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)

The parietal pleura of rabbits was incubated with 14C-glucosamine. It was found that 14C-glucosamine was incorporated into the fraction of crude glycosaminoglycans. Then the crude glycosaminoglycans were fractionated by using specific mucopolysaccharide-lyases (hyaluronidase from streptomyces hyalurolytics, chondroitinase AC and chondroitinase ABC). As a result, evidence was obtained that hyaluronic acid was synthesized in parietal pleura and was released into the surroundings.
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PMID:[Biosynthesis of hyaluronic acid in parietal pleura of the rabbit (author's transl)]. 49 96

Proteoglycans isolated under associative conditions in the presence of protease inhibitors from human nucleus pulposus contained 17% aggregate and 83% non-aggregating monomer (Kav = 0.5 on Sepharose CL-2B). Isolated aggregate after reduction and alkylation was resolved into two components (Kav = 0.15 and 0.43) on Sepharose CL-2B. Labeled proteoglycans isolated from parallel samples pulsed with [35S]sulfate and chased for up to 18 h were present largely as aggregated material (up to 78%). Reduction and alkylation of the labeled samples gave a labeled proteoglycan monomer with Kav = 0.15. Both the labeled and unlabeled chondroitin sulfate chains had the same distribution on Sepharose CL-6B and equivalent molecular weights (Mr = 2.0 x 10(3)). After chondroitinase ABC digestion, the unlabeled keratan sulfate-protein core was polydisperse with a Kav = 0.38 on Sepharose CL-4B while the labeled keratan sulfate-protein core had a Kav = 0.05. This indicates that the newly synthesized proteoglycan had a large core protein and suggests that the proteoglycans present in nucleus pulposus are originally synthesized as large molecular weight, aggregating proteoglycans.
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PMID:Aggregated proteoglycan synthesis in organ cultures of human nucleus pulposus. 50 May 96

Rat ovarian granulosa cells were isolated from immature female rats after stimulation with pregnant mare's serum gonadotropin and then maintained in culture. Proteoglycans were labeled using [35S]sulfate, D-[3h]glucosamine, or L-[3H]serine as precursors. 35S-labeled proteoglycans in the medium increased linearly up to 72 h after a 6- to 8-h lag period, and those in a 4 M guanidine HCl extract of the cell layer increased for about 16 h and then reached a plateau and stayed fairly constant up to 72 h. Two distinct sizes of proteoglycans were observed in the medium. The smaller (Kav = 0.60 on Sepharose CL-2B) had lower buoyant densities in dissociative gradients (rho less than 1.4 g/ml). The larger (Kav = 0.26 on Sepharose CL-2B) had high buoyant densities (recovered mainly in the bottom (D1) fraction of the dissociative gradient). More than 90% of the D1 proteoglycans contained dermatan sulfate chains (average Mr = 38,000) which yielded 84% 4-sulfated and 15% disulfated disaccharides after digestion with chondroitinase ABC. About 8% of the 35S-label in D1 was present as a heparan sulfate proteoglycan. When [3H]-glucosamine was used as a precursor, 28% of the 3H activity in the D1 proteoglycans was located in three major oligosaccharide components, two of which were similar or identical with those observed previously in D1 proteoglycans isolated from porcine follicular fluid. These results plus similar susceptibility of the labeled proteoglycans to proteolytic enzymes, especially plasmin, suggest that the granulosa cells synthesize the predominant follicular fluid proteoglycans.
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PMID:Biosynthesis of proteoglycans by rat granulosa cells cultured in vitro. 50 Jul 20

Monolayer cultures of arterial fibroblasts from 13-day chick embryonic aorta incorporated 35SO42- into glycosaminoglycans containing both glucuronic and iduronic acids. Bacterial chondroitinase ABC converted more than 98% of the 35SO4-labeled polymer to mono- or disaccharides, including (1) N-acetyl-D-galactosamine 4-sulfate, (2) delta 4,5-glucuronic acid 2- or 3-sulfate leads to N-acetylgalactosamine 6-sulfate, and (3) the unsaturated disaccharides normally obtained from chondroitin 4-sulfate and chondroitin 6-sulfate sequences. Chondroitinase AC converted only 77% of the 35SO4-labeled polymer to the same mono- and disaccharides and yielded, in addition, the following oligosaccharide products: (1) delta 4,5-glucuronic acid leads to N-acetylgalactosamine 4- or 6-sulfate leads to iduronic acid leads to N-acetylgalactosamine 6- or 4-sulfate; (2) N-acetylgalactosamine 4-sulfate leads to iduronic acid 2- or 3-sulfate leads to N-acetylgalactosamine 6-sulfate; (3) delta 4,5-glucuronic acid leads to N-acetylgalactosamine 4-sulfate leads to (iduronic acid leads to N-acetylgalactosamine 4-sulfate)2; (4) delta 4,5-glucuronic acid leads to N-acetylgalactosamine 4- or 6-sulfate leads to (iduronic acid leads to N-acetylgalactosamine 6- or 4-sulfate)2; (5) higher oligosaccharides containing iduronic acid and N-acetylgalactosamine 4-sulfate.
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PMID:Hybrid glycosaminoglycans synthesized by monolayers of chick embryo arterial fibroblasts. 51 51

Embryonic chick muscle contains two developmentally regulated lectins, which may be involved in cell interactions. These endogenous lectins are assayed as agglutinins of appropriate test erythrocytes. One of these, called lectin-2, interacts with specific glycosaminoglycans, especially heparin and dermatan sulfate. Lectin-2 is present at constant levels in both chick fibroblast and chick muscle cells throughout 14 days of culture but is released into the medium of cultured embryonic muscle after 7-8 days of culture, soon after myoblast fusion. Lectin-2 interacts strongly with a component of substrate-attached material in embryonic muscle cultures which is extractable from the cutlure dishes with alkali after the cells have been removed with ethylediaminetetraacetic acid. The active component in the substrate-attached material appears to be a glycosaminoglycan that is a more potent inhibitor of lectin-2 agglutination activity than any of the known glycosaminoglycans that we have tested. The active material is degraded by chondroitinase ABC but not by chondrotinase AC, hyaluronidase, or proteolytic enzymes and thus appears to be similar to dermatan sulfate. The results of these studies raise the possibility that lectin-2 functions by interacting with glycosaminoglycans, either associated with the cell surface or with the extracellular matrix.
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PMID:Extracellular lectin and its glycosaminoglycan inhibitor in chick muscle cultures. 52 83

Micro-scale isolation of sulfated glycopeptide from tissue was achieved by successive application of pronase digestion (Step 1), cetylpyridinium chloride-fractionation (Step 2), crude heparinase digestion or chondroitinase ABC digestion plus nitrous acid treatment (Step 3) and preparative cellulose acetate membrane-electrophoresis (Step 4). By this method, sulfated glycopeptide was obtained in a high yield from estrogen-treated rabbit uterus.
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PMID:A method for micro-scale isolation of sulfated glycopeptide from tissue. 52 51

The development of the sclerotome is considered as a model for the formation of mesenchyme from an epithelium. In early epithelial somites, transmission and scanning electron microscopy indicate considerable ultrastructural similarity between the future sclerotome and dermamyotomal regions. Subsequently, these two regions diverge in their development. In the forming dermamyotome, junctional complexes become more extensive and the cells become elongated, closely applied to each other, and have angular surface contours. In the forming sclerotome, there is an early reduction in apical junctions. The cells elongate, keeping their original polarity, and acquire numerous filopodia which contain punctate junctions at sites of cell-to-cell contact. Associated with cellular extension is an expansion of the intercellular spaces which do not contain any ultrastructurally recognizable material. Evidence for a role of hyaluronic acid in the expansion of the intercellular spaces is presented. As identified by the susceptibility of cetylpyridinium chloride precipitates to Streptomyces hyaluronidase and chromatographic separation of chondroitinase ABC digestion products, as much as 64--68% of the [3H]glucosamine-labeled glycosaminoglycans synthesized by explanted somites is hyaluronic acid. In addition, hyaluronidase-sensitive label is localized in the intercellular spaces of the sclerotome, as demonstrated by autoradiography. When Streptomyces hyaluronidase is injected in ovo into living embryos, the sclerotomal mesenchyme differentiates morphologically, but intercellular spaces are drastically reduced. It is hypothesized that the sclerotomal cells produce a hyaluronate-enriched extracellular matrix which is inflated by hydration to mediate the expansion of the sclerotomal mass towards the notochord.
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PMID:The role of extracellular matrix in the formation of the sclerotome. 52 73

Proteoglycan subunits (PGS) were isolated from bovine articular cartilage of calves and from cows, 18 months and 8 years old respectively. From the latter cartilage of osteoarthrotic and of non-osteoarthrotic sites was taken. PGS were characterized by gel-chromatography on Sepharose 2B columns and subjected to digestion with chondroitinase ABC and with papain. The isolated keratan sulphate-protein cores obtained from chondroitinase digestion were characterized on Sepharose 4B and the chondroitin sulphate chains on Sephadex G-200 gels. A larger molecular size of PGS was found in calf cartilage than in the other samples. This was attributed to the larger molecular size of chondroitin, whereas no change was observed in the keratan sulphate-protein cores. No change was observed in molecular size of PGS, isolated chondroitin sulphates or keratan sulphate-protein cores in osteoarthrosis in comparison with non-osteoarthrotic cartilage from the same joint or from younger adult animals.
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PMID:Proteoglycan structure of bovine articular cartilage. Variation with age and in osteoarthrosis. 53 16

Incubation of chick embryo epiphyseal microsomal preparations with either UDP-[14C]GlcUA or UDP-[14C]-GalNAc plus exogenous chondroitin 6-sulfate resulted in the incorporation of either a single [14C]GlcUA or a [14C]GalNAc onto the nonreducing ends of the exogenous glycosaminoglycan. Degradation by chondroitinase ABC yielded the terminal products [14C]Di-OS, [14C]Di-6S, and [14C]GalNAc. Incubations of the microsomal preparations with either UDP-[14C]GlcUA or UDP-GalN[3H]Ac without exogenous chondroitin 6-sulfate resulted in the addition of a single sugar onto the nonreducing end of endogenous chondroitin sulfate. Degradation by chondroitinase ABC yielded the terminal products [14C]Di-OS, [14C]Di-6S, and GalN[3H]Ac in a molar ratio of approximately 1:1:3.5. Incubations of the microsomal preparations with both UDP-[14C]-GlcUA and UDP-GalN[3H]Ac together resulted in formation of [14C,3H]chondroitin chains added to the endogenous chondroitin sulfate. Degradation by chondroitinase ABC resulted in products with a molar ratio of [14C,3H]Di-OS to GalN[3H]Ac varying from approximately 1:1.5 to 1:3. The results of these experiments indicate that chondroitin 6-sulfate terminates at its nonreducing end in a mixture of GlcUA and GalNAc (some sulfated). GalNAc is somewhat more frequent as the terminal sugar and adds more readily to endogenous acceptors.
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PMID:Biosynthesis of chondroitin sulfate. Chain termination. 56 46

Disc material from horse, ox, sheep, pig, dog and cat was stained by the Alcian-blue-critical electrolyte concentration technique and with the standard and two-step periodic acid Schiff methods. The effects of pretreatment with hyaluronidase and with chondroitinase was also evaluated. There appears to be a small increase in total cellular glycosaminoglycan content with age in all species: cellular material of high molecular weight however only increases in aged animals. The degree of sulphation of cellular glycosaminoglycans does not vary with age or with position in the disc.
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PMID:Staining of glycosaminoglycans in intervertebral disc cells. 60 1


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