Topic
Keratan sulfate
About: Keratan sulfate is a research topic. Over the lifetime, 1253 publications have been published within this topic receiving 57984 citations. The topic is also known as: keratan sulfate & KS.
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TL;DR: The structure of the linkage region for keratan sulfate on corneal proteoglycans is clearly derived from a complex type of N-linked glycoprotein oligosaccharide precursor, indicating that only the oligosACcharides that have been processed to the complex type are used as primers for synthesizing keratan sulphate chains.
70 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: The data suggest that collagen fibrils interact with the KS-rich regions of several aggrecan monomers aligned within a proteoglycan aggregate, and the fibril could serve as a backbone in at least some of the Aggrecan complexes.
70 citations
TL;DR: 105KC represents the first model to have maintained the post-fetal chondrocytic proteoglycan phenotype in stable culture and sheds light on the biological characteristics of chondrosarcomas.
Abstract: Keratan sulphate is an integral component of the large aggregating proteoglycans of mature human articular cartilage. The keratan sulphate content of chondrocytic proteoglycans increases during maturation, and it is a useful marker of mature-type chondrocytic proteoglycans. Ordinarily, in cell culture, chondrocytes from non-neoplastic tissues dedifferentiate, diminish or cease to synthesize aggregating proteoglycans with the same amount of keratan sulphate as those formed in vivo, and do not maintain their in vivo phenotype. In tissue culture, this down-regulation of synthesis of keratan sulphate is irreversible. The study of the metabolism of mature human chondrocytes has been hampered by the absence of stable models. We report a cell-line, 105KC, derived from a human chondrosarcoma, that has maintained a stable proteoglycan phenotype during more than three years of culture. Analysis with immunofluorescence suggested that 105KC cells continued to synthesize keratan sulphate in long-term culture. Biochemical analysis demonstrated that 105KC cells maintained the production of chondrocytic large-aggregating proteoglycans and that keratan sulphate composed 13 per cent of their glycosaminoglycan content. To our knowledge, 105KC represents the first model to have maintained the post-fetal chondrocytic proteoglycan phenotype in stable culture. This study documents the feasibility of the development of mature chondrocytic cell-lines and sheds light on the biological characteristics of chondrosarcomas.
70 citations
Journal Article•
TL;DR: Histologic and histochemical evaluation of formalin-fixed segments of the cultured disks indicated that the chondrocytes proliferated in the implant, producing small groups and linear segments of cells by day 14, and Alcian blue-stained matrix was evident in the pericellular region of chond rocytes in sections of disks harvested on days 14, 18, and 22.
Abstract: Cartilage resurfacing by chondrocyte transplantation, using porous collagen matrices as a vehicle to secure the cells in cartilage defects, has been used experimentally in animals. This in vitro study evaluated the temporal morphologic features and proteoglycan synthesis of chondrocyte-laden collagen matrices. Forty-two porous collagen disks were implanted with a minimum of 6 x 10(6) viable chondrocytes, covered by a polymerized collagen gel layer, and 6 disks were harvested after 0, 3, 7, 10, 14, 18, or 22 days of incubation in supplemented Ham's F12 medium at 37 C and 5% CO2. Histologic and histochemical evaluation of formalin-fixed segments of the cultured disks indicated that the chondrocytes proliferated in the implant, producing small groups and linear segments of cells by day 14. The collagen framework remained intact over the course of the study with thick areas attributable to depositions of matrix material after day 10. Alcian blue-stained matrix was evident in the pericellular region of chondrocytes in sections of disks harvested on days 14, 18, and 22. Glycosaminoglycan (GAG) assay by dimethylmethylene blue dye binding after papain digestion of the disk segments revealed negligible amounts of GAG at day 0. Significant (P < or = 0.0001) increase in total GAG content was observed by day 3 (0.329 micrograms/mg of disk) and further increases were observed until a plateau in GAG quantity was seen on day 14. Mean peak GAG content was 0.553 +/- 0.062 micrograms/mg. Secondary treatment of the papain-digested implants with keratanase and chondroitinase ABC yielded similar trends in chondroitin sulfate (CS) and keratan sulfate (KS) concentrations.(ABSTRACT TRUNCATED AT 250 WORDS)
70 citations