average molecular weight between 21,000 and 25,000 for the newly synthesized chondroitin sulfate. This value was confirmed by gel filtration chromatography, which also showed that the average molecular weight of the newly synthesized chondroitin sulfate decreased up to 15% under conditions of 2-fold stimulation. Proteoglycans were extracted from sterna incubated with [3H]serine and 35SO4(2-) and analyzed by isopycinic centrifugation in CsCl and by zone sedimentation in a sucrose gradient. A major proteoglycan fraction could be separated by either method. Incorporation of both isotopes into this proteoglycan fraction, and into glycosaminoglycans isolated after papain digestion, was stimulated in a coordinate manner. Almost identical results were obtained with both separation techniques. The results indicate that the synthesis of the major proteoglycan, and probably also of a minor one, is stimulated by serum and triiodothyronine.
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PMID:Stimulation of proteoglycan synthesis in chick embryo sternum by serum and L-3,5,3'-triiodothyronine. 13 41

Electron microscopy of ruthenium red stained bovine aorta before and after chondroitinase digestion demonstrates proteoglycans on and between collagen fibrils. The collagen-associated proteoglycans include a proteoglycan previously purified from this tissue as demonstrated by immunocytochemistry and are extractable with high molar guanidine HC1. In loci rich in proteoglycans such as areas of turbulent flow in calves, more proteoglycan can be demonstrated morphologically, and these molecules also coat elastin.
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PMID:The ground substance of the arterial wall. Part 2. Electron-microscopic studies. 13 92

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


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