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: It is suggested that keratan sulfate-sulfotransferase (GlcNAc-6-Sulfotranferase) is a key enzyme in keratan sulphate biosynthesis and that its decrease is primarily responsible for the marked decrease in keraten sulfate synthesis after in vitro culture.
26 citations
TL;DR: Proteoglycan subunits extracted in the presence of proteinase inhibitors from autologous knee and shoulder cartilage were examined in different donors of various ages, in order to determine the effect of weight bearing on the age-related changes in proteoglycan structure.
26 citations
TL;DR: Six mouse hybrid cell lines were isolated which secrete antibodies which appear to recognise a carbohydrate structure found only on corneal keratan sulfate proteoglycan, which can serve as a basis for separation of corneals types using antibody affinity chromatography.
Abstract: Six mouse hybrid cell lines were isolated which secrete antibodies to rabbit corneal proteoglycan. All six antibodies interacted with the same fraction of the proteoglycan, precipitating approximately 50% of proteoglycan labelled in the protein moiety. A radioimmunoassay using these antibodies measured concentrations as low as 1 g/m1 unlabelled rabbit corneal proteoglycan. Human corneal proteoglycanj corneal keratan sulfate, and an oligosaccharide fraction from corneal digests all interacted with the antibodies at concentrations similar to whole rabbit proteoglycan. Proteoglycans from cultured rabbit stromal fibroblasts and from sclera were 20 to 50-fold less effective in competition for antibody. Endo-β-galactosidase treatment of proteoglycan reduced antibody binding, but protease or chondroitinase treatments did not. Labelled proteoglycan separated by antibody affinity chromatography contained only keratan sulfate, whereas proteoglycan not bound to affinity columns contained only chondroitin sulfate. Th...
26 citations
TL;DR: It is suggested that the differences found between first and second extractions of cartilage, between upper and lower layers of Cartilage, and between knee and hip cartilage are caused by variations in the relative amount of nonaggregating proteoglycans and/or variations in proteoglycan size.
Abstract: Proteoglycans (A1 fractions) were extracted with 4M guanidine hydrochloride (GuHCl) from human articular cartilage samples of a wide age range Distinctions were made between hip and knee, and upper and lower layers The residues of these extractions were digested with purified collagenase, and a second extraction with 4M GuHCl was performed, which yielded appreciable amounts of proteoglycans When pro-teoglycans from second extractions were compared with those from first extractions, the following changes were observed: an increase in chondroitin sulfate; a relative decrease in keratan sulfate; a decrease in protein content; and a decrease in the ratio of chondroitin 6-sulfate to chondroitin 4-sulfate The same changes were found when nonaggregating proteoglycans were compared with proteoglycan aggregates, when proteoglycans from young cartilage were compared with those from mature cartilage, when proteoglycans from knee cartilage were compared with those from hip cartilage, and when proteoglycans from upper layers of cartilage were compared with those from deeper layers It is suggested that the differences found between first and second extractions of cartilage, between upper and lower layers of cartilage, and between knee and hip cartilage are caused by variations in the relative amount of nonaggregating proteoglycans and/or variations in proteoglycan size
26 citations
TL;DR: The potential roles of the sulfated GAGs in the pathogenesis and progression of protein aggregation diseases from a perspective of their sulfation modification are reviewed.
Abstract: Protein aggregation diseases are characterized by intracellular or extracellular deposition of misfolded and aggregated proteins. These aggregated deposits contain multiple proteinaceous and non-protein components that are thought to play critical roles in the etiology and pathogenesis of protein aggregation diseases in vivo. One of these components, the sulfated glycosaminoglycans (GAGs), includes heparan sulfate, chondroitin sulfate, and keratan sulfate. The sulfated GAGs are negatively charged heteropolysaccharides expressed in all mammalian tissues. Enzymatically generated structural patterns and the degree of sulfation in GAGs determine GAGs' specific interactions with their protein ligands. Here, we review the potential roles of the sulfated GAGs in the pathogenesis and progression of protein aggregation diseases from a perspective of their sulfation modification. We also discuss the possibility of sulfated GAGs as therapeutic targets for protein aggregation diseases.
26 citations