Print Email Facebook Twitter Contribution of collagen network features to functional properties of engineered cartilage 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 HealthCartilageChondrocyteCollagenCrosslinksMechanical properties3 aminopropionitrilealginic acidcollageninterstitial collagenasewateranimal cellanimal cell culturearticlearticular cartilagecartilage cellcartilage matrixcattlecollagen degradationcontrolled studycross linkingnonhumanpriority journalprotein degradationrigiditytissue engineeringwater retentionAlginatesAminopropionitrileAnimalsBiomechanicsCartilage, ArticularCattleCell CountCells, CulturedChondrocytesExtracellular MatrixFibrillar CollagensGene ExpressionMatrix MetalloproteinasesOsteoarthritisPermeabilityPhenotypeRegenerationStress, MechanicalTime FactorsTissue 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 Files To receive the publication files, please send an e-mail request to TNO Library.