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Age-related changes in the structure of the keratan sulphate chains attached to fibromodulin isolated from articular cartilage.

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Age-related changes in the structure of the keratan sulphate chains attached to fibromodulin isolated from articular cartilage. / Lauder, R. M.; Huckerby, T. N.; Nieduszynski, I. A.; Plaas, A. H.

In: Biochemical Journal, Vol. 330 , 1998, p. 753-757.

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@article{b494fd982a0a48d09a49c04e34b46e07,
title = "Age-related changes in the structure of the keratan sulphate chains attached to fibromodulin isolated from articular cartilage.",
abstract = "Bovine articular cartilage fibromodulin has been isolated from animals aged 3 months to 8 years, and the attached keratan sulphate (KS) chains digested with keratanase II. The oligosaccharides generated have been reduced, examined by high-pH anion-exchange chromatography and their structures identified by comparison with standards. It has been shown that in fibromodulin from young articular cartilage, the KS chains do not possess either non-reducing terminal (alpha2-6)-linked N-acetylneuraminic acid or fucose (alpha1-3)-linked to sulphated N-acetylglucosamine residues. However, an age-related increase has been observed in the abundance of both (alpha2-6)-linked N-acetylneuraminic acid and (alpha1-3)-linked fucose, neither of which is found in KS isolated from non-articular cartilage, irrespective of the age of the source. Interestingly, the KS chain length remains constant as a function of age, which possibly relates to a role in collagen fibril assembly. In addition, no significant age-related changes were identified in levels of galactose sulphation.",
author = "Lauder, {R. M.} and Huckerby, {T. N.} and Nieduszynski, {I. A.} and Plaas, {A. H.}",
year = "1998",
language = "English",
volume = "330 ",
pages = "753--757",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",

}

RIS

TY - JOUR

T1 - Age-related changes in the structure of the keratan sulphate chains attached to fibromodulin isolated from articular cartilage.

AU - Lauder, R. M.

AU - Huckerby, T. N.

AU - Nieduszynski, I. A.

AU - Plaas, A. H.

PY - 1998

Y1 - 1998

N2 - Bovine articular cartilage fibromodulin has been isolated from animals aged 3 months to 8 years, and the attached keratan sulphate (KS) chains digested with keratanase II. The oligosaccharides generated have been reduced, examined by high-pH anion-exchange chromatography and their structures identified by comparison with standards. It has been shown that in fibromodulin from young articular cartilage, the KS chains do not possess either non-reducing terminal (alpha2-6)-linked N-acetylneuraminic acid or fucose (alpha1-3)-linked to sulphated N-acetylglucosamine residues. However, an age-related increase has been observed in the abundance of both (alpha2-6)-linked N-acetylneuraminic acid and (alpha1-3)-linked fucose, neither of which is found in KS isolated from non-articular cartilage, irrespective of the age of the source. Interestingly, the KS chain length remains constant as a function of age, which possibly relates to a role in collagen fibril assembly. In addition, no significant age-related changes were identified in levels of galactose sulphation.

AB - Bovine articular cartilage fibromodulin has been isolated from animals aged 3 months to 8 years, and the attached keratan sulphate (KS) chains digested with keratanase II. The oligosaccharides generated have been reduced, examined by high-pH anion-exchange chromatography and their structures identified by comparison with standards. It has been shown that in fibromodulin from young articular cartilage, the KS chains do not possess either non-reducing terminal (alpha2-6)-linked N-acetylneuraminic acid or fucose (alpha1-3)-linked to sulphated N-acetylglucosamine residues. However, an age-related increase has been observed in the abundance of both (alpha2-6)-linked N-acetylneuraminic acid and (alpha1-3)-linked fucose, neither of which is found in KS isolated from non-articular cartilage, irrespective of the age of the source. Interestingly, the KS chain length remains constant as a function of age, which possibly relates to a role in collagen fibril assembly. In addition, no significant age-related changes were identified in levels of galactose sulphation.

M3 - Journal article

VL - 330

SP - 753

EP - 757

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

ER -