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)

The viscoelastic properties of culture medium obtained from confluent 3T3-L1 preadipocytes, after differentiation with isobutyl-methylxanthine and dexamethasone, were studied with a rotational Couette viscometer. In close association with adipocyte differentiation, the culture medium showed gel-like properties, in concert with an increase in viscosity. This behavior vanishes after digestion by Streptomyces hyaluronidase or chondroitinase ABC, but not after application of collagenase, pronase, trypsin, DNase, or neuraminidase, or by treatment with EDTA or mercaptoethanol, indicating that the primary substance responsible for this behavior is hyaluronic acid. The material revealed a non-Newtonian behavior with an irreversible disruption of the network by shear force at high speeds. The viscosity of the medium, containing about 1 microgram/ml of hyaluronic acid, was calculated to be similar to that of a solution containing 1.7 mg high molecular weight hyaluronic acid per milliliter of stock culture medium. The comparison of rheological properties between the culture medium and solutions of hyaluronic acid indicated the possibility of a highly organized network in the culture medium that is more complicated than a simple interaction between homologous hyaluronic acid molecules. The non-Newtonian behavior depends on the hyaluronic acid concentration in the medium as well as on the length of exposure of the 3T3-L1 cells to the isobutyl-methylxanthine/dexamethasone mixture. The results point toward the possibility of interaction between hyaluronic acid and binding proteins.
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PMID:Rheological effects of the presence of hyaluronic acid in the extracellular media of differentiated 3T3-L1 preadipocyte cultures. 768 59

The molecular specificity of the dental papilla of a bell-stage tooth was studied by production of dental-papilla-reactive monoclonal antibodies (Mabs). One of the Mabs, designated 7C5, recognized an epitope present in glycosaminoglycan. Several lines of evidence suggested that the 7C5-epitope consists of chondroitin 6-sulfate. The Mab did not react with mouse dental epithelium, but reacted uniformly with mesenchymal tissue in the mandibular process and accumulated in the dental sac and in the papilla of bell-stage tooth germs. The 7C5-staining was lost from the differentiating odontoblasts, while the staining in the molar tooth papilla was accumulated in the subodontoblastic layer. In the developing mouse incisor, the 7C5-epitope was restricted to the lingual-posterior area. The 7C5-epitope was also present in pulpal tissue and predentin of different types of teeth of various mammalian species, including man, sheep, swine, and rat. Collagenase pre-treatment of tissue sections abolished the bulk of the 7C5-reactivity in peridental mesenchyme during embryonic stages while leaving the staining of the dental papilla intact. In newborn and adult teeth, collagenase also impaired the reactivity in the pulp except for the subodontoblastic layer. This suggests the existence of different subpopulations of the 7C5-epitope containing proteoglycans in dental papilla and pulp. A high-molecular-weight proteoglycan, sensitive to chondroitinase ABC but not to heparinase or heparitinase, was immunoprecipitated by 7C5 from extracts of bell-stage mouse tooth germs. We suggest that the evolutionary conservation of chondroitin 6-sulfate in the dental pulp reflects its properties as non-terminally differentiated tissue and perhaps the retention of a potential to differentiate to odontoblasts.
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PMID:A chondroitin sulfate epitope in mammalian dental pulp and its developmental expression in mouse dental papilla. 769 81

The object of this study was to determine the correlation between clinical symptoms and the activity of enzymes such as collagenase, chondroitinase, and hyaluronidase produced by bacteria isolated from infected root canals. The materials examined consisted of 28 teeth with apical periodontitis from 25 patients. Bacteria producing collagenase or chondroitinase and hyaluronidase were found to be significantly related to subacute clinical symptoms involving percussion pain. The frequency of bacteria producing collagenase was higher in isolates from root canals with a radiolucent area over 5 mm in diameter than in those from canals having a radiolucent area less than 5 mm in diameter.
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PMID:Relationship between clinical symptoms and enzyme-producing bacteria isolated from infected root canals. 800 69

The tectorial membrane is a gel-like, acellular connective tissue overlying the microscopic organ of Corti--the auditory sensory structure. It is instrumental in the sound-synchronous deflection of the stereocilia of the hair cells, a central event in auditory transduction. It is well established that collagen, primarily type II, constitutes the major protein of the tectorial membrane, with smaller amounts of types IX and XI also present. However, conclusive information on the proteoglycans in this structure is lacking. Tectorial membranes were extracted with a 4 M guanidine--HCl solvent, and proteoglycans isolated after ethanol precipitation and collagenase treatment. A colorimetric assay based on the binding of the cationic dye safranin O to glycosaminoglycans, in combination with enzymatic techniques, detected significant amounts of chondroitin sulfate and keratan sulfate (0.29 and 0.17% on a wet weight basis, respectively). Agarose-polyacrylamide electrophoresis of chondroitinase-digested samples revealed a core protein with a similar molecular mass to that of the large cartilage proteoglycan aggrecan. This proteoglycan reacted with the antibody 3-B-3 (recognizing modified chondroitin 6-sulfate linkage region oligosaccharides). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed several low molecular mass proteins which reacted with 5-D-4, specific for keratan sulfate, one of which showed characteristics of fibromodulin. Comparison of the quantitative aspects of various connective tissue components of tectorial membrane with other type II collagen-containing structures revealed that this tissue resembles highly hydrated cartilage.
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PMID:Uronic acid-containing glycosaminoglycans and keratan sulfate are present in the tectorial membrane of the inner ear: functional implications. 827 27

After in vivo administration of purified antibody against cultured mesangial cell (anti-MC IgG), glomerular basement membrane (GBM) was selectively bound. The glomerular bound anti-MC IgG exhibited a monospecificity for a 109-kDa antigen extracted from cultured mesangial cells and normal GBM. The antigen was not digestible by collagenase, heparitinase, or chondroitinase and was revealed by immunoelectron microscopy of a normal glomerular component to be predominantly distributed along the lamina rara externa of GBM and to be absent in mesangium. The ample expression of the antigen in puromycin aminonucleoside nephrosis implies that it represents a significant sclerotic material in glomerulonephritis. Abnormal production of GBM components by mesangial cells may play an important role in glomerulosclerosis.
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PMID:Coexpression of a novel glomerular basement membrane matrix material in mesangial cell culture and glomerulosclerosis. 854 99

A review of the world medical literature on chemonucleolysis with an emphasis on recent studies, meta-analyses, and the history of the procedure in North America from a regulatory, social, and medicolegal perspective was performed to determine the current status of chemonucleolysis in the management of disc displacement. The world literature supports the use of chymopapain for chemonucleolysis as a safe and effective alternative to surgical disc excision. The efficacy of chymopapain has been shown by prospective, randomized, placebo-controlled, double-blind trials with a minimum 10-year follow-up period. The safety of chymopapain injection compared with surgery has been demonstrated in meta-analyses and in extensive post-marketing surveillance in the United States and Europe. Clinical studies with collagenase and laboratory studies with chondroitinase ABC have shown that chemonucleolysis can be performed with enzymes other than chymopapain. Clinical trials have been performed with collagenase for chemonucleolysis, but all of the results have not been published. Preclinical research with chondroitinase ABC has demonstrated its usefulness for chemonucleolysis in the animal model, but human trials have not begun.
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PMID:Update on chemonucleolysis. 911 26

We report further characterization of a cementum-derived protein that promotes the adhesion and spreading of periodontal cells. The cementum attachment protein (CAP) was extracted from bovine cementum, separated by diethylamino ethyl (DEAE)-cellulose chromatography, and purified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and C18 reverse phase high performance liquid chromatography. The purified preparation contained a single protein band migrating with M(r) 56,000. It did not cross-react with polyclonal antibodies to osteopontin, vitronectin, or other attachment proteins. The attachment activity was resistant to chondroitinase ABC digestion. An internal amino acid sequence of six peptides was determined by microsequencing, and the peptide sequences were not present in other attachment proteins described in cementum. Four sequences contained Gly-X-Y repeats typical of collagen helix. One 17 amino acid peptide had 82% homology with a type XII collagen domain. However, bovine type XII collagen did not promote fibroblast attachment. Although another 19-amino-acid-long peptide had 95% homology to bovine alpha 1 [I], two other peptides were only 74% and 68% homologous, and the CAP was not recognized by anti-type I collagen antibody. The attachment activity of CAP was susceptible to bacterial collagenase. The CAP did not cross-react with antibodies to type V, XII, and XIV collagens. These data and our previous immunostaining data indicate that the CAP is not related to other collagens or attachment proteins and that it is a collagenous attachment protein localized in cementum.
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PMID:Characterization of a collagenous cementum-derived attachment protein. 915 84

Negative charged sites in the normal rabbit articular cartilage were investigated using cationic colloidal iron methods. In light microscopy of the cartilage stained with the colloidal iron at pH 1.5, a distinct Prussian blue reaction was observed in the pericellular matrix, and a weak blue reaction in the territorial and interterritorial matrices. At pH 7.0, a diffuse Prussian blue reaction was observed in the pericellular and interterritorial matrices. Digestion with chondroitinase ABC, hyaluronidase and keratanase could not erase the Prussian blue reaction. However, the sections digested with collagenase followed by chondroitinase ABC showed significant elimination of the Prussian blue reaction. Electron microscopy of ultrathin sections stained with the colloidal iron at pH 1.5 revealed that the cationic colloid particles were deposited abundantly in the pericellular matrix and dotted along collagen fibrils in the territorial and interterritorial matrices. The present results suggest that negatively charged sites in the articular cartilage derive mostly from chondroitin sulfate, whose proteoglycans firmly bind to collagen fibrils. Such an ultrastructure may maintain the electrostatic microenvironment in the collagen plexus, holding much water in the cartilage matrix, and also producing biomechanical properties such as tensile strength and elasticity of the cartilage.
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PMID:Negative charges bound to collagen fibrils in the rabbit articular cartilage: a light and electron microscopic study using cationic colloidal iron. 947 52

The method for the determination of hyaluronan and chondroitin/dermatan sulfates in the tissue sections on a glass slide, which were prepared by histological technique, was established by applying to porcine skin. The degradation of these glycosaminoglycans to the unsaturated disaccharides in porcine skin sections on a glass slide was achieved by chondroitinase ABC and ACII in the presence of highly purified bacterial collagenase. Subsequently, the resulting unsaturated disaccharides were determined by HPLC with fluorometric postcolumn derivatization using 2-cyanoacetamide as a reagent. So far, the determination of the glycosaminoglycans in the tissues has taken up more than 5 days, whereas the determination of the glycosaminoglycans in the frozen sections by the present method was completed within a day. In addition, applications of the present method to the serial polyester wax sections processed with a small surgical knife made it possible to determine the glycosaminoglycans in a local part in the tissue section. The present method should open a way for the clinical analysis of glycosaminoglycans in the pathological tissue samples.
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PMID:Quantification of hyaluronan and chondroitin/dermatan sulfates in the tissue sections on glass slides. 991 75

In order to evaluate the ability of the arthroscopic indentation instrument, originally developed for the measurement of cartilage stiffness during arthroscopy, to detect cartilage degeneration, we compared changes in the stiffness with the structural and constitutional alterations induced by enzymes on the tissue in vitro. The culturing of osteochondral plugs on Petri dishes was initiated in Minimum Essential Medium with Earle's salts and the baseline stiffness was measured. Then, the experimental specimens were digested using 50 microg ml(-1) trypsin for 24 h, 0.1 U ml(-1) chondroitinase ABC or 30 U ml(-1) purified collagenase (type VII) for 24 h or 48 h (n = 8-15 per group). The control specimens were incubated in the medium. After the enzyme digestion, the end-point stiffness was measured and the specimens for the microscopic analyses were processed. The proteoglycan (PG) distribution was analysed using quantitative microspectrophotometry and the quantitative evaluation of the collagen network was made using a computer-based polarized light microscopy analysis. Decrease (p < 0.05) of cartilage stiffness was found after 24 h trypsin (36%) and 48 h chondroitinase ABC (24%) digestion corresponding to a decrease (p < 0.01) of up to 80% and up to 30% in the PG content respectively. Decrease of the superficial zone collagen content or arrangement (78%, p < 0.001) after 48 h collagenase digestion also induced a decrease (30%, p < 0.001) in cartilage stiffness. We conclude that our instrument is capable of detecting early structural and compositional changes related to cartilage degeneration.
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PMID:Experimental validation of arthroscopic cartilage stiffness measurement using enzymatically degraded cartilage samples. 1007 Jul 99


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