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: In this paper, the authors show that mice lacking a functional fibromodulin gene exhibit an altered morphological phenotype in tail tendon with fewer and abnormal collagen fiber bundles, and they demonstrate that the orchestrated action of several leucine-rich repeat glycoproteins/proteoglycans influence the architecture of collagen matrices.
434 citations
TL;DR: It is suggested that HCII is the only thrombin inhibitor in human plasma that can be activated by dermatan sulfate.
428 citations
TL;DR: Experiments with aggregate preparations reconstituted from mixtures with [3H]acetylated or unlabeled proteoglycans showed that the larger protein fraction is derived from a portion of the protein in the proteoglycan monomer molecules while the smaller isderived from one of the small molecular weight "link proteins" that are present in proteogly can aggregate preparations.
415 citations
TL;DR: It is concluded that the release of aggrecan fragments from articular cartilage into the synovial fluid seen at all stages of human osteoarthritis is promoted by the action of a normal cartilage proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain.
Abstract: Synovial fluid was collected from patients with recent knee injury and from patients with early or late stage osteoarthritis. Chondroitin sulfate-substituted aggrecan fragments present in these fluids, and in normal bovine synovial fluid, were purified by cesium chloride gradient centrifugation, enzymically deglycosylated and fractionated by gel filtration on Superose-12. Each sample contained two major aggrecan core protein populations with apparent molecular masses of ∼ 90 kD and 150 kD. For all samples, NH2-terminal analysis of both populations gave a single major sequence beginning ARGSV. This NH2 terminus results from cleavage of the human aggrecan core protein at the Glu 373-Ala 374 bond within the interglobular domain between the G1 and G2 domains. Cleavage at this site also occurs during control and interleukin-1 stimulated aggrecan catabolism in bovine cartilage explant cultures (Sandy, J., P. Neame, R. Boynton, and C. Flannery. 1991. J. Biol. Chem. 266:8683-8685). These results indicate that the major aggrecan fragments present in both osteoarthritic human synovial fluid and in normal bovine synovial fluid are large, being composed of a short NH2-terminal stretch of the interglobular domain, the G2 domain, the keratan sulfate domain, and variable lengths of the chondroitin sulfate domain(s). We conclude that the release of aggrecan fragments from articular cartilage into the synovial fluid seen at all stages of human osteoarthritis (Lohmander, L. S. 1991. Acta Orthop. Scand. 62:623-632) is promoted by the action of a normal cartilage proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain. (Less)
407 citations
TL;DR: A novel proteoglycan (PG) has been identified in culture medium from thin slices of the superficial zone of bovine articular cartilage and may serve as a functional metabolic marker for chondrocytes of the shallow zone of articular Cartilage.
404 citations