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.

Keratan Sulfate: Biosynthesis, Structures, and Biological Functions

Abstract: Keratan sulfate is a glycosaminoglycan that has been investigated in the cornea and skeletal tissues for decades. Endoglycosidases and monoclonal antibodies specific for keratan sulfate have been developed. These materials have facilitated the analysis of keratan sulfate biosynthesis and structures. Likewise, they have expedited study of the biological roles of keratan sulfate in vitro and in vivo. It has been shown that keratan sulfate is also expressed in the central nervous system and functions as a regulator of neuronal regeneration/sprouting. Here, we describe methods to determine the enzymatic activity of GlcNAc6ST, which is involved in keratan sulfate biosynthesis, and to extract and prepare ocular keratan sulfate for a disaccharide composition analysis. Immunohistochemistry for an anti-keratan sulfate epitope in the brain is also described.

Occurrence and Structural Analysis of Highly Sulfated Multiantennary N-linked Glycan Chains Derived from a Fertilization-Associated Carbohydrate-Rich Glycoprotein in Unfertilized Eggs of Tribolodon hakonensis

Abstract: This study represents the first detailed investigation of the nature of highly sulfated (keratan-sulfate-like) complex-type asparagine-linked glycans having a tetraantennary core structure and shows the effectiveness of fast-atom-bombardment mass spectrometric (FAB-MS) methods incorporating derivatization and mild methanolysis for analyzing such complex types of sulfated glycans. The structure of the N-glycan chains was unambiguously established by a combination of compositional analysis, methylation analysis, mild methanolysis for desulfation, hydrazinolysis/nitrous acid deamination, enzymatic (endo-β-galactosidase and peptide: N-glycosidase F) digestions, and instrumental analyses (1H-NMR spectroscopy and FAB-MS) which revealed the novel repeating sulfated carbohydrate sequences, ±Galβ1 4Galβ1[ 4(HSO3 6)GlcNAcβ1 3(±Galβ1 4)Galβ1]n (see Structure I; p+q+r+s ≈ 14). This sequence is unique in: (a) the skeletal structure is similar to that of keratan sulfate but is completely devoid of 6-O-sulfated Gal residues and (b) the presence of branched Gal residues in the sequence 4GlcNAcβ1 3(Galβ1 4)Galβ1.

Interactions of glycosaminoglycans with DNA and RNA synthesizing enzymes in vitro.

Abstract: The sulfated glycosaminoglycans chondroitin 4-sulfate, chondroitin 6-sulfate, keratan sulfate, dermatan sulfate, heparin, and glycosaminoglycan polysulfate are competitive inhibitors of the DNA-dependent RNA polymerase, the DNA-dependent RNA polymerase and the RNA-dependent DNA polymerase (reverse transcriptase). The unsulfated glycosaminoglycans chondroitin and hyaluronate are without any influence on the synthesis of DNA and RNA. The strongest inhibitor is a glycosaminoglycan polysulfate with four sulfate groups per disaccharide unit. It has the following inhibitor constants: DNA polymerase, Ki = 1.5 X 10(-6) M; RNA polymerase, Ki = 0.9 X 10(-6) M; reverse transcriptase, Ki = 1.1 X 10(-6) M. The inhibition is closely correlated to the degree of sulfation of the glycosaminoglycans. There is a relationship between the sulfate/hexosamine ratio and the degree of inhibition. The inhibition of the DNA and RNA synthesizing enzymes by sulfated glycosaminoglycans depends on the nature of the template. With double-stranded DNA as template, inhibition occurs only when sulfated glycosaminoglycans are added before or shortly after (30 s) initiation of the synthesis. There is no inhibition if the inhibitors are added after the onset of the synthesis. On the other hand, with a single-stranded template synthesis was blocked completely at each phase of reaction.