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

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.
 ...
PMID:Acidic glycosaminoglycans in human kidney tissue. 12 23

1) Chondroitin sulfate and dermatan sulfate of bovine arterial tissue exist as copolymers with a varying degree of hybridization between chondroitin and dermatan sulfates. A fraction rich in dermatan sulfate hybridized with 20% chondroitin sulfate (termed DS-rich hybrid) and a fraction rich in chondroitin sulfate containing 17% DS as copolymer constituent (CS-rich hybrid) can be isolated by the subfractionation of the arterial tissue CS-DS preparation. 2) When arterial tissue segments were preincubated with [14C]glucosamine, 95% of the radioactivity incorporated into the glycosaminoglycans was found to be present in the galactosamine moiety of all of the CS-DS subfractions, whereas the relative proportion of 14C radioactivity incorporated into the galactosamine and uronic acid components was 51:49 following preincubation with [14C]glucose. In both experiments the specific radioactivity of the DS-rich hybrids was twice as high as that of the CS-rich hybrids. 3) Enzymatic degradation of the hybrid CS-DS subfractions by chondroitin AC and ABC lyases revealed that the specific radioactivity of the CS and DS disaccharide units released from the DS-rich hybrids was twice as high as those isolated from the CS-rich hybrids, but within each hybrid fraction the galactosamine moieties of the CS and DS units and their glucuronic and iduronic acid components exhibited equal specific radioactivities. 4) The results strongly support the assumption that distinct compartments exist for the formation of hybrid CS-DS proteoglycans with different proportions of CS and DS.
 ...
PMID:Studies on the chemistry of arterial wall, XVII. Metabolic characteristics of different types of chondroitin sulfate-dermatan sulfate hybrids in arterial tissue. 121 69

The ultrastructural localization of glycosaminoglycans (GAGs) in the developing human outflow apparatus was investigated. The aqueous outflow system from human eyes at 26th and 36th fetal week and 2 years of age was stained with ruthenium red to identify GAGs with the transmission electron microscope. Luminal surface of the inner wall of the Schlemm's canal, basal lamina of the endothelial cells, basal lamina-like material, amorphous substances and collagen fibrils in juxta-canalicular tissue were associated with ruthenium red-stainable material. The basal lamina of the endothelial cells of Schlemm's canal was stained less obviously in 2-year-old trabecular tissue. The composition of the ruthenium red-stainable material was determined by treatment of each tissue with streptomyces hyaluronidase, chondroitinase AC, and chondroitinase ABC respectively. Hyaluronic acid was identified in each ruthenium red-stainable extracellular component. Chondroitin sulfate was identified in all ruthenium red-stainable components except luminal surface of the canal. The presence of dermatan sulfate was confirmed in the amorphous components and collagen fibrils of juxta-canalicular tissue. The results suggest that GAGs in fetal trabecular tissue already contribute to the outflow resistance and that alterations of the pattern of GAGs may take place as development proceeds.
 ...
PMID:[Demonstration of glycosaminoglycans (GAGs) in fetal human trabecular tissue]. 137 83

Chondroitin sulfate was examined in the extracellular matrix of the canine medial and lateral superior olivary nuclei by light and electron microscopic immunocytochemistry. The extracellular matrix around the large neurons was intensely stained with a monoclonal antibody recognizing D-glucuronic acid 2-sulfate----N-acetylgalactosamine 6-sulfate (D-unit) and this staining degree was remarkably reduced after chondroitinase ABC digestion. Neuronal cytoplasm, glial cells or capillaries in these nuclei were not stained with the monoclonal antibody. The results indicate the presence of disaccharide residue of D-glucuronic acid 2-sulfate----N-acetylgalactosamine 6-sulfate in the chondroitin sulfate proteoglycan of the extracellular matrix.
 ...
PMID:Chondroitin sulfate in the extracellular matrix of the medial and lateral superior olivary nuclei in the dog. 138 Aug 72

The structurally related type XII-like collagen molecules TL-A and TL-B were recently identified in fetal bovine epiphyseal cartilage and subsequently shown to be collagen types XII and XIV, respectively. By indirect immunofluorescent staining of cartilage using monoclonal antibodies to the NC3 domains of each molecule, it was shown that type XII collagen was present predominantly around cartilage canals, the articular surface, subperichondrial margins, and the perichondrium, was less so in the remaining cartilage matrix, and was absent from the growth plate region. In the permanent cartilage of trachea, type XII stained somewhat more intensely in the margins beneath the loose connective tissue. Type XIV collagen localized more uniformly throughout the articular cartilage and was also absent from the growth plate region, whereas in tracheal cartilage, its distribution was similar to type XII. We have characterized the structure of these cartilage molecules and compared them with those from fetal bovine skin. Extraction of cartilage with 1 M NaCl and differential NaCl precipitation yields a fraction enriched for these two collagens. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting with monoclonal antibodies to the large amino-terminal non-triple-helical domain, NC3, revealed the presence in cartilage of two forms of type XII collagen: type XIIB, the molecule previously identified in chick and bovine tissues, and type XIIA, a much larger form equivalent to the molecule recently identified in WISH-transformed epithelial cell culture medium (Lunstrum, G. P., McDonough, A. M., Marinkovich, M. P., Keene, D. R., Morris, N. P., and Burgeson, R. E. (1992) J. Biol. Chem. 267, 20087-20092). Digestion with bacterial collagenase shows that the increased mass is present in the NC3A domain. Additional purification by velocity sedimentation and observation of rotary-shadowed images demonstrates molecules with extended non-triple-helical arms approximately 80 nm in length analogous to the WISH cell molecules. Electrophoretic mobilities of bands corresponding to type XIIA, but not type XIIB, are sensitive to chondroitinase ABC, indicating that type XIIA is a chondroitin sulfate proteoglycan and that modification occurs predominantly within the NC3A domain distal to NC3B. Neither type XIIB from skin nor type XIIA from WISH cells are chondroitinase-sensitive. By similar analysis, a portion of the type XIV collagen chains in cartilage was also sensitive to chondroitinase digestion. Chondroitin sulfate is apparently not located on its NC3 domain. As in skin, collagen types XII and XIV have subtly different distributions within cartilage and type XII may have a tissue-specific structure.
 ...
PMID:Characterization of collagen types XII and XIV from fetal bovine cartilage. 140 Mar 27

Swarm rat chondrosarcoma cell cultures were metabolically labeled with [35S]sulfate, [3H]glucose, or [3H]glucosamine. Chondroitin sulfate chains were isolated from purified aggrecan using alkaline borohydride treatment and Superose 6 chromatography. Various linkage region oligosaccharide alditols were derived from these chains using sequential chondroitinase digestions (ABC lyase followed by ACII lyase). They were then further processed by mercuric acetate treatment, which removed the 4,5-unsaturated uronosyl residue from the nonreducing end of the linkage, and then beta-galactosidase digestion which liberated the 2 galactose residues from the xylitol reducing terminus. Alkaline phosphatase digestions were performed to verify the presence of phosphate esters. All linkage region structures were isolated and identified using a combination of Progel-TSK G2500 and CarboPac PA1 chromatography steps in conjunction with monosaccharide analyses. This study revealed that chondroitin sulfate chains from aggrecan synthesized by rat chondrosarcoma cells in vitro have the following properties: 1) three out of every four of their linkage regions carry a phosphate ester on xylose, 2) nearly three out of every five chains begin the repeating disaccharide region with an unsulfated first disaccharide unit, 3) nearly twice as many nonphosphorylated chains have a sulfated first disaccharide than their phosphorylated counterparts, and 4) the vast majority of these chains do not contain sulfated galactose in their linkage regions. This report also describes a borohydride reduction procedure to confer alkali stability to the 3-substituted, unsaturated disaccharides derived from chondroitinase digests of chondroitin sulfate. Furthermore, a CarboPac PA1 method is demonstrated that separates these reduced disaccharides with exceptional resolution.
 ...
PMID:Structural analysis of the linkage region oligosaccharides and unsaturated disaccharides from chondroitin sulfate using CarboPac PA1. 155 66

Monoclonal antibodies specific for unsulfated, 4-sulfated, and 6-sulfated disaccharide "stubs" that remain attached to the core protein after chondroitinase ABC digestion of chondroitin/dermatan sulfate proteoglycans have been used to study the localization of chondroitin and the two isomeric chondroitin sulfates in developing rat cerebellum. At 1-2 weeks postnatal, unsulfated chondroitin is present in the granule cell layer, molecular layer, and prospective white matter, but there was no staining of the external granule cell layer other than light staining of Bergmann glia fibers. By 3 weeks postnatal, staining of the molecular layer has disappeared and has diminished in the white matter, whereas in adult cerebellum only the granule cell layer remains stained. The staining pattern of chondroitin 4-sulfate is similar to that for chondroitin at 1-2 weeks postnatal, but in contrast to chondroitin, chondroitin 4-sulfate increases in the molecular layer at 3 weeks, and this becomes the most densely stained region of adult cerebellum. Chondroitin 6-sulfate is present predominantly in the prospective white matter of 1-2 week postnatal cerebellum, although significant staining of the granule cell layer is also seen. By 3 weeks postnatal the granule cell staining of chondroitin 6-sulfate has decreased, and in adult cerebellum staining is seen only in the white matter and to a lesser extent in the granule cell layer. Electron microscopy confirmed the presence of chondroitin sulfate in the cytoplasm of neurons and glia of adult brain.(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:Immunocytochemical localization of chondroitin and chondroitin 4- and 6-sulfates in developing rat cerebellum. 170 39

The chondroitin sulphate chains of proteoglycans are not uniformly sulphated. Commonly, regions of under- and over-sulphation are found. It is probable that variability in chondroitin sulphation has physiological significance, although such structure-function relationships largely remain unexplored. Chondroitin sulphate from rat chondrosarcoma proteoglycan has been found to possess no oversulphated residues. It is primarily chondroitin 4-sulphate, although a significant proportion of unsulphated disaccharides (14%) are also present. It appears that some unsulphated disaccharides are concentrated only at the point of attachment to the linkage region (i.e. it is the major unsaturated disaccharide remaining attached to chondrosarcoma proteoglycan core produced by chondroitinase ABC digestion). This proteoglycan core binds monoclonal antibody (MAb) 3B3. Although 3B3 principally binds to 6-sulphated 'stubs' of proteoglycan cores [Couchman, Caterson, Christner & Baker (1984) Nature (London) 307, 650-652], given a high concentration of unsulphated 'stubs', it can alternatively bind to these residues. It is also evident that caution must be exercised in using MAb 3B3 to identify chondroitin 6-sulphated proteoglycans.
 ...
PMID:An unsulphated region of the rat chondrosarcoma chondroitin sulphate chain and its binding to monoclonal antibody 3B3. 189 87

Soluble chondroitin sulfate proteoglycans (CSPGs), prepared from 10-d-old rat brain, were added to the culture medium of PC12D cells containing NGF to examine the effects on NGF-induced neurite outgrowth from the cells. PC12D cells, a flat-shaped variant of PC12 pheochromocytoma cells, are characteristic of prompt neurite formation in response not only to NGF, but also to cAMP-enhancing reagents such as forskolin. Brain CSPGs inhibited the neurite elongation irreversibly in a dose-dependent manner; complete inhibition was observed at a concentration of 50 nmol uronic acid/ml. Closely similar dose-dependent inhibition was observed in the forskolin-induced neurite outgrowth from PC12D cells. NGF-induced neurite outgrowth from conventional PC12 cells was also inhibited completely by 50 nmol uronic acid/ml CSPGs. Some brain CSPGs seemed to be inhibitory, but the cartilage-unique CSPG did not show any inhibitory effect. Chondroitin sulfate, a polysaccharide moiety of CSPGs, did not show any inhibitory effect even at a concentration of 250 nmol uronic acid/ml, while core proteins prepared from brain CSPGs by digestion with chondroitinase ABC exhibited inhibitory activity similar to that of intact CSPGs. This indicates that the site of the inhibitory activity exists in the core protein moiety of brain CSPGs. From these observations, it is conceivable that brain CSPGs are involved in the regulation of neuronal differentiation.
 ...
PMID:Inhibitory effects of brain chondroitin sulfate proteoglycans on neurite outgrowth from PC12D cells. 200 62

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.
 ...
PMID:Histological localization of myxoid tissue in normal human palatal mucosa and its glycosaminoglycans. 244 96


1 2 3 4 5 6 7 8 9 10 Next >>