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J Biol Chem, Vol. 273, Issue 41, 26408-26414, October 9, 1998

Human Aggrecan Keratan Sulfate Undergoes Structural Changes during Adolescent Development

Gavin M. BrownDagger , Thomas N. Huckerby, Michael T. Baylissparallel , and Ian A. NieduszynskiDagger

From the Dagger  Department of Biological Sciences, Institute of Environmental and Natural Sciences, Lancaster University, Bailrigg, Lancaster, LA1 4YQ United Kingdom, the  Polymer Centre, School of Physics and Chemistry, Lancaster University, Bailrigg, Lancaster, LA1 4YA United Kingdom, and the parallel  Royal Veterinary College (University of London), Department of Veterinary Basic Science, Royal College Street, London, NW1 0TU United Kingdom

Alkaline borohydride-reduced keratan sulfate chains were isolated from human articular cartilage aggrecan from individuals of various ages (0-85 years old). The chains were structurally characterized using 1H NMR spectroscopy, gel permeation chromatography, and oligosaccharide profiling (after digestion with the enzymes keratanase and keratanase II). The results show that from birth to early adolescence (0-9 years) the levels of alpha (1-3)-fucosylation, alpha (2-3)-sialylation, and galactose sulfation increase. Also, the weight-average molecular weight of the chains increases. During maturation (9-18 years) the levels of fucosylation and galactose sulfation continue to increase and alpha (2-6)-sialylation of the chains occurs. In adult life (18-85 years) there is little change in the weight-average molecular weight of the chains, and the levels of fucosylation, sialylation, and sulfation remain fairly constant.


Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.



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