Title
Ageing and zonal variation in post-translational modification of collagen in normal human articular cartilage: The age-related increase in Non-Enzymatic Glycation affects biomechanical properties of cartilage
Author
Bank, R.A.
Bayliss, M.T.
Lafeber, F.P.J.G.
Maroudas, A.
Tekoppele, J.M.
Gaubius Instituut TNO
Publication year
1998
Abstract
A biomechanical failure of the collagen network is postulated in many hypotheses of the development of osteoarthritis with advancing age. Here we investigate the accumulation of non-enzymatic glycation (NEG) products in healthy human articular cartilage, its relation to tissue remodelling and its role in tissue stiffening. Pentosidine levels were low up to age 20 years, and increased linearly after this age. This indicates extensive tissue remodelling at young age, and slow turnover of collagen after maturity has been reached. The slow remodelling is supported by the finding that enzymatic modifications of collagen (hydroxylysine, hydroxylysylpyridinoline, and lysylpyridinoline) were not related to age. The high remodelling is supported by levels of the crosslink lysylpyridinoline (LP) as a function of distance from the articular surface. LP was highest at the surface in mature cartilage (> 20 years), whereas in young cartilage (< 10 years) the opposite was seen; highest levels were close to the bone. LP levels in cartilage sections at age 14 years are high at the surface and close to the bone, but they are low in the middle region. This indicates that maturation of cartilage in the second decade of life starts in the upper half of the tissue, and occurs last in the tissue close to the bone. The effect of NEG products on instantaneous deformation of cartilage was investigated as a functional of topographical variations in pentosidine levels in vivo and in relation to in vitro induced NEG. Consistently, higher pentosidine levels were associated with a stiffer collagen network. A stiffer and more crosslinked collagen network may become more brittle and more prone to fatigue.
Subject
Health Biology
Biomedical Research
amino acid
collagen
collagen fibril
deoxypyridinoline
hydroxylysine
pentosidine
pyridinoline
pyridoxine
unclassified drug
adolescent
amino acid analysis
articular cartilage
clinical article
collagen metabolism
controlled study
cross linking
glycation
human tissue
osteoarthritis
preschool child
protein processing
school child
Adult
Aged
Aged, 80 and over
Aging
Arginine
Biomechanics
Cartilage, Articular
Child
Child, Preschool
Collagen
Cross-Linking Reagents
Glycosylation End Products, Advanced
Humans
Hydroxylysine
Infant
Lysine
Middle Aged
Protein Processing, Post-Translational
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http://resolver.tudelft.nl/uuid:e9eb02de-7990-491f-8454-cf3731f99637
TNO identifier
234372
ISSN
0264-6021
Source
Biochemical Journal, 330 (1), 345-351
Document type
article