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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19 Jul 2000
TL;DR: An IL-12 production inhibitor which comprises, as an active ingredient, a keratan sulfate oligosaccharide or a derivative thereof, for example, a karatin sulfate OGS comprising at least one repeating unit of either one of the disaccharides represented by the following formulas: Gal(6s)-GlcNAc (6s) and Gal( 6s)-GalNAc as mentioned in this paper, where Gal represents a galactose residue, Glc NAc represents an N-acetylglucosamine residue, 6s indicates that 6
Abstract: An IL-12 production inhibitor which comprises, as an active ingredient, a keratan sulfate oligosaccharide or a derivative thereof, for example, a keratan sulfate oligosaccharide comprising at least one repeating unit of either one of the disaccharides represented by the following formulas: Gal (6s)-GlcNAc (6s) and Gal (6s)-GlcNAc wherein Gal represents a galactose residue, GlcNAc represents an N-acetylglucosamine residue, 6s indicates that 6-0-sulfate ester is formed at a Hydroxyl group at the 6-position, and - represents a glycosidic linkage.
7 citations
TL;DR: Using synovial fluid of individuals with osteoarthritis as a prototypic biologic fluid containing one part proteoglycan per 100 to 1000 parts of other protein, profiles of proteoglycans were produced without preliminary purification through agarose-acrylamide gel electrophoresis, transfer to nitrocellulose, and triple immunoblotting.
7 citations
TL;DR: The data so far obtained on this part of the cornea keratan sulfate show that it is heterogeneous and contains besides the terminal glucosamine, mannose and fucose in a similar ratio as found in undegraded keratan sulphate.
Abstract: We present a defined chemical method for the isolation of the oligosaccharide linking the protein to the disaccharide units of keratan sulfate from bovine corneas. 1) Hydrazinolysis removes the amino acids from the peptido keratan sulfate, and leads to deacetylation of the glucosamine residues but does not split off the sulfate groups. 2) NaB3H4 reduction selectively labels the reducing terminal glucosamine of the chain by converting it to [3H]glucosaminitol. 3) Nitrous acid deamination splits the glycosidic bonds of glucosamine and converts this sugar into 2,5-anhydromannose but also leads to several derivatives of the free terminal [3H]glucosaminitol. 4) Na12CN treatment stabilizes the reactive 2,5-anhydromannose and the terminal compounds containing aldehyde groups in a cyanhydrin reaction. 5) The oligosaccharide structure between the glucosamine residue at the reducing end and the first glucosamine of the disaccharide chain is not degraded by this procedure and is obtained intact and in labelled form. The data so far obtained on this part of the cornea keratan sulfate show that it is heterogeneous and contains besides the terminal glucosamine, mannose and fucose in a similar ratio as found in undegraded keratan sulfate. The predominant compound probably contains three neutral sugar residues.
7 citations
TL;DR: Chondroitin sulfates from bovine nasal septum and lamprey cartilage and keratan sulfate from human costal cartilage show a wide molecular size polydispersity by acrylamide gel electrophoresis, which indicates that the polysaccharides are probably distributed in a continuum of varying chain lengths.
7 citations
01 Jan 2005
TL;DR: This chapter reviews current knowledge of the 6-O-HS endosulfatase (Sulf) enzymes, including their unique structural and enzymatic properties as novel extracellular heparin and keratan sulfate chains, and their roles as well as therapeutic applications in the control of tumor growth and angiogenesis.
Abstract: Publisher Summary This chapter reviews current knowledge of the 6-O-HS endosulfatase (Sulf) enzymes, including their unique structural and enzymatic properties as novel extracellular heparan endosulfatases, their regulatory functions in extracellular HS-dependent Wnt and fibroblast growth factors (FGF) signaling in stem cell progenitors, and their roles as well as therapeutic applications in the control of tumor growth and angiogenesis. Conservation of the hydrophilic domain (HD) sequence in association with catalytic and C-terminal domains has enabled identification of Sulf proteins in vertebrates and invertebrates. Sulf enzymes are functionally distinct from other sulfatases, including GlcNR6Sase, in their restricted expression in stem cells, their localization on the cell surface, and their substrate specificity and activity as heparan sulfate (HS)-specific 6-O-endosulfatases. The cell surface localization of Sulf on expressing cells suggests its cell autonomous function. Sulfs were predicted to act on GlcN 6-O-sulfate residues in HS based on their sequence homology with lysosomal GlcNR6Sase, an exoenzyme that removes 6-O-sulfate groups from the nonreducing-terminal GlcN residue of HS, heparin (HP), and keratan sulfate chains.
7 citations