Title
Putative role of lysyl hydroxylation and pyridinoline cross-linking during adolescence in the occurrence of osteoarthritis at old age
Author
Bank, R.A.
Verzijl, N.
Lafeber, F.P.J.G.
Tekoppele, J.M.
Gaubius instituut TNO TNO Preventie en Gezondheid
Publication year
2002
Abstract
Objective: The collagen network in human articular cartilage experiences a large number of stress cycles during life as it shows hardly any turnover after adolescence. We hypothesized that, to withstand fatigue failure, the physical condition of the collagen network laid down at adolescence is of crucial importance for the age of onset of osteoarthritis (OA). Methods: We have compared the lysyl hydroxylation level and pyridinoline cross-link level of the collagen network of degenerated (DG) cartilage of the femoral knee condyle (representing a preclinical early stage of OA) with that of normal cartilage from the contralateral knee. The biological age of the collagen network was determined by means of pentosidine levels. For each donor, collagen modifications of normal cartilage were compared with DG cartilage that showed no significant remodeling of the collagen network (as evidenced by identical pentosidine levels). Results: DG cartilage contained significantly more hydroxylysine residues per collagen molecule in comparison with healthy cartilage from the same donor, both in the upper and lower half (the region near the articular surface and adjacent to bone, respectively). In addition, a significantly higher level of pyridinoline cross-linking was observed in the upper half of DG cartilage. Considering the biological age of the collagen network, the changes observed in DG cartilage must have been present several decades before cartilage became degenerated. Conclusions: The data suggest that high levels of lysyl hydroxylation and pyridinoline cross-linking result in a collagen network that fails mechanically in long term loading. Areas containing collagen with low hydroxylysine and pyridinoline levels are less prone to degeneration. As such, this study indicates that post-translational modifications of collagen molecules synthesized during adolescence are causally involved in the pathogenesis of OA. © 2002 OsteoArthritis Research Society International. Chemicals/CAS: Amino Acids; Arginine, 74-79-3; Collagen, 9007-34-5; Cross-Linking Reagents; Hydroxylysine, 28902-93-4; Lysine, 56-87-1; pentosidine, 124505-87-9; pyridinoline, 63800-01-1
Subject
Health Biology
Biomedical Research
Collagen
Fatigue
Hydroxylysine
Osteoarthritis
Pyridinoline
collagen
hydroxylysine
pentosidine
pyridinoline
adolescence
adult
aged
article
articular cartilage
cartilage degeneration
clinical article
collagen synthesis
controlled study
cross linking
fatigue
femur condyle
human
human tissue
hydroxylation
knee osteoarthritis
onset age
pathogenesis
priority journal
senescence
stress
stress strain relationship
Aged
Aged, 80 and over
Amino Acids
Arginine
Case-Control Studies
Collagen
Cross-Linking Reagents
Humans
Hydroxylysine
Lysine
Middle Aged
Osteoarthritis, Knee
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DOI
https://doi.org/10.1053/joca.2001.0487
TNO identifier
236458
ISSN
1063-4584
Source
Osteoarthritis and Cartilage, 10 (2), 127-134
Document type
article