Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: DrugBank:APRD00216 (ABC)
 8,859 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Acid mucopolysaccharides in mast cell granules were histochemically studied in the lesion of urticaria pigmentosa and in the dermis of normal human skin. Alcian blue and azure A were used to stain mucopolysaccharides. Bromphenol blue was employed for detection of basic proteins. In a further attempt to identify various polyanions, staining was carried out with alcian blue containing various concentrations of electrolytes. Methylation, saponification, and digestion with streptomyces or testicular hyaluronidase, chondroitinase ABC, sialidase, or desoxyribonuclease were also employed. The results obtained are most likely to suggest the presence of hyaluronic acid in mast cell granules.
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PMID:Histochemical demonstration of hyaluronic acid in human dermal mast cells. 5 4

Proteoglycans were identified and localized histochemically and ultrastructurally in normal and hyperplastic arterial intimas in nonhuman primates (Macaca nemestrina). These regions were consistently more alcianophilic than the adjacent medial layers and this alcianophilia was absent after treatment with glycosaminoglycan-degradative enzymes. Ultrastructurally, the intimal intercellular matrix consisted of numerous, irregularly shaped, 200-500-A diameter granules possessing 30--60-A diameter filamentous projections, and these granules were dispersed between collagen and elastic fibers. The granules exhibited a marked affinity for ruthenium red and were interconnected via their filamentous projections. The ruthenium red-positive granules were intimately associated with the plasma membrane of intimal smooth muscle cells and attached to collagen fibrils and elastic fibers. The matrix granules were completely removed after testicular hyaluronidase or chondroitinase ABC digestion but only partially removed after leech hyaluronidase treatment. These results suggest that the matrix granules contain some hyaluronic acid and one or more isomers of chondroitin sulfate. In addition to the large ruthenium red-positive matrix granules, a smaller class of ruthenium red-positive granule (100--200-A diameter) was present within the basement membranes beneath the endothelium and surrounding the smooth muscle cells. Ruthenium red also exhibited an affinity for the surface coat of the smooth muscle cells. The potential importance of proteoglycans in arterial intimal hyperplasia is discussed.
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PMID:Proteoglycans in primate arteries. I. Ultrastructural localization and distribution in the intima. 5 34

Histochemical localization of the estrogen-induced sulfated glycoproteins was made in the estrogen-treated rabbit uterus. Biochemical studies by a group of Endo et al, affirmed these particular glycoproteins were PAS-positive and metachromatic as stained with TB. No sign of digestion, however, has been detected in a series of tests with alpha-amylase, testicular hyaluronidase, streptomyces hyaluronidase, chondroitinase AC and chondroitinase ABC, and heparinase. The apical portions of the epithelial and glandular cells, obviously expanded by the estrogen treatment, display strong beta-metachromasia with TB (pH 4.0), saliva-resistant PAS-positive reactions, and also alcianophilia with AB (pH 2.5). These reactions are not reduced after the treatment with the enzymes above-mentioned. Meanwhile, in the stromal matrix, the same enzymes give an influence to diminish the reactions to various extent. Our results suggest that the estrogen-induced sulfated glycoprotein is definitely localized in the apical portions of the epithelial and glandular cells. The identity is emphasized between the substance that is elucidated in the histochemical sections and the sulfated glycoproteins that have been specified solely by means of biochemical assays.
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PMID:Histochemical localization of estrogen induced sulfated glycoprotein in rabbit uterus. 5 8

Acid mucopolysaccharides in dermal papillae of hair follicles from both bald and on-bald regions of the scalp of stump-tailed macaques were studies histochemically. Alcian Blue, Azure A and Periodic acid Schiff methods were used for staining mucopolysaccharides, and Bromphenol Blue for staining basic proteins. In an attempt to identify various polyanions, staining was carried out with Alcian Blue containing different concentrations of electrolytes. Methylation, saponification, mild acid hydrolysis and digestion with streptomyces or testicular hyaluronidase, chondroitinase ABC, or sialidase, were also used. The results indicate that chondroitin sulphate B is present in the papillae of terminal hair follicles in early and intermediate anagen, and degraded chondroitin sulphates are present in the papillae of vellus and terminal hair follicles in late anagen.
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PMID:Acid mucopolysaccharides in hair papillae of the stump-tailed macaque (Macaca speciosa). 5 48

Treatment of tissue sections with enzymes wich degrade specific types of glycosaminoglycans should provide a means for localizing glycosaminoglycans in tissue sections. The feasibility of this technique was examined by utilizing endogenously labelled glycosaminoglycans in chick and quail embryos. Less than 8% of the total glycosaminoglycans appear to be lost non-specifically during fixation and dehydration. Both Streptomyces hyaluronidase and chondroitinase ABC degraded more than 90% of their respective substrates and demonstrated minimal non-specific extraction of other glycosaminoglycans. The selectivity of chondroitinase ABC for sulphated glycosaminoglycans was substantially increased by raising the pH of the incubation buffer to 8.6. At this pH, chondroitinase ABC degraded negligible amounts of hyaluronic acid. Use of both Streptomyces hyaluronidase and chondroitinase ABC confirmed that embryonic hyaluronic acid binds Alcian Blue under conditions that were previously believed specific for sulphated glycosaminoglycans. We suggest that this may be due to the increased molecular weight of embryonic hyaluronic acid compared to the hyaluronic acid in adult tissues. The results presented suggest that treatment of adjacent sections with buffer, chondroitinase ABC at pH 8.6, and Streptomyces hyaluronidase and subsequent staining with Alcian Blue provides a method for localizing and quantitating glycosaminoglycans in tissue sections.
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PMID:The histochemical specificity of Streptomyces hyaluronidase and chondroitinase ABC. 8 Mar 94

The carbohydrate component in amyloid was histochemically compared with that in colloid or hyaline. Alcian blue, azure A, and periodic acid Schiff were used to stain mucopolysaccharides. In a further attempt to identify various polyanions, staining was carried out with alcian blue containing various concentrations of electrolytes. Methylation, saponification, acid hydrolysis, and digestion with streptomyces or testicular hyaluronidase, or chondroitinase ABC were also employed. The results obtained suggest that the presence of heparitin sulfate in amyloid, of chondroitin sulfate A in hyaline, and of chondroitin sulfate C in colloid.
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PMID:Histochemical investigation of acid mucopolysaccharides in amyloid, colloid and hyaline. 8 75

Using histochemical methods, the presence of acidic glycosaminoglycans in the cell nuclei of 51 human irides and a series of monkey organs was demonstrated. In general, these substances are sensitive to testicular hyaluronidase and chondroitinase ABC and also to Streptomyces hyaluronidase, when using special staining methods. The specificity of testicular hyaluronidase was tested by inhibition with heparin. By simultaneously staining with alcian blue and Feulgen, acidic glycosaminoglycans can be distinguished from the nucleic acids. Sporadically, hyaluronidase-resistant substances with a specific acidic glycosaminoglycan stainability occur. We assume the existence of various acidic glycosaminoglycans in the cell nuclei. Aging changes were not traceable with constancy.
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PMID:Histochemical demonstration of acidic glycosaminoglycans in the cell nuclei of the iris and other tissues. 8 2

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

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


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