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)

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

The bone inducing factor derived from BF osteosarcoma was purified in the following manner. Step 1. The sarcoma, grown in CBA mice, was excised and lyophilized. Step 2. The powder was washed with chilled acetone. Step 3. The acetone-treated powder was then homogenized with chilled distilled water. Step 4. Washing with 0.15M KCl. Step 5. The precipitate was incubated in in 0.2 N NH2OH, pH7.0, for 48 H at 25 degrees. After Step 5, the bone-forming activity showed a slight increase; however, the factor remained insoluble. The properties of the factor were as follows. The factor is relatively relatively heat stable; the osteogenic activity survived the treatment at 75 degrees for 15 min or at 55 degrees for 19 h. The activity was easily lost by mechanical shaking. Incubation with DNase, RNase, neuraminidase, chondroitinase ABC and beta-galactosidase left the osteogenic activity intact, but treatment with either pronase or collagnease destroyed this activity. The results suggest that the factor may be a protein. The activity was seen with the lyophilized BF osteosarcoma cells (without matrix), and it is probable that the factor was exclusively synthesized in the cells. The bone formation, observed across a millipore filter when living BF osteosarcoma enclosed in a millipore chamber was implanted in mice, suggests the synthesis and secretion of the factor from the cells.
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PMID:Studies on a factor responsible for new bone formation from osteosarcoma in mice. 105 58

The cytoplasmic sialomucin in Paget cells of both mammary and extramammary Paget's diseases was examined, using a new method proposed by Volz et al. (1987a, b). The staining methods used involved an electrolyte-Alcian Blue (pH = 5.8) and periodic acid Schiff. Oxidation was performed with 0.4 mmol/l periodate in 1 mol/l HCl at 4 degrees C or 50 mmol/l periodate in distilled water at room temperature for 1 h. Methylation, saponification, borohydride reduction, and digestion with diastase, neuraminidase (Vibrio cholerae) or chondroitinase ABC, were also employed. The cytoplasmic mucin was found to exhibit positive reaction for the above staining which were variously altered by the chemical modification procedures and diminished in intensity or abolished by digestion with neuraminidase. These results suggest that the cytoplasmic mucin in Paget cells is sialomucin without side-chain substituent in genital Paget's disease, and that with a substituent at C7 in mammary Paget's disease.
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PMID:Histochemical analysis of sialomucin in Paget cells of mammary and extramammary Paget's disease. 137 8

We examined biochemically and immunocytochemically the type and distribution of mineral binding proteoglycans (PGs) in rat mid-shaft subperiosteal bone using three monoclonal antibodies (MAb 1-B-5, 9-A-2, and 3-B-3) which specifically recognize unsulfated chondroitin, chondroitin 4-sulfate (C4-S) and dermatan sulfate (DS), and chondroitin 6-sulfate. Bone proteins were extracted from fresh specimens with a three-step technique: 4 M guanidine HCl (GdnCl), aqueous EDTA without GdnCl (E-extract), followed by GdnCl. Western blot analysis of SDS-polyacrylamide gel electrophoresis revealed that E-extract after chondroitinase ABC digestion reacted strongly with MAb 9-A-2 but not with MAb 1-B-5 or 3-B-3. After adehyde fixation, ethanolic trimethylammonium EDTA was used as a demineralizing agent for light and electron immunocytochemistry. This provided good retention of water-soluble PGs in the specimens. After chondroitinase ABC pre-treatment of tissue sections, MAb 9-A-2 specifically stained C4-S and/or DS in the walls of osteocyte lacunae and bone canaliculi in the mineralized matrix as well as in the unmineralized matrix such as pre-bone, vascular canals, and pericellular matrix surrounding osteocytes; the remainder of the mineralized matrix lacked staining. These results indicate that mineral binding PGs contain C4-S and/or DS and are exclusively localized in the walls of the bone lacuna and canaliculus.
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PMID:Biochemical and immunocytochemical characterization of mineral binding proteoglycans in rat bone. 189 98

The acid mucopolysaccharides (AMPs) in the human trabecular meshwork were studied ultrahistochemically with hyaluronidase and chondroitinase ABC digestion in 15 normal eyes and 27 cases of primary open-angle glaucoma (POAG). It was found that in normal eyes, hyaluronidase-sensitive AMPs existed in the connective tissue of cribriform meshwork and trabeculae. They could play an important role in regulating the aqueous outflow resistance. In POAG, the amount of AMPs in the trabecular meshwork was increased, leading to increased aqueous outflow resistance through the combination of hyaluronic acid with water, forming electron-dense "plaque" materials in a matrix of chondroitin sulfate.
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PMID:[An ultrahistochemical study of the trabecular meshwork in normal and open-angle glaucomatous eyes]. 214 7

Eighteen specimens of palatal mucosa were taken from 17 human subjects. Paraffin-wax sections were stained by routine methods and with various techniques to demonstrate glycosaminoglycans (GAG). In some sections, GAG were removed by selective degradative procedures before staining. Beneath all rugae, there were myxoid areas varying in size and marginal definition. Collagen fibres were few; elastic and reticulin fibres were numerous in a minority of sections. Alcianophilia at pH 2.5, preventable by streptomyces hyaluronidase digestion, suggested the presence of hyaluronic acid beneath the rugae. Alcian-blue staining at pH 1.0 and with the critical electrolyte concentration method using 0.5 M MgCl2 did not distinguish the myxoid tissue from the surrounding connective tissue and could be prevented by digestion with testicular hyaluronidase or chondroitinase ABC. Chondroitin sulphate and, or dermatan sulphate thus may be present but were not localized to the myxoid tissue. This unusual zone of loose connective tissue may act as a physical buffer resisting the local effects of high loads by allowing reversible extrusion of the water.
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PMID:Histological localization of myxoid tissue in normal human palatal mucosa and its glycosaminoglycans. 244 96

1. Proteoglycans were isolated from human and equine glomeruli or tubules by guanidine extraction and anion exchange chromatography. 2. These proteoglycan preparations contained about equal amounts of heparan sulfate and chondroitin sulfates. 3. During the preparation of glomerular or tubular basement membranes the main part of proteoglycans (greater than 50%) was extracted in the salt extract. Chondroitin sulfate proteoglycan was mainly found in the water and salt extracts of glomeruli and tubules, heparan sulfate proteoglycan in the deoxycholate extracts and the basement membranes. 4. The glomerular basement membrane (GBM) contains about 12% (human) or 20% (equine) of the proteoglycans of the total glomerulus. They consist of greater than 70% (equine) or 80% (human) of heparan sulfate. 5. Heparan sulfate proteoglycan was isolated from the proteoglycan preparations of human or equine glomeruli and tubules by additional treatment with nucleases and chondroitinase ABC followed by CsCl gradient centrifugation. 6. Protein accounts for about 40% (dry weight) of the heparan sulfate proteoglycans. Their amino acid composition is characterized by a high content of glycine, but 3-hydroxyproline, 4-hydroxyproline and hydroxylysine are lacking. 7. The biochemical characteristics of the heparan sulfate proteoglycan of human or equine glomeruli or tubules differ from that isolated from rat glomeruli by their higher protein content and their amino acid composition. The significance of these differences is discussed.
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PMID:Heparan sulfate proteoglycan from human and equine glomeruli and tubules. 297 41

Glycosaminoglycans (GAG) were isolated from bovine retinal microvessel basement membrane (RMV-BM) and quantitatively analyzed using a recently described competitive binding assay that is specific for and sensitive to nanogram amounts of heparan and chondroitin sulfates. Treatment of osmotically lysed retinal microvessels with the ionic detergent deoxycholate (DOC), required for liberation of the extracellular matrix for plasma membrane lipoproteins and purification of the insoluble matrix, solubilized less than 5% of the GAG in the water-insoluble material. Total GAG content in the DOC-insoluble basement membranes was approx. 0.52 micrograms/mg dry weight; about 70% of the measurable GAG was resistant to both chondroitinase ABC and chondroitinase AC digestion and was sensitive to nitrous acid treatment, indicating its heparan sulfate nature. Cellulose acetate electrophoresis revealed two bands, one of which had an electrophoretic mobility similar to heparan sulfate standard and was sensitive to nitrous acid; the other migrated in the same position as chondroitin sulfate standard and was sensitive to chondroitinase ABC and chondroitinase AC digestion. These results provide evidence that RMV-BM contains chondroitin sulfate(s) as well as heparan sulfate, and offer the first quantitative analysis of GAG in this extracellular matrix.
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PMID:Analysis of glycosaminoglycans in bovine retinal microvessel basement membrane. 333 12

An acidic glycoconjugate containing mannose, galactose and phosphate in approximately equimolar amounts was extracted from Leishmania donovani promastigotes and partially characterized. The glycoconjugate could be metabolically labeled with either [3H]mannose or [3H]galactose and was extractable from a delipidated residue fraction with water/ethanol/diethyl ether/pyridine/concentrated NH4OH (15:15:5:1:0.017) at 25 degrees C. The radioactively labeled glycoconjugate was found to possess the following characteristics: 1) comprised 45-60% of the total [3H]mannose label incorporated into macromolecules; 2) was soluble in alkaline solvents and 0.5% Triton X-100; 3) migrated as a broad band upon electrophoresis on sodium dodecyl sulfate-polyacrylamide gels with an approximate molecular weight of 15,000-30,000; 4) bound to DE52 cellulose and was eluted with a salt gradient of 0-0.1 M NaCl; 5) was insensitive to Pronase, hyaluronidase, chondroitinase, endo-beta-N-acetylglucosaminidase H, and endo-beta-galactosidase; and 6) possessed hydrophobic properties. An unusual feature of the glycoconjugate was its lability to mild acid hydrolysis (0.02 N HCl, 15 min, 60 degrees C). As determined by alkaline phosphatase and glycosidase digestion and paper chromatographic analysis, the major fragment generated by mild acid hydrolysis was found to be a phosphorylated galactosyl-beta-mannose disaccharide. All of these characteristics suggest that the glycoconjugate may be a polysaccharide and, possibly, may be important in parasite-host cell interactions.
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PMID:Expression of an unusual acidic glycoconjugate in Leishmania donovani. 670 85

The semilunar menisci of the knee have an important mechanical function and are commonly involved in joint degeneration. However, previously published analyses of the compositions of normal and degenerate human menisci vary widely. In the present study the glycosaminoglycan content and composition of selected areas of the menisci of eight normal knees of working foxhounds were determined. The menisci contained 10% less water and abut 8-fold less glucosaminoglycan than did the articular cartilage of these animals. Although the glycosaminoglycan composition was the same in different regions of the menisci, the total amounts varied considerably. Of the chondroitinase digestible material, approx. 60% was chondroitin 6-sulphate, 25% chondroitin 4-sulphate, 10% chondroitin and 5% dermatan sulphate. Hyaluronic acid accounted for about 6% of the total uronic acid.
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PMID:The glycosaminoglycans of canine menisci. 679 64


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