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Keratan sulfate biosynthesis

Stable Identifier
R-HSA-2022854
Type
Pathway
Species
Homo sapiens
Locations in the PathwayBrowser
Summation

Keratan sulfate (KSI) is the best characterised keratan sulfate. It is 10 times more abundant in cornea than cartilage. KSI is attached to an asparagine (Asn) residue on the core protein via an N-linked branched oligosaccharide (an N-glycan core structure used as a precursor in N-glycan biosynthesis). KSI is elongated by the alternate additions of galactose (Gal) and N-acetylglucosamine (GlcNAc), mediated by glycosyltransferases. Elongation is terminated by the addition of a single N-acetylneuraminic acid (sialyl) residue. KSI is also sulfated on Gal and GlcNAc residues by at least two sulfotransferases (Funderburgh 2000, Funderburgh 2002, Quantock et al. 2010). KSI can be attached to asparagine residues on core proteins, creating so called proteoglycans (PGs). Seven common core proteins found in corneal and skeletal tissues are used as examples here.

Literature References
PubMed ID Title Journal Year
12512857 Keratan sulfate biosynthesis IUBMB Life 2002
11030741 Keratan sulfate: structure, biosynthesis, and function Glycobiology 2000
20213925 Structural and biochemical aspects of keratan sulphate in the cornea Cell Mol Life Sci 2010
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Participant Of
Event Information
Orthologous Events