Lauder, R. M. and Huckerby, T. N. and Nieduszynski, I. A. and Plaas, A. H. (1998) Age-related changes in the structure of the keratan sulphate chains attached to fibromodulin isolated from articular cartilage. Biochemical Journal, 330. pp. 753-757. ISSN 0264-6021Full text not available from this repository.
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.
|Journal or Publication Title:||Biochemical Journal|
|Subjects:||R Medicine > R Medicine (General)|
|Departments:||Faculty of Health and Medicine > Biomedical & Life Sciences|
Faculty of Science and Technology > Lancaster Environment Centre
|Deposited By:||Dr Bob Lauder|
|Deposited On:||09 Dec 2010 09:29|
|Last Modified:||29 Apr 2017 01:50|
Actions (login required)