Showing papers on "Keratan sulfate published in 1982"
TL;DR: This monodimesional electrophoresis method is suitable for routine screening of large numbers of samples to provide a guide to the nature of the enzyme deficiency in the mucopolysaccharidoses.
124 citations
TL;DR: The glycosaminoglycans of the normal human and bovine lungs and of the major structural components of these organs (pleura, 'alveoli', peripheral and central bronchi, arteries and veins) were investigated and significant changes in the mucopolysaccharide levels were found during maturation and aging.
45 citations
TL;DR: Results suggest that antibodies against corneal keratan sulfate proteoglycan may include some that react with the keratan sulphate chains, as well as those directed against the core protein.
44 citations
TL;DR: From the products obtained after digestion with various mutant fibroblasts and with purified N-acetylgalactosamine 6-sulphate sulphatase, it is suggested that [35S]sulPHate is released almost exclusively from galactose 6- sulphates residues.
Abstract: Upon incubation of keratan [35S]sulphate with normal fibroblasts both [35S]sulphate and N-acetylglucosamine 6-[35S]sulphate are liberated. From the products obtained after digestion with various mutant fibroblasts and with purified N-acetylgalactosamine 6-sulphate sulphatase we suggest that (i) [35S]sulphate is released almost exclusively from galactose 6-sulphate residues; (ii) N-acetylgalactosamine 6-sulphate sulphatase exhibits galactose 6-sulphate sulphatase activity; (iii) both sulphatase activities are deficient in Morquio disease type A.
40 citations
TL;DR: Six mouse hybrid cell lines were isolated which secrete antibodies which appear to recognise a carbohydrate structure found only on corneal keratan sulfate proteoglycan, which can serve as a basis for separation of corneals types using antibody affinity chromatography.
Abstract: Six mouse hybrid cell lines were isolated which secrete antibodies to rabbit corneal proteoglycan. All six antibodies interacted with the same fraction of the proteoglycan, precipitating approximately 50% of proteoglycan labelled in the protein moiety. A radioimmunoassay using these antibodies measured concentrations as low as 1 g/m1 unlabelled rabbit corneal proteoglycan. Human corneal proteoglycanj corneal keratan sulfate, and an oligosaccharide fraction from corneal digests all interacted with the antibodies at concentrations similar to whole rabbit proteoglycan. Proteoglycans from cultured rabbit stromal fibroblasts and from sclera were 20 to 50-fold less effective in competition for antibody. Endo-β-galactosidase treatment of proteoglycan reduced antibody binding, but protease or chondroitinase treatments did not. Labelled proteoglycan separated by antibody affinity chromatography contained only keratan sulfate, whereas proteoglycan not bound to affinity columns contained only chondroitin sulfate. Th...
26 citations
TL;DR: Two proteoglycans isolated from the femurs of quail actively producing medullary bone were separated using DEAE Bio-Gel A and apparently only the keratan sulfate proteoglycan is associated with the new medullARY bone matrix.
Abstract: 1. 1. Two proteoglycans isolated from the femurs of quail actively producing medullary bone were separated using DEAE Bio-Gel A. 2. 2. The first to elute in the gradient was a keratan sulfate proteoglycan with an average buoyant density of 1.53 g/ml and a K av = 0.57 on Sepharose CL-4B. 3. 3. The second proteoglycan to elute contained chondroitin 4-sulfate. 4. 4. Apparently only the keratan sulfate proteoglycan is associated with the new medullary bone matrix.
26 citations
Journal Article•
TL;DR: Investigation of the role of osteoclasts or chondroclasts in degradation and synthesis of complex carbohydrates indicates that the dissolution of sulfated glycoconjugates requires osteoclastic engulfment of degraded material and subsequent intracellular digestion, whereas the dissolved collagen fibrils appears to be completed extracellularly.
24 citations
TL;DR: The influence of exogenously-added glycosaminoglycans and glycoproteins on DNA synthesis in isolated nuclei, from normal and malignant tissues, was investigated and heparin inhibitedDNA synthesis in both normal and tumor cell nuclei.
23 citations
TL;DR: The preliminary analyses showed that the chondroitin sulphate from the acetabular cartilage contained exclusively 6-sulphated disaccharide units and there was some heterogeneity in keratan sulphate.
Abstract: The distribution of glycosaminoglycans (GAGs) in different functional regions (weight-bearing and nonweight-bearing portions) of the human hip joint cartilage was studied. The results obtained were as follows: (1) Weight-bearing cartilage contains larger amounts of GAGs than nonweight-bearing, cartilage. (2) Weight-bearing cartilage contains keratan sulphate in higher ratio to chondroitin sulphate than nonweight-bearing cartilage. (3) The differences in content and composition of GAGs between the weight-bearing and nonweight-bearing portions are more pronounced in the femoral head than in the acetabulum. The preliminary analyses showed that the chondroitin sulphate from the acetabular cartilage contained exclusively 6-sulphated disaccharide units and there was some heterogeneity in keratan sulphate.
19 citations
01 Jan 1982
16 citations
TL;DR: There was a striking deficiency of galactose 6-sulfate sulfatase activity in the cultured skin fibroblasts of patients with Morquio syndrome, which could be explained by the hypothesis that accumulation of keratan sulfate and chondroitin 6-Sulfate in MorquIO syndrome is due to a deficiency of Galactose6-solfate sulf atase and N-acetylgalactosamine 6-methine 6- sulfate
TL;DR: Human teratocarcinoma-derived cells of line PA 1, which are capable of differentiating in vitro, incorporate label from radioactive sulfate and/or glucosamine into several large-sized glycosaminoglycans including hyaluronate, chondroitin sulfate/dermatan sulfate co-polymers, heparan sulfates and keratan-sulfate-like molecules, which were identified by specific degradation methods.
Abstract: Human teratocarcinoma-derived cells of line PA 1, which are capable of differentiating in vitro [Zeuthen, J. et al. (1980) Int J. Cancer, 25, 19-32], incorporate label from radioactive sulfate and/or glucosamine into several large-sized glycosaminoglycans including hyaluronate, chondroitin sulfate/dermatan sulfate co-polymers, heparan sulfate and keratan-sulfate-like molecules. All these polysaccharide fractions were identified by specific degradation methods. The labeled hyaluronate was degraded into a mixture of unsaturated octa-, hexa- and tetra-saccharides by a treatment with Streptomyces hyaluronidase (EC 4.2.2.1). The chondroitin sulfate/dermatan sulfate co-polymers were cleaved with chondroitin AC lyase (EC 4.2.2.5) into unsaturated disaccharides and a series of unsaturated oligosaccharides; the latter were degraded by a treatment with chondroitin ABC lyase (EC 4.2.2.4) into unsaturated disaccharides. Heparan sulfate was degraded with nitrous acid into free inorganic [35S]sulfate and a series of [35S]sulfate-labeled oligosaccharides and/or glycopeptides. The keratan-sulfate-like molecules were hydrolyzed by a treatment with endo-beta-galactosidase from Escherichia freundii into a series of distinct [35S]sulfate-labeled oligosaccharides; small oligosaccharides were liberated also from [3H]galactose-labeled molecules. The smallest one of the liberated oligosaccharides was tentatively identified as a sulfated disaccharide.
TL;DR: In the region of the aortic arch the concentration and the relative proportion of hyaluronate, dermatan sulfate and chondroitin 4-sulfat decrease on ageing, whereas those of heparan sulfates, keratan sulfates and chonroitin 6-Sulfate increase, and in the middle region of human aortae only keratan sulphate andChondroit in 4^sulfate increases with age.
Abstract: The glycosaminoglycans in human aortae between the 2nd and the 8th decade of age consist chiefly of chondroitin 4-sulfate (20-30%), chondroitin 6-sulfate (20-29%) and heparan sulfate (18-27%), followed by dermatan sulfate (13-17%), hyaluronate (5-15%), keratan sulfate (4-8%) and chondroitin (1-3%). The concentrations of chondroitin 6-sulfate and heparan sulfate decrease from the 2nd to the 8th decade, whereas the concentration and relative proportion of keratan sulfate increase especially from the 6th to the 8th decade. With regard t the longitudinal distributions of the glycosaminoglycans in human aortae the 4th and the 8th decade of age were studied. The total glycosaminoglycan concentration of the younger group exhibits an increase from proximal to distal regions, whereas in the older group the glycosaminoglycan concentration remains nearly constant in all Segments, beirig higher in the aortic arch and lower in the two distal regions than in the corresponding regions of younger aortae. In the region of the aortic arch the concentration and the relative proportion of hyaluronate, dermatan sulfate and chondroitin 4-sulfat decrease on ageing, whereas those of heparan sulfate, keratan sulfate and chondroitin 6-sulfate increase. In the middle region of human aortae only keratan sulfate and chondroitin 4^sulfate increase with age. In the region of the bifurcatio, where the highest deposition of inorganic material has been found, Contents and relative proportions of hyaluronate, Jceratan sulfate and dermatan sulfate iiicrease during ageing, whereas those of heparan sulfate and the chondroitin sulfates, especially chondroitin 6-sulfate, decrease.
01 Jan 1982
TL;DR: Various roles are considered for proteoglycans in the mechanisms of mineralization of cartilage matrix and osteoid during endochondral bone formation.
Abstract: The structures and functions of proteoglycans are discussed, emphasizing those from cartilage. Various roles are considered for proteoglycans in the mechanisms of mineralization of cartilage matrix and osteoid during endochondral bone formation.
Journal Article•
TL;DR: Using a new radiolabeled substrate from shark cartilage keratan sulfate, it was found that there was a striking deficiency of β-galactosidase activity in the cultured skin fibroblasts of patients with GM1-gangliosidosis.
Journal Article•
TL;DR: This paper is the first report to demonstrate the presence of keratan sulfate in skin tissue, which is especially abundant in the skin, cornea, and caudal fin of Pacific mackerel, and in the cornea of horse Mackerel.
Abstract: A new method for the detection of keratan sulfate in connective tissue has been developed without its prior isolation from a mixture of glycosaminoglycan. The method relies on the specificaction of an endo-β-galactosidase from Flavobacterium sp. on keratan sulfate. Besides being found in mammals, keratan sulfate is widely distributed in the connective tissues of teleost; it is especially abundant in the skin, cornea, and caudal fin of Pacific mackerel, and in the cornea of horse mackerel. From the skin of Pacific mackerel, a crude preparation of polysaccharide was obtained, which contained a large amount of carbohydrate chains susceptible to endo-β-galactosidase. The fraction with the carbohydrate chains was isolated by treating the preparation with hyaluronidase and chondroitinase ABC. The purified substance was characterized using chemical and infrared spectrum analyses, and was indentified as keratan sulfate. This paper is the first report to demonstrate the presence of keratan sulfate in skin tissue.
TL;DR: The results strongly suggested that the keratan sulfate of bovine cornea contains three mannose residues per chain, as an integral component of the linkage region to protein.
Abstract: After exhaustive digestion of bovine corneas with a protease, keratan sulfate fractions of different chain length were obtained by ethanol fractionation on a cellulose column, followed by ion-exchange column chromatography. Compositional analysis of these fractions showed that aspartic acid is the predominant amino acid and that the keratan sulfate in each fraction contains aspartic acid and mannose in the molar ratio of 1:3. Molecular weights of these fractions, estimated by gel chromatography, were close to the calculated values based on the molar ratios of the components to three moles of mannose. The results strongly suggested that the keratan sulfate of bovine cornea contains three mannose residues per chain, as an integral component of the linkage region to protein.