Showing papers on "Keratan sulfate published in 1979"
TL;DR: A new rapid, sensitive, and reproducible method is presented which allows the separation of all known animal glycosaminoglycans in a single monodimensional electrophoresis on cellulose acetate.
185 citations
TL;DR: The analyses indicate that the proteoglycans synthesized by corneas in organ culture were similar to, if not identical with, their counterparts in the stroma although they are synthesized in different prportions in vitro than they acumulate in vivo.
137 citations
TL;DR: The data suggest that stage 23 to 24 mesenchyme cells undergo normal chondrogenic maturation in culture in the presence of xylosides even though most of the polysaccharides are synthesized onto the exogenously supplied xylOSide substrate and released into the medium, which is abnormal in general morphology.
99 citations
TL;DR: Proteoglycans of calf and steer articular cartilage were studied with a view of assessing structure and changes occurring as a result of the aging process and showed a maturation-related decrease in chondroitin sulfate content and an enrichment in keratan sulfate chains in both the chondrodynamically larger and smaller keratan sulphate-rich regions.
97 citations
TL;DR: It is concluded that the structural integrity of the proteoglycan macromolecule is essential for its effect on cell adhesion.
Abstract: Proteoglycan was isolated from cartilage and freed from contaminating glycoproteins and hyaluronic acid. The macromolecule consists of a protein core covalently linked to a number of glycosaminoglycan side chains, namely chondroitin sulphate and keratan sulphate. This proteoglycan retards the attachment of a variety of cell types to tissue culture plastic and to collagen. Glycosaminoglycans alone, have no significant effect on rates of attachment. Similarly, trypsinized proteoglycan is without effect. It is concluded that the structural integrity of the proteoglycan macromolecule is essential for its effect on cell adhesion.
95 citations
TL;DR: Human articular cartilage was obtained post mortem from the lateral femoral condyles of 30 subjects aged from under 1 to 70 years and changes with age were observed in GAG concentration and in the proportion of individual GAG.
Abstract: Human articular cartilage was obtained post mortem from the lateral femoral condyles of 30 subjects aged from under 1 to 70 years. Cryostat sections taken 0--100 micrometers and 900--100 micrometers deep to the cartilage surface were exhaustively extracted to recover the glycosaminoglycans (GAG). After fractionation by cellulose acetate electrophoresis and enzyme depolymerisation individual GAG were determined by alcian blue -0.05 M MgCl2 and disaccharide microassay procedures. Changes with age were observed in GAG concentration and in the proportion of individual GAG. Large alterations occurred during the period of skeletal growth (0--16y). At birth GAG formed about 50% of the dry weight of cartilage, a value that decreased to about 15% in adult cartilage. Chondroitin sulphates (ChS) formed the principal GAG of articular cartilage and accounted for almost all of the GAG of the infant material. The ChS decreased with age and were partially replaced by keratan sulphate (KS), so the KS eventually comprised 12% of the GAG. Hyaluronic acid (HA) was identified and was found to increase linearly with age to form 6% by weight of the cartilage GAG by 60y.
70 citations
TL;DR: Both changes in the solubility of collagen as well as in the distribution pattern of the glycosaminoglycans seem to be related to cervical dilatation.
68 citations
TL;DR: Changes in composition could lead to alterations in the proportion and size of the aggregates they form in the cartilages, furnishing the conditions for the processes of growth and calcification to occur.
Abstract: The structure of chondroitin sulfates and proteoglycans extracted from human normal young and adult cartilages and also from human arthrosic cartilages are reported. The adult articular cartilage contains almost exclusively chondroitin 6-sulfate, whereas the normal young and the arthrosic cartilage chondroitin sulfates are hybrid polymers, containing 4-sulfated and 6-sulfated disaccharide units, distributed in a quite random way along the molecules. The young cartilage proteoglycans also differ from the adult cartilage proteoglycans by their contents of keratan sulfate, the relative proportion of nonaggregating proteoglycans and electrophoretic migration in agarose gel slabs. The proteoglycans from arthrosic cartilages are very similar to those from young normal cartilages. Such changes in composition could lead to alterations in the proportion and size of the aggregates they form in the cartilages, furnishing the conditions for the processes of growth and calcification to occur.
42 citations
TL;DR: This study shows that the keratan sulfate type repeating unit is also present in the neutral glycosphingolipids of bovine erythrocyte membranes.
38 citations
TL;DR: Chondro-osseous tissue from four patients with the Kniest dysplasia was studied histochemically using a new plastic embding technique and suggests that there may be a defect in the synthesis, structure, or secretion of a major cartilage matrix component which leads to its accumulation in the chondrocyte rough endoplasmic reticulum.
Abstract: Summary: Chondro-osseous tissue from four patients with the Kniest dysplasia was studied histochemically using a new plastic embding technique. Extensive vacuolar changes were observed p-1 throughout the endochondral growth plate and adjacent resting cartilage. These changes occurred within the cartilage matrix and also in the lacunae of degenerating chrondrocytes. The septa of the lesions contained chondroitin sulfate, but little keratan sulfate or collagen. Resting cartilage not adjacent to the growth plate stained irregularly and showed few of the vacuolar lesions, and chondrocytes were enlarged and contained cytoplasic inclusions, but no vacuolar material. Thus, there appears to be a sequence of events initiated by cellular accumulation of a substance and progressing to cellular and matrix degeneration. Speculation: The findings suggest that there may be a defect in the synthesis, structure, or secretion of a major cartilage matrix component (e.g, proteoglycan, collagen) which leads to its accumulation in the chondrocyte rough endoplasmic reticulum. Both cellular and matrix degeneration subsequently occur either due to a toxic effect of this material or to the absence of the normal molecule.
33 citations
TL;DR: Results taken together with those previously obtained from studies on human fibroblast cultures suggest that normal skin fibroblasts contain at least five specific sulfatases and diminished activity of any one may result in a specific storage disease.
Journal Article•
TL;DR: The electrophoretic pattern and keratan sulfate content in these proteoglycans from adult cartilage are clearly distinct from those of the young and tumoral cartilages.
Abstract: Differences in the glycosaminoglycans and proteoglycans synthesized by "young," "adult," and tumoral chondrocytes are reported. Young cartilage and human chondrosarcoma contain chondroitin 4- and 6-sulfates, whereas adult human cartilage contains almost exclusively chondroitin 6-sulfate. High keratan sulfate content is reported in adult cartilage, whereas it is almost absent in young and tumoral cartilages. The electrophoretic pattern and keratan sulfate content in these proteoglycans from adult cartilage are clearly distinct from those of the young and tumoral cartilages. The high molecular weight is the distinguishing property of the glycosaminoglycan synthesized by tumoral chondrocytes.
TL;DR: The synthesis of proteoglycan aggregates could, however, be partly restored by transfer of the monolayer cells to a suspension culture, and the production of small-sized “ubiquitous proteoglycans” was found.
TL;DR: It is suggested that in bovine tissues a single galactosyltransferase participates in the synthesis of both high and low molecular weight Galactosides including the assembly of the repeating disaccharide of cornea keratan sulfate.
TL;DR: Proteoglycan was isolated from a human chondrosarcoma which contained all glycosaminoglycans found in articular cartilage, and two forms of keratan sulfate were identified following treatment with alkaline borohydride.
TL;DR: Glycosaminoglycan content, composition and molecular weight were determined in liver obtained from a patient with Morquio syndrome (Mucopolysaccharidosis IV) as compared to the control liver.
TL;DR: Cartilaginous and/or osseous foci were observed in eight aortas from 20 rabbits immunized against heterologous aorta homogenates and sacrificed 11 to 24 months later and some of the observed changes seemed to be true markers of these transformations.
Abstract: Cartilaginous and/or osseous foci were observed in eight aortas from 20 rabbits immunized against heterologous aorta homogenates and sacrificed 11 to 24 months later. They were studied by means of histological and histochemical methods and compared with normal aortas, cartilage and bone. Some of the observed changes seemed to be true markers of these transformations. Chondroid metaplasia was characterized by 1) generalized increase in alcianophilic hyaluronidase sensitive substances. 2) Appearance of Dermatan and/or Keratan sulfates round some isolated cells. 3) Advent of G6Pase and Alk.Phase activities in cells adjacent to osseous foci. Osteous metaplasia was characterized by 1) decrease, then disappearance of alcianophilic and PAS positive material, 2) increase in osteoblastic alkaline Pase-activities.
TL;DR: The present data suggest that the remodeling of proteoglycan consumption of glycogen in bovine costal cartilage occur on calcification, and the relative content of chondroitin sulfate decreases with a concomitant increment in that of keratan sulfate on calcifying.
Abstract: Carbohydrate-containing substances were extracted from non-calcified (NCC) and calcified (CC) portions of bovine costal cartilage with 0.5 M LaCl3 by the method of Mason and his co-workers, followed by dilution of the extract with 9 volumes of water. The precipitate formed on dilution yielded Fr. P, while Fr. S was obtained from the supernatant. Fr. P was separated into two subfractions by gel filtration on Sepharose 2B. The experimental results showed that Fr. P contained proteoglycans with different molecular sizes and compositions, while Fr. S contained proteoglycan, hyaluronic acid, glycoproteins, and glycogen. The present data suggest that in the proteoglycan of Fr. P, the relative content of chondroitin sulfate decreases with a concomitant increment in that of keratan sulfate on calcification. In addition, elevation of the ratio of chondroitin 4-sulfate to chondroitin 6-sulfate, together with a small increment of non-sulfated disaccharide units in the chondroitin sulfate chains appear to occur on calcification. The glycogen content in Fr. S diminished on calcification. The present observations suggest therefore that the remodeling of proteoglycan consumption of glycogen in bovine costal cartilage occur on calcification.
Journal Article•
TL;DR: The human intervertebral discs which were obtained by cadavers and anterior discectomy are investigated histochemically and there was no histologically and histochemical observable difference in the cervical and lumbar discs.
Abstract: The human intervertebral discs which were obtained by cadavers and anterior discectomy are investigated histochemically. Chondroitin-4S, chondroitin-6S, dermatan sulfate, hyaluronic acid and keratan sulfate were detected in the human intervertebral disc by various histochemical methods. pH2.5, pH1.1 toluidin blue metachromasia and 0.4M MgCl2 alcianophilia became weaker with increasing age, and the herniated disc were weaker than controlled discs in the same age group. Chondroitin-4S and chondroitin-6S were distributed throughout the discs. There was no clear localization of the various glycosaminoglycans in the human intervertebral disc, with the exception of keratan sulfate. There was no histologically and histochemically observable difference in the cervical and lumbar discs.
TL;DR: Keratan sulfate-rich peptides were isolated after digestion of proteoglycans from bovine nasal cartilage and bovines nucleus pulposus with chondroitinase ABC, trypsin and chymotrypsin.
TL;DR: The results seem to indicate that the biosynthesis of keratan sulfate has some relation to that of chondroitin 6-sulfate.
Abstract: Biosynthesis of chondroitinase-resistant glycosaminoglycans as minor components was studied in the cartilages of chick embryos and of newborn chickens and rats Sternal and knee cartilages were labeled in vitro with35SO
4
2−
, and then35S-labeled glycosaminoglycans were analyzed In rats up to 2 weeks old, only one glycosaminoglycan could be detected as heparan sulfate In the chick embryos and the newborn chickens, however, keratan sulfate as well as heparan sulfate could be detected As chondroitinase-sensitive glycosaminoglycans, large amounts of both chondroitin 4- and 6-sulfates were synthesized in the chick cartilage, but the synthesis of chondroitin 6-sulfate could scarcely be seen in the rat cartilage The results seem to indicate that the biosynthesis of keratan sulfate has some relation to that of chondroitin 6-sulfate
01 Jan 1979
01 Jan 1979
TL;DR: On sequential extraction of bovine corneas with 0.155 M NaCl and 1 M CaCl2 two macromolecular fractions were obtained in a ratio of 0.7–1.5, both containing glycosa-minoglycans and a hexosamine containing non-glycosaminoglycan subfraction.
Abstract: On sequential extraction of bovine corneas with 0.155 M NaCl and 1 M CaCl2 two macromolecular fractions were obtained in a ratio of 0.7–1.5, both containing glycosa-minoglycans and a hexosamine containing non-glycosaminoglycan subfraction.
01 Jan 1979
TL;DR: In this paper, the authors investigated the possibility that the enzyme in the prospositus could be a sulfatase specific for 6-sulfated substrates having the D-glucose configuration, whose deificiency might be responsible for the accumulation of keratan sulfate and chondroitin 6sulfate in Morquio disease.
Abstract: Publisher Summary Propositus is affected by a mucopolysaccharidos different from those already known and possibly caused by the deficiency of an enzyme normally participating in the degradation of keratan and heparan sulfate. In fact, the clinical and radiological features of the propositus represent an association of findings typical of diseases in which heparan sulfate or keratan sulfate accumulate. As acetylglucosamine 6-sulfate is the only functional group common to the repeating units of heparan and keratan sulfate, possibility that the enzyme in the prospositus could be a sulfatase specific for 6-sulfated substrates having the D-glucose configuration has been considered. This hypothesis requires the assumption that at least another sulfatase must exist, specific for 6-sulfated substrates having the D-galactose configuration, whose deificiency might be responsible for the accumulation of keratan sulfate and chondroitin 6-sulfate in Morquio disease. This chapter describes a study to verify these hypotheses in which N-acetyl-glucosamine 6-sulfate, N- acetylgalactosamine 6-sulfate, and galactose 6-sulfate using chlorosulfonic acid, according to the method of Suzuki and Strominger, were synthesized.
01 Jan 1979
TL;DR: The epithelium appears to have a decisive influence on its synthesis, which may be of regulatory character and the destruction of the fibrillary character of the stroma by CaCl 2 does not take place, at least not to the same extent as in de-epithelialyzed swollen corneas.
Abstract: Publisher Summary This chapter defines the incorporation of glucosamine glycosaminoglycans and the influence of corneal epithelium. Multiple extractions of de-epithelialized, minced, or homogenized bovine corneas with 0.15 M NaCl can remove up to 80% of the extractable hexosamine (HexN) without any morphologic effect on either the collagen fibers or lamellar organization. Subsequent extraction of up to 95% of the remaining HexN with 1.0 MCaCl 2 (pH 8) led to disruption of the mature banded-collagen fibers leaving short dense fibrils embedded in a material having the density and fine fibrillar structure of basal lamina. Both extractions produced keratan sulfate (KS) and chondroitin 4-sulfate (C-4-S) in ca. 2:1 ratio and a certain amount of glycoprotein. These experiments are undertaken to investigate the phenomenon and to study the possible influence of the corneal epithelium in the process. The epithelium appears to have a decisive influence on its synthesis, which may be of regulatory character. The destruction of the fibrillary character of the stroma by CaCl 2 does not take place, at least not to the same extent as in de-epithelialyzed swollen corneas. This indicates that this disruption of the fibril structure is not the primary effect of CaCl 2 .
01 Jan 1979