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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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01 Jan 2016
TL;DR: Heparin, the most studied GAG, is unique in its intracellular location in mast cell and basophil granules, and it regulates a number of important biological activities.
Abstract: In recent years, much attention has been paid to the chemistry and biochemistry of carbohydrates due to their many functions both inside and outside living cells. The glycosaminoglycans (GAGs) are related linear, polydisperse, microheterogeneous polyanionic polysaccharides. The most common GAGs are heparin, heparan sulfate, hyaluronic acid, chondroitin sulfate, dermatan sulfate, and keratan sulfate. The GAGs are generally believed to exert their biological activities through the localization, stabilization, activation, or inactivation of interacting proteins (1). These interactions play important roles in the normal physiology of animals (2) and are also involved in certain pathological processes (3). Heparin, the most studied GAG, is unique in its intracellular location in mast cell and basophil granules. Exogenous heparin is regularly used as an anticoagulant/antithrombotic agent to maintain blood flow in the vasculature through the binding and activation of antithrombin III (ATIII, a coagulation serine protease inhibitor, SERPIN) (1). Heparin has been found to bind a wide range of proteins (1,4), and it regulates a number of important biological activities. Heparan sulfate, structurally similar to heparin, is localized on the external surface of cell membranes and in the extracellular matrix and plays a major role in cell–cell and cell–protein interaction (1). Heparan sulfate (not heparin) is also believed to be an endogenous receptor for circulating growth factors and chemokines that reg-

1 citations

Journal ArticleDOI
TL;DR: The keratan sulfate content of human intervertebral disc tissues ranged from 7 to 78 mumole galactose equivalents/g fresh weight; the root mean square error was 2 mumole/g; 10-25 mg of tissue were required.
Abstract: An assay for keratan sulfate in papain digests of human intervertebral disc and other tissues has been developed. The digest is applied to the acetate form of a tertiary amine acrylic anion-exchange resin, the oligosaccharide hexose is removed by washing the resin with 0.2 M sodium acetate buffer pH 5.0, then the keratan sulfate is eluted quantitatively with 1.0 M pyridinium sulfate pH 2.5 and assayed for hexose by the anthrone reaction. The keratan sulfate content of human intervertebral disc tissues ranged from 7 to 78 μmole galactose equivalents/g fresh weight; the root mean square error was 2 μmole/g; 10–25 mg of tissue were required. The separation of oligosaccharides from keratan sulfate was confirmed by gel permeation chromatography, sugar composition, ester sulfate analysis, and nuclear magnetic resonance.

1 citations

Journal ArticleDOI
TL;DR: It is suggested that anti-sulfatide aantibody was cross-reactive with heparan sulfate, especially heparin, and calf thymus DNA, and that this antibody recognizes certain structures containing repetitive, negatively charged groups as functional epitopes.

1 citations

Book ChapterDOI
TL;DR: Nonradioactive colorimetric enzymatic assays are described for these glycosyltransferases and sulfotransferases, in which the leaving nucleotides or nucleosides are hydrolyzed using specific phosphatases, and the released phosphate is subsequently detected using malachite reagents.
Abstract: Glycosaminoglycans (GAGs) are linear polysaccharides with repeating disaccharide units. GAGs include heparin, heparan sulfate, chondroitin sulfate, dermatan sulfate, keratan sulfate, and hyaluronan. All GAGs, except for hyaluronan, are usually sulfated. GAGs are polymerized by mono- or dual-specific glycosyltransferases and sulfated by various sulfotransferases. To further our understanding of GAG chain length regulation and synthesis of specific sulfation motifs on GAG chains, it is imperative to understand the kinetics of GAG synthetic enzymes. Here, nonradioactive colorimetric enzymatic assays are described for these glycosyltransferases and sulfotransferases. In both cases, the leaving nucleotides or nucleosides are hydrolyzed using specific phosphatases, and the released phosphate is subsequently detected using malachite reagents.

1 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
202310
202222
20217
20209
201912
201812