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Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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TY - JOUR
T1 - The structure of the keratan sulphate chains attached to fibromodulin from human articular cartilage
AU - Lauder, R M
AU - Huckerby, T N
AU - Nieduszynski, I A
PY - 1997/8
Y1 - 1997/8
N2 - The small keratan sulphate proteoglycan, fibromodulin, has been isolated from pooled human articular cartilage. The main chain repeat region and the chain caps from the attached N-linked keratan sulphate chains have been fragmented by keratanase II digestion, and the oligosaccharides generated have been reduced and isolated. Their structures and abundance have been determined by high pH anion-exchange chromatography.These regions of the keratan sulphate from human articular cartilage fibromodulin have been found to have the following general structure:[GRAPHICS]Significantly, both alpha(2-6)- and alpha(2-3)-linked N-acetyl-neuraminic acid have been found in the capping oligosaccharides. Fucose, which is alpha(1-3)-linked as a branch to N-acetylglucosamine, has also been found along the length of the repeat region and in the capping region. The chains, which have been found to be very highly sulphated, are short; the length of the repeat region and chain caps is ca. nine disaccharides.These data demonstrate that the structure of the N-linked keratan sulphate chains of human articular cartilage fibromodulin is similar, in general, to articular cartilage derived O-linked keratan sulphate chains. Further, the general structure of the keratan sulphate chains attached to human articular cartilage fibromodulin has been found to be generally similar to that of both bovine and equine articular cartilage fibromodulin.
AB - The small keratan sulphate proteoglycan, fibromodulin, has been isolated from pooled human articular cartilage. The main chain repeat region and the chain caps from the attached N-linked keratan sulphate chains have been fragmented by keratanase II digestion, and the oligosaccharides generated have been reduced and isolated. Their structures and abundance have been determined by high pH anion-exchange chromatography.These regions of the keratan sulphate from human articular cartilage fibromodulin have been found to have the following general structure:[GRAPHICS]Significantly, both alpha(2-6)- and alpha(2-3)-linked N-acetyl-neuraminic acid have been found in the capping oligosaccharides. Fucose, which is alpha(1-3)-linked as a branch to N-acetylglucosamine, has also been found along the length of the repeat region and in the capping region. The chains, which have been found to be very highly sulphated, are short; the length of the repeat region and chain caps is ca. nine disaccharides.These data demonstrate that the structure of the N-linked keratan sulphate chains of human articular cartilage fibromodulin is similar, in general, to articular cartilage derived O-linked keratan sulphate chains. Further, the general structure of the keratan sulphate chains attached to human articular cartilage fibromodulin has been found to be generally similar to that of both bovine and equine articular cartilage fibromodulin.
KW - fibromodulin
KW - small proteoglycan
KW - keratan sulphate
KW - glycosaminoglycan
KW - sulphation
KW - keratanase II
KW - human
KW - N-ACETYLNEURAMINIC ACID
KW - CARBOHYDRATE DIFFERENTIATION ANTIGENS
KW - BOVINE TRACHEAL CARTILAGE
KW - SULFATE CHAINS
KW - II DIGESTION
KW - COLLAGEN
KW - OLIGOSACCHARIDES
KW - PROTEOGLYCANS
KW - IDENTIFICATION
KW - CHROMATOGRAPHY
U2 - 10.1023/A:1018552913584
DO - 10.1023/A:1018552913584
M3 - Journal article
VL - 14
SP - 651
EP - 660
JO - Glycoconjugate Journal
JF - Glycoconjugate Journal
SN - 0282-0080
IS - 5
ER -