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 disaccharide 2-acetamido-2-deoxy-β- d -glucopyranosyl-(1→3)- d -[1-3H]-galactitol, prepared from keratan sulfate, was rapidly hydrolyzed by the A and B isoenzymes of normal human liver hexosaminidase (EC 3.2.1.30), and by the B isozyme prepared from the liver of a patient who had died of Tay-Sachs disease as discussed by the authors.
5 citations
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TL;DR: The concentrations of keratan sulfates and unmodified keratan sulfur increased in the vertebral body growth plate in patients with idiopathic scoliosis and sulfation and acetylation of total glycosaminoglycans decreased.
Abstract: The concentrations of keratan sulfates and unmodified keratan sulfates increased in the vertebral body growth plate in patients with idiopathic scoliosis. Sulfation and acetylation of total glycosaminoglycans decreased by 50 and 30%, respectively. These changes reflect the decrease in biological activity of molecules that modulate function of the growth plate.
5 citations
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TL;DR: It is found that a highly sulfated KS disaccharide, L4, suppresses lung inflammation and is effective against COPD and its exacerbation in mouse models and chemically designed to create new ligands with higher affinity and activity.
5 citations
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TL;DR: The total GAG accumulation in the medium was much greater than that of the cell layer indicating that the cells are synthesizing relatively large amounts of GAGs, although incorporation of these macromolecules into the extracellular matrix was consistently low.
5 citations
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TL;DR: Keratan sulfate II was prepared from the proteolytic digest of pig nucleus pulposus proteoglycan and the amino acid sequence was deduced to be Ala-Pro-Ser- pro-Gly, which is different from those reported for the attachment sites of chondroitin sulfate on core proteins from various sources.
Abstract: Keratan sulfate II was prepared from the proteolytic digest of pig nucleus pulposus proteoglycan. The polysaccharide chains containing the fragment peptides of the core protein at their reducing terminal were subjected to anhydrous HF-solvolysis reaction and one of the glycopeptides from the keratan sulfate II-core protein linkage regions was isolated. The amino acid sequence of the peptide was deduced to be Ala-Pro-Ser-Pro-Gly, which is different from those reported for the attachment sites of chondroitin sulfate on core proteins from various sources. The results provided the first solid amino acid sequence for the keratan sulfate II-core protein linkage regions and suggested that the amino acid sequence of the core protein might determine the distribution of chondroitin sulfates and keratan sulfates along the core protein of the proteoglycan molecule.
5 citations