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 livers and spleens from three patients with cerebral GM1-gangliosidosis contained greatly increased concentrations of a mucopolysaccharide tentatively identified as keratan sulfate, and the concentration of a very soluble sialomucopolySaccharide was also increased.
Abstract: The livers and spleens from three patients with cerebral G(M1)-gangliosidosis contained greatly increased concentrations of a mucopolysaccharide tentatively identified as keratan sulfate. The concentration of a very soluble sialomucopolysaccharide was also increased. Concentrations of these compounds were not increased in the viscera of patients with Tay-Sachs disease (G(M2)-gangliosidosis). G(M1)-gangliosidosis appears to be a combined cerebral gangliosidosis and visceral mucopolysaccharidosis.
90 citations
TL;DR: The CNS antigen is similar, but not identical, to the cartilage antigen, and may represent another member of the family of high molecular weight CSPGs which bind to and aggregate with hyaluronic acid.
90 citations
TL;DR: Keratan sulfate proteoglycans (KSPGs) play a pivotal role in the development and maintenance of corneal transparency and are expressed by many tissues other than cornea, but keratocan mRNA is more selectively expressed in theCorneal tissue of the adult mouse.
90 citations
TL;DR: It is established that none of the glycosaminoglycans in plasma are covalently linked to plasma proteins, and plasma heparan sulfate may play an important role in plasma lipoprotein metabolism.
Abstract: We have described methodology for the isolation and quantitation of glycosaminoglycans present in human plasma. Plasma glycosaminoglycans can be quantitatively adsorbed on a DEAE-Sephacel ion exchanger and eluted with a salt gradient as two groups: a low-charge fraction and a high-charge fraction. The low-charge fraction consists of chondroitin sulfate with a low sulfate content and the high-charge fraction consists of heparan sulfate, chondroitin sulfate, and keratan sulfate (type I). We have determined the plasma concentration of each of these glycosaminoglycans in six normal human subjects. We have established that none of the glycosaminoglycans in plasma are covalently linked to plasma proteins. All are isolated as complexes with plasma proteins in noncovalent linkages. The glycosaminoglycans in the low-charge fraction are bound with high affinity to a single plasma glycoprotein by a lectin-type bond that can be disrupted by a simple glycoside. The high-charge fraction contains three major proteins and several minor proteins associated with the glycosaminoglycans by both lectin-type and ionic bonding. The plasma proteins associated with glycosaminoglycans represent less than 0.5% of the total plasma proteins. Little is known about the physiologic role of the plasma glycosaminoglycans as components of metabolic processes. Because glycosaminoglycans have been implicated in lipid metabolism and atherosclerosis, we tested all of these compounds, isolated in free form, on the in vitro hydrolysis of triglycerides by lipoprotein lipase. Plasma heparan sulfate stimulated the rate of this reaction severalfold. All other plasma glycosaminoglycans were inactive. Thus, plasma heparan sulfate may play an important role in plasma lipoprotein metabolism.
90 citations
TL;DR: It is concluded that the 190-kDa hHARE can function independently of other hHare isoforms to mediate the endocytosis of multiple glycosaminoglycans, and the rat and human small HARE isoforms have different glycosamina specificities and sensitivities to inhibition by cross-reacting antibodies.
90 citations