{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,8,31]],"date-time":"2024-08-31T08:58:24Z","timestamp":1725094704242},"reference-count":28,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2018,2,13]],"date-time":"2018-02-13T00:00:00Z","timestamp":1518480000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Dutch Arthritis Foundation","award":["13-3-406"],"award-info":[{"award-number":["13-3-406"]}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal Orthopaedic Research"],"published-print":{"date-parts":[[2018,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:sec><jats:label \/><jats:p>An important aspect in cartilage ageing is accumulation of advanced glycation end products (AGEs) after exposure to sugars. Advanced glycation results in cross\u2010links formation between the collagen fibrils in articular cartilage, hampering their flexibility and making cartilage more brittle. In the current study, we investigate whether collagen cross\u2010linking after exposure to sugars depends on the stretching condition of the collagen fibrils. Healthy equine cartilage specimens were exposed to <jats:sc>l<\/jats:sc>\u2010threose sugar and placed in hypo\u2010, iso\u2010, or hyper\u2010osmolal conditions that expanded or shrank the tissue and changed the 3D conformation of collagen fibrils. We applied micro\u2010indentation tests, contrast enhanced micro\u2010computed tomography, biochemical measurement of pentosidine cross\u2010links, and cartilage surface color analysis to assess the effects of advanced glycation cross\u2010linking under these different conditions. Swelling of extracellular matrix due to hypo\u2010osmolality made cartilage less susceptible to advanced glycation, namely, the increase in effective Young's modulus was approximately 80% lower in hypo\u2010osmolality compared to hyper\u2010osmolality and pentosidine content per collagen was 47% lower. These results indicate that healthy levels of glycosaminoglycans not only keep cartilage stiffness at appropriate levels by swelling and pre\u2010stressed collagen fibrils, but also protect collagen fibrils from adverse effects of advanced glycation. These findings highlight the fact that collagen fibrils and therefore cartilage can be protected from further advanced glycation (\u201cageing\u201d) by maintaining the joint environment at sufficiently low osmolality. Understanding of mechanochemistry of collagen fibrils provided here might evoke potential ageing prohibiting strategies against cartilage deterioration. \u00a9 2018 The Authors. <jats:italic>Journal of Orthopaedic Research<\/jats:italic> Published by Wiley Periodicals, Inc. on behalf of Orthopaedic Research Society. J Orthop Res 36:1929\u20131936, 2018.<\/jats:p><\/jats:sec>","DOI":"10.1002\/jor.23857","type":"journal-article","created":{"date-parts":[[2018,1,15]],"date-time":"2018-01-15T11:00:50Z","timestamp":1516014050000},"page":"1929-1936","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Non\u2010enzymatic cross\u2010linking of collagen type II fibrils is tuned via osmolality switch"],"prefix":"10.1002","volume":"36","author":[{"given":"Behdad","family":"Pouran","sequence":"first","affiliation":[{"name":"Department of Orthopedics UMC Utrecht Heidelberglaan100, 3584CX Utrecht The Netherlands"},{"name":"Faculty of Mechanical, Maritime, and Materials Engineering, Department of Biomechanical Engineering Delft University of Technology (TU Delft) Mekelweg 2, 2628CD Delft The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Parisa R.","family":"Moshtagh","sequence":"additional","affiliation":[{"name":"Department of Orthopedics UMC Utrecht Heidelberglaan100, 3584CX Utrecht The Netherlands"},{"name":"Faculty of Mechanical, Maritime, and Materials Engineering, Department of Biomechanical Engineering Delft University of Technology (TU Delft) Mekelweg 2, 2628CD Delft The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Vahid","family":"Arbabi","sequence":"additional","affiliation":[{"name":"Department of Orthopedics UMC Utrecht Heidelberglaan100, 3584CX Utrecht The Netherlands"},{"name":"Faculty of Mechanical, Maritime, and Materials Engineering, Department of Biomechanical Engineering Delft University of Technology (TU Delft) Mekelweg 2, 2628CD Delft The Netherlands"},{"name":"Faculty of Engineering, Department of Mechanical Engineering University of Birjand 615\/97175 Birjand Iran"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jessica","family":"Snabel","sequence":"additional","affiliation":[{"name":"Department of Metabolic Health Research TNO P.O. 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