Keratan sulfate chains

One very long molecule of hyaluronate is associated noncovalently with about 100 molecules of the core protein aggrecan. Each aggre-can molecule contains many covalently bound chondroitin sulfate and keratan sulfate chains. Link proteins situated at the junction between each core protein and the hyaluronate backbone mediate the core protein-hyaluronate interaction. 

GlcNAc. KSII members are O-linked to a Ser/Thr residue of the core protein they are primarily found in cartilage, are highly sulfated, and are terminated by sialic acids. KSIII are found in brain tissue and have a unique linker between the keratan sulfate chain and the protein a Man O-linked to a Ser of the protein. 

Oeben M, Keller R, Stuhlsatz HW, Greihng H. Constant and variable domains of different disaccharide structure in corneal keratan sulfate chains. Biochem. J. 1987 248(1) 85—93. 

Skeletal keratan sulfate and corneal keratan sulfate chains are attached to core protein through O-linked oligosaccharides [29] and N-linked oligosaccharides [30,31] respectively, identical to O-linked and N-linked oligosaccharides of the general class of glycoproteins. 

The keratan and chondroitin/dermatan sulfate levels in normal human corneas and corneas affected by macular corneal dystrophies types I and II were compared (10). The results revealed that the keratan sulfate chain size was reduced and chain sulfation was absent in type I, and that sulfation of both GlcNAc and Gal was significantly reduced in type II. The chondroitin/dermatan sulfate chain sizes were also decreased in all diseased corneas, and the contents of 4- and... 

Keratan sulfate chains are formed by the action of glycosyl transferases that link... 

The physical and mechanical properties of cartilage are certainly important for the physiological role of this tissue. Proteoglycan in connection with collagen and other constituents of this tissue may affect its physical properties. Cartilage proteoglycan is a complex species. To a protein core, many chondroitin sulfate and keratan sulfate chains are attached. 

Effect of chondroitinase ABC. This enzyme (chondroitin ABC lyase, EC A.2.2.A.) also depolymerizes the hyaluronic acid backbone of aggregate. In addition, it can degrade chondroitin sulfate chains of monomer, but not its keratan sulfate chains. 

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