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Contribution of collagen network features to functional properties of engineered cartilage

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Author: Bastiaansen-Jenniskens, Y.M. · Koevoet, W. · Bart, A.C.W. de · Linden, J.C. van der · Zuurmond, A.M. · Weinans, H. · Verhaar, J.A.N. · Osch, G.J.V.M. van · Groot, J. de
Type:article
Date:2008
Institution: TNO Kwaliteit van Leven
Source:Osteoarthritis and Cartilage, 3, 16, 359-366
Identifier: 240678
doi: doi:10.1016/j.joca.2007.07.003
Keywords: 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

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.