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J Biol Chem, Vol. 273, Issue 41, 26408-26414, October 9, 1998
,
, and
From the 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
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
Royal Veterinary College (University
of London), Department of Veterinary Basic Science, Royal College
Street, London, NW1 0TU United Kingdom
(1-3)-fucosylation,
(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
(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.
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