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)

We examined immunocytochemically the type and distribution of glycosaminoglycans and proteoglycans (PG) in predentin and dentin demineralized with EDTA after aldehyde fixation of rat incisors using (a) four monoclonal antibodies (1-B-5,9-A-2,3-B-3, and 5-D-4) which recognize epitopes in unsulfated chondroitin (C0-S), chondroitin 4-sulfate (C4-S), chondroitin 6-sulfate (C6-S), and keratan sulfate (KS) associated with the PG, and (b) monoclonal (5-D-5) and polyclonal antibodies specific for the core protein of large and small dermatan sulfate (DS) PG. Light microscope immunoperoxidase staining after pre-treatment of tissue sections with chondroitinase ABC localized the majority of stainable PG (C4-S, KS, DSPG, C0-S, and C6-S) in predentin and, to a lesser extent (C4-S and small DSPG), in the dentin matrix. The former site demonstrated relatively homogeneous PG distribution, whereas the latter site revealed that strong staining of C4-S and small DSPG was confined mostly to dentinal tubules surrounding odontoblastic processes, with only weak staining in the rest of the dentin matrix. These results indicate that there is not only a definite difference between PG of predentin and dentin but also a selective decrease in the concentration or alteration of these macromolecules during dentinogenesis and mineralization.
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PMID:Immunohistochemical localization of glycosaminoglycans and proteoglycans in predentin and dentin of rat incisors. 168 34

In the course of an ultrastructural cytochemical study of intracellular sulphated proteoglycans involving the addition of cetylpyridinium chloride in the primary aldehyde fixative, a remarkable ultrastructural preservation of the collagen-associated sulphated proteoglycans was observed. Together with the preservation of their localization among the collagen fibrils (with, for some of them, a 50 nm periodic association with d-bands) and of their native elongated shape, previously observed under similar technical conditions, these stick-shaped and chondroitinase ABC-sensitive proteoglycans exhibited a typical pattern with several dense longitudinal parallel tracks (periodicity: 3-4 nm) not described as yet. Readily observable without high iron diamine-staining, the morphology of these cetylpyridinium chloride-precipitated and collagen-associated polyanions was particularly enhanced after incubation in the diamine solution which ascertained their sulphate content. Such a common ultrastructural organization with parallel tracks for both intracellular (i.e., in eosinophilic polymorphonuclear cells and Kurloff cells) and extracellular CPC-precipitated sulphated proteoglycans could correspond to intrinsic properties of the complexed molecules and could be related to 'double track' proteoglycans observed under other technical conditions in basement membranes.
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PMID:Collagen-associated sulphated proteoglycans. Ultrastructure after formaldehyde-cetylpyridinium chloride fixation. 172 36

In order to visualize by light microscopy the glycosaminoglycans (GAGs) in the rat tongue mucosa, the tissue was fixed with cuprolinic-blue (CB)-aldehyde and the staining enhanced by autometallographic (AM) procedure. As other polyanions were also detected, enzymatic digestions with hyaluronidase, chondroitinase ABC and pronase were performed on these tissues in order to test the specificity of the staining. Chondroitinase ABC caused a dramatic decrease of silver grains in the lamina propria whereas hyaluronidase and pronase induced only discrete or no modification. This supported the concept that the GAGs visualized by CB and autometallography in this area as dermatan sulphate. The other polyanions (mostly DNA and RNA) seen in the epithelial layers were unaffected by these enzyme treatments.
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PMID:Autometallographic visualization of glycosaminoglycans in the tongue mucosa of rats using cuprolinic blue and enzymatic digestions. 186 53

A direct Schiff reaction of elastic tissues has been known for many years, but the nature of the native aldehyde-rich components has not been clear. In this study, chicken, quail, and rat embryos and adult rat lung, aorta, and kidney were fixed in methacarn or in a formalin solution, embedded in paraffin, and sections of 8-10 micron obtained. Rehydrated sections were incubated for various periods in solutions of the enzymes chondroitinase ABC, clostripain, collagenase, elastase, heparatinase, hyaluronidase, subtilisin Carlsberg ("protease"), or trypsin, and in solutions of phosphomolybdic acid or sodium borohydride. After incubation, sections were placed, without prior oxidation, in Schiff's reagent, and were ultimately observed and photographed in transmitted light or with blue or green epifluorescence. A Schiff-positive substance was found, always and exclusively, in elastic tissues of the vasculature and lungs, which was hydrolyzed by the proteolytic enzymes to an extent that ranged from complete loss of Schiff reaction in minutes (trypsin) to no loss of Schiff reaction in 22 hr (clostripain). The Schiff-reactive protein preceded the time of appearance of elastin in the early embryos. We conclude that the aldehyde-rich protein responsible for this reaction is a harbinger of elastogenesis in vivo and speculate that it may represent the elastic microfibril or a component thereof.
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PMID:A new interpretation of the direct Schiff reaction of elastic connective tissue. 244 56

Histochemical estimation of acid glycosaminoglycan was critically re-evaluated, using the meniscus, intervertebral disc, ossified yellow ligament, ganglion, Dupuytren's fascia and several other tissues. Each tissue was stained with toluidine blue, alcian blue, high iron diamine, low iron diamine, aldehyde fuchsin and dialyzed iron-ferrocyanide. Digestion techniques for GAG were used in these staining methods, and the effects of protease inhibitors (PI) on digestion were also examined. In this study, the optimal temperature for digestion with Streptomyces hyaluronidase was between 37 degrees C and 43 degrees C, which varied according to the tissue examined. The addition of PI seemed necessary because the enzymatic treatment without PI resulted in an excessive decrease of staining. Protease-free chondroitinase ABC, which did not excessively decrease staining results, was found to be more useful than chondroitinase ABC without PI.
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PMID:[A histochemical study of acid glycosaminoglycans on normal and pathological cartilage, ligaments and several other connective tissues]. 244 81

Twenty seven bladder tumors, three ureteral tumors and one renal pelvic tumor were studied by means of light microscopic histochemical methods for demonstration and identification of acid mucopolysaccharides. Alcian blue (pH 1.0), alcian blue (pH 2.5), periodic acid-Schiff (PAS) and aldehyde-fuchusin stainings were performed. These stainings showed that all tumor specimens contained acid mucopolysaccharides. For identifying individual acid mucopolysaccharides, enzyme digestion procedures were performed prior to staining with alcian blue. (streptomyces hyaluronidase, testicular hyaluronidase, chondroitinase ABC, chondroitinase AC, keratanase, heparinase, heparitinase.) According to these experiments, high-grade, and high-stage tumors contained large amounts of sulfated mucopolysaccharides. Squamous cell carcinomas of the bladder contained especially large amounts of chondroitin sulfate AC.
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PMID:[Histochemical studies of bladder tumors]. 294 17

The binding of peanut agglutinin (PNA) and soybean agglutinin (SBA) to cartilage proteoglycans was investigated by histochemical, ultrastructural cytochemical, and biochemical methods. Following aldehyde fixation, specimens of rat epiphyseal cartilage were examined by horseradish peroxidase-labelled lectin cytochemistry with and without prior digestion in chondroitinase ABC. At the light microscope level neither PNA nor SBA exhibited any affinity for cartilage matrix, but became strongly bound following chondroitinase treatment. Similarly, at the ultrastructural level, extracellular matrix granules, presumed to be proteoglycan monomer(s), lacked PNA affinity in undigested specimens, and stained very weakly with SBA. Both PNA and SBA weakly to moderately stained the trans cisternae of the Golgi-flattened cisternae in chondrocytes. The chondrocyte plasmalemma lacked PNA staining, but reacted weakly with SBA. Following chondroitinase digestion, PNA and SBA stained matrix granules, and the cell surface of chondrocytes intensely, whereas the Golgi trans cisternae, the Golgi-derived vacuoles, and multivesicular bodies demonstrated weak to moderate reactivity. Proteoglycan aggregates purified from rat chondrosarcoma and bovine nasal cartilage bound PNA and SBA avidly after digestion with chondroitinase. Undigested proteoglycans lacked affinity for PNA and reacted very weakly with SBA. These results indicate that both PNA and SBA specifically react with chondroitinase-modified oligosaccharide(s) bound to core proteins of cartilage proteoglycans. This provided a specific histochemical and ultrastructural cytochemical procedure for localizing chondroitin sulphate-containing proteoglycans.
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PMID:Specific binding of peanut agglutinin and soybean agglutinin to chondroitinase ABC-digested cartilage proteoglycans: histochemical, ultrastructural cytochemical, and biochemical characterization. 339 1

Neurons in the human visual cortex were demonstrated to possess an intensely negatively charged surface coat which was stained with cationic iron colloid and aldehyde fuchsin. Digestion with hyaluronidase eliminated both the iron colloid and fuchsin stainings of the coats. Treatment with chondroitinase ABC, heparitinase and keratanase eliminated the iron colloid staining of the coats, but did not interfere with the fuchsin staining. Electron microscopy of ultrathin sections revealed that the cationic iron particles were preferentially deposited in the perineuronal tissue spaces. These findings indicate that the surface coats consist of sulfated proteoglycans, which, as an extracellular matrix, occupy the perineuronal tissue spaces. This study further demonstrates that neurons with such surface coats are identical with neurons labeled with lectin Vicia villosa agglutinin. The cell surface glycoproteins reactive to this lectin may not be the structural elements of the sulfated coats since the lectin labeling was not interrupted by the hyaluronidase digestion.
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PMID:Neurons with intensely negatively charged extracellular matrix in the human visual cortex. 773 78

The human visual cortex, especially its ganglionic lamina, was found to contain many neurons with perineuronal sulfated proteoglycans which were stained with cationic iron colloid and aldehyde fuchsin. It also contained many neurons with surface glycoproteins labeled with lectin Vicia villosa agglutinin (VVA) or Glycine max agglutinin (SBA). Double staining frequently showed that the neurons stained with cationic iron colloid were not labeled with lectin VVA or SBA. Hyaluronidase and chondroitinase ABC/heparitinase/keratanase digestions eliminated the perineuronal cationic iron colloid reaction, but never interfered with the cell surface lectin labeling. These findings indicate that the cell surface glycoproteins reactive to lectin VVA or SBA are neither structural elements nor adhesive molecules of the proteoglycans. Double staining further demonstrated that in some neurons with perineuronal sulfated proteoglycans, the cytoplasm was labeled with lectin Arachis hypogaea agglutinin (PNA). It was further noticed that the lectin VVA-labeled neurons were not always identical with the neurons labeled with lectin SBA or with lectin PNA.
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PMID:Neurons with perineuronal sulfated proteoglycans in the human visual cortex, with special reference to their reactions to lectins. 852 42

Neurons of intracerebellar nuclei in the mouse brain were demonstrated to possess a marked surface coat, formed 3-4 weeks after birth, which was stainable with cationic iron colloid or aldehyde fuchsin. Neurons with a similar surface coat were noted as relay or local interneurons in rather restricted areas such as the occipital cortex, retrosplenial cortex, zona incerta, hippocampal subiculum and spinal posterior horn. Dark neurons with condensed cytoplasm were also shown to be covered with the surface coat. The surface coat was stained doubly with cationic iron colloid and aldehyde fuchsin. Digestion with hyaluronidase eliminated the stainability of the surface coat to both agents. Combined digestion with chondroitinase ABC, heparitinase and keratanase eliminated the cationic iron colloid staining of the surface coat, but did not interfere with the aldehyde fuchsin staining of the surface coat. Electron microscopy of ultrathin sections revealed that the iron particles indicating sulfated proteoglycans were preferentially deposited in the perineuronal tissue spaces. Many neurons in the hippocampal subiculum possessed cell surface glycoproteins which were labeled with lectin Vicia villosa or soybean agglutinin and formed 1-2 weeks after birth. Double staining revealed that these lectin-labeled neurons were identical in part with the neurons reactive to the cationic iron colloid. Dark neurons began to appear 3-4 weeks after birth. The formation of perineuronal sulfated proteoglycans and the appearance of dark neurons, both occurring during the weaning period, may reflect the morphological and physiological completion of the brain. Dark neurons are suggested to be exhausted cells that are restored to light or normal neurons after sleep.
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PMID:Perineuronal sulfated proteoglycans and dark neurons in the brain and spinal cord: a histochemical and electron microscopic study of newborn and adult mice. 884 37


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