Print Email Facebook Twitter The canine 'groove' model, compared with the ACLT model of osteoarthritis Title The canine 'groove' model, compared with the ACLT model of osteoarthritis Author Marijnissen, A.C.A. van Roermund, P.M. TeKoppele, J.M. Bijlsma, J.W.J. Lafeber, F.P.J.G. TNO Preventie en Gezondheid Publication year 2002 Abstract Objective: The frequently used anterior cruciate ligament transection (ACLT) model of osteoarthritis (OA) in the dog, makes use of a permanent trigger (joint instability) for inducing degenerative changes. The present study evaluates a canine model of degenerative cartilage damage, mimicking OA, which is induced without making use of permanent joint instability. Methods: The articular cartilage of the weight-bearing areas of the femoral condyles in one knee of ten beagle dogs was damaged by making grooves, without damaging the subchondral bone. Surgery was followed by 10 weeks intensified loading of the affected joint. Subsequently, joint damage and inflammation were evaluated. The effects were compared with those of the ACLT model. Results: Histological analysis showed chondrocyte clusters around cartilage lesions and moderate loss of proteoglycans in the 'groove' model. Synovial inflammation was mild. Biochemical analysis of cartilage showed changes in matrix proteoglycan turnover, proteoglycan content, and collagen damage, all characteristics of OA. Synovial fluid MMP-1, -3 and -13 activity was enhanced. Changes were found in condyles and plateau, were similar for all animals tested, and were similar to the changes observed in the ACLT model. Conclusion: The presently described canine 'groove' model shows characteristics identical to those seen in the ACLT model but differs in a way that the changes are induced without joint instability. The latter is expected to make the 'groove' model more sensitive to treatment. © 2002 OsteoArthritis Research Society International. Chemicals/CAS: Collagen, 9007-34-5; Collagenases, EC 3.4.24.-; Matrix Metalloproteinase 1, EC 22.214.171.124; Matrix Metalloproteinase 13, EC 3.4.24.-; Matrix Metalloproteinase 3, EC 126.96.36.199; Proteoglycans Subject BiologyBiomedical ResearchCanine modelCartilageOsteoarthritisProteoglycanscollagencollagenase 3interstitial collagenasematrix proteinproteoglycanstromelysinanimal experimentanimal modelanimal tissueanterior cruciate ligamentarticlearticular cartilagebiochemistrycartilage cellcartilage degenerationcollagen degradationcontrolled studydisease modeldisease severitydogenzyme activityevaluationfemalefemur condylehistopathologyjoint stabilitykneenonhumanosteoarthritispriority journalprotein depletionsynovial fluidsynovitistissue injuryweight bearingAnimalsCartilage, ArticularChondrocytesCollagenCollagenasesDogsFemaleMatrix Metalloproteinase 1Matrix Metalloproteinase 13Matrix Metalloproteinase 3Models, AnimalOsteoarthritisProteoglycansSynovial FluidWeight-Bearing To reference this document use: http://resolver.tudelft.nl/uuid:fc87805a-6625-4005-a632-44ff2567211b DOI https://doi.org/10.1053/joca.2001.0491 TNO identifier 236463 ISSN 1063-4584 Source Osteoarthritis and Cartilage, 10 (2), 145-155 Document type article Files To receive the publication files, please send an e-mail request to TNO Library.