Title
Contribution of collagen network features to functional properties of engineered cartilage
Author
Bastiaansen-Jenniskens, Y.M.
Koevoet, W.
de Bart, A.C.W.
van der Linden, J.C.
Zuurmond, A.M.
Weinans, H.
Verhaar, J.A.N.
van Osch, G.J.V.M.
de Groot, J.
TNO Kwaliteit van Leven
Publication year
2008
Abstract
Background: Damage to articular cartilage is one of the features of osteoarthritis (OA). Cartilage damage is characterised by a net loss of collagen and proteoglycans. The collagen network is considered highly important for cartilage function but little is known about processes that control composition and function of the cartilage collagen network in cartilage tissue engineering. Therefore, our aim was to study the contribution of collagen amount and number of crosslinks on the functionality of newly formed matrix during cartilage repair. Methods: Bovine articular chondrocytes were cultured in alginate beads. Collagen network formation was modulated using the crosslink inhibitor β-aminopropionitrile (BAPN; 0.25 mM). Constructs were cultured for 10 weeks with/without BAPN or for 5 weeks with BAPN followed by 5 weeks without. Collagen deposition, number of crosslinks and susceptibility to degradation by matrix metalloproteinase-1 (MMP-1) were examined. Mechanical properties of the constructs were determined by unconfined compression. Results: BAPN for 5 weeks increased collagen deposition accompanied by increased construct stiffness, despite the absence of crosslinks. BAPN for 10 weeks further increased collagen amounts. Absence of collagen crosslinks did not affect stiffness but ability to hold water was lower and susceptibility to MMP-mediated degradation was increased. Removal of BAPN after 5 weeks increased collagen amounts, allowed crosslink formation and increased stiffness. Discussion: This study demonstrates that both collagen amounts and its proper crosslinking are important for a functional cartilage matrix. Even in conditions with elevated collagen deposition, crosslinks are needed to provide matrix stiffness. Crosslinks also contribute to the ability to hold water and to the resistance against degradation by MMP-1. © 2007 Osteoarthritis Research Society International.
Subject
Health
Cartilage
Chondrocyte
Collagen
Crosslinks
Mechanical properties
3 aminopropionitrile
alginic acid
collagen
interstitial collagenase
water
animal cell
animal cell culture
article
articular cartilage
cartilage cell
cartilage matrix
cattle
collagen degradation
controlled study
cross linking
nonhuman
priority journal
protein degradation
rigidity
tissue engineering
water retention
Alginates
Aminopropionitrile
Animals
Biomechanics
Cartilage, Articular
Cattle
Cell Count
Cells, Cultured
Chondrocytes
Extracellular Matrix
Fibrillar Collagens
Gene Expression
Matrix Metalloproteinases
Osteoarthritis
Permeability
Phenotype
Regeneration
Stress, Mechanical
Time Factors
Tissue Engineering
To reference this document use:
http://resolver.tudelft.nl/uuid:fb0529e7-cd54-4423-8165-a6a161cb3a1d
DOI
https://doi.org/10.1016/j.joca.2007.07.003
TNO identifier
240678
ISSN
1063-4584
Source
Osteoarthritis and Cartilage, 16 (3), 359-366
Document type
article