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  • Glycoconjugate J 1997 14 651

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The structure of the keratan sulphate chains attached to fibromodulin from human articular cartilage

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The structure of the keratan sulphate chains attached to fibromodulin from human articular cartilage. / Lauder, R M ; Huckerby, T N ; Nieduszynski, I A .

In: Glycoconjugate Journal, Vol. 14, No. 5, 08.1997, p. 651-660.

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@article{159df6fa8a2a4267b438ecda2a2c99e8,
title = "The structure of the keratan sulphate chains attached to fibromodulin from human articular cartilage",
abstract = "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.",
keywords = "fibromodulin, small proteoglycan, keratan sulphate, glycosaminoglycan, sulphation, keratanase II, human, N-ACETYLNEURAMINIC ACID, CARBOHYDRATE DIFFERENTIATION ANTIGENS, BOVINE TRACHEAL CARTILAGE, SULFATE CHAINS, II DIGESTION, COLLAGEN, OLIGOSACCHARIDES, PROTEOGLYCANS, IDENTIFICATION, CHROMATOGRAPHY",
author = "Lauder, {R M} and Huckerby, {T N} and Nieduszynski, {I A}",
year = "1997",
month = aug,
doi = "10.1023/A:1018552913584",
language = "English",
volume = "14",
pages = "651--660",
journal = "Glycoconjugate Journal",
issn = "0282-0080",
publisher = "Springer Netherlands",
number = "5",

}

RIS

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 -