FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W4295648533> ?p ?o ?g. }

• W4295648533 endingPage "189" @default.
• W4295648533 startingPage "178" @default.
• W4295648533 abstract "The function of articular cartilage as a load-bearing connective tissue is derived primarily from a balanced interaction between the swelling proteoglycan (PG) matrix and tension-resistant collagen fibrous network. Such balance is compromised during joint disease such as osteoarthritis (OA) due to degradation to PGs and/or collagens. While the PG degradation is generally thought to be related to a loss of protein abundance, the collagenous degradation is more complex as it can be caused independently by a decrease of collagen content, disorganisation of fibrous structure and softening of individual collagen fibrils. A comprehensive understanding of the initial trajectories of degradation of PGs and collagen network can improve our chance of finding potential therapeutic solutions for OA. Here, we developed geometrically, structurally, and compositionally realistic and sample-specific Finite Element (FE) models under the framework of multiphasic mixture theory, from which the elastic moduli of collagen fibres and the PG load-bearing quality in healthy and diseased cartilages were estimated by numerical optimisation of the multi-step indentation stress relaxation force-time curves. We found the intrinsic quality of collagen fibres, measured by their elastic moduli, to stay constant for healthy and diseased cartilages. Combining with previous findings which show unaltered collagen content during early stages of OA, our results suggest the disorganisation of collagen fibrous network as the first form of collagenous degradation in osteoarthritic cartilage. We also found that PG degradation involves not only a loss of protein abundance, but also the quality of the remaining PGs in generating sufficient osmotic pressure for load bearing. This study sheds light on the mechanism of OA pathogenesis and highlights the restoration of collageneous organisation in cartilage as key medical intervention for OA. Collagen network in articular cartilage consists of individual fibres that are organised into depth-dependent structure specialised for joint load-bearing and lubrication. During osteoarthritis, the collagen network undergoes mechanical degradation, but it is unclear if a loss of content, disorganisation of fibrous structure, or softening of individual fibres causes this degeneration. Using mechanical indentation, Finite Element modelling, and numerical optimisation methods, we determined that individual fibres did not soften in early disease stage. Together with previous findings showing unaltered collagen content, our results pinpoint the disorganisation of collagen structure as the main culprit for early collagenous degradation in osteoarthritic cartilage. Thus, early restoration in cartilage of collagen organisation, instead of individual fibre quality, may be key to slow osteoarthritis development." @default.
• W4295648533 created "2022-09-14" @default.
• W4295648533 creator A5002170206 @default.
• W4295648533 creator A5013903559 @default.
• W4295648533 creator A5022590395 @default.
• W4295648533 creator A5082454261 @default.
• W4295648533 creator A5091418494 @default.
• W4295648533 date "2022-11-01" @default.
• W4295648533 modified "2023-10-16" @default.
• W4295648533 title "The intrinsic quality of proteoglycans, but not collagen fibres, degrades in osteoarthritic cartilage" @default.
• W4295648533 cites W1066096829 @default.
• W4295648533 cites W127220886 @default.
• W4295648533 cites W1487036716 @default.
• W4295648533 cites W1966686938 @default.
• W4295648533 cites W1967774339 @default.
• W4295648533 cites W1972155312 @default.
• W4295648533 cites W1973118841 @default.
• W4295648533 cites W1973164976 @default.
• W4295648533 cites W1973886144 @default.
• W4295648533 cites W1974537097 @default.
• W4295648533 cites W1981039285 @default.
• W4295648533 cites W1983009555 @default.
• W4295648533 cites W1987135075 @default.
• W4295648533 cites W1992105939 @default.
• W4295648533 cites W1992614274 @default.
• W4295648533 cites W2002947324 @default.
• W4295648533 cites W2011931614 @default.
• W4295648533 cites W2014524368 @default.
• W4295648533 cites W2017950984 @default.
• W4295648533 cites W2019038382 @default.
• W4295648533 cites W2020342708 @default.
• W4295648533 cites W2029621921 @default.
• W4295648533 cites W2030381040 @default.
• W4295648533 cites W2030610672 @default.
• W4295648533 cites W2031144025 @default.
• W4295648533 cites W2033620253 @default.
• W4295648533 cites W2036532414 @default.
• W4295648533 cites W2040962644 @default.
• W4295648533 cites W2050624061 @default.
• W4295648533 cites W2055072688 @default.
• W4295648533 cites W2055884129 @default.
• W4295648533 cites W2055978912 @default.
• W4295648533 cites W2057822669 @default.
• W4295648533 cites W2058232580 @default.
• W4295648533 cites W2058721833 @default.
• W4295648533 cites W2059224417 @default.
• W4295648533 cites W2062155239 @default.
• W4295648533 cites W2065499250 @default.
• W4295648533 cites W2070899131 @default.
• W4295648533 cites W2073775623 @default.
• W4295648533 cites W2075211151 @default.
• W4295648533 cites W2077173015 @default.
• W4295648533 cites W2078419502 @default.
• W4295648533 cites W2086027952 @default.
• W4295648533 cites W2094223932 @default.
• W4295648533 cites W2095964234 @default.
• W4295648533 cites W2101108021 @default.
• W4295648533 cites W2124722865 @default.
• W4295648533 cites W2126870355 @default.
• W4295648533 cites W2133235008 @default.
• W4295648533 cites W2133787690 @default.
• W4295648533 cites W2133809313 @default.
• W4295648533 cites W2135616992 @default.
• W4295648533 cites W2137029158 @default.
• W4295648533 cites W2137201386 @default.
• W4295648533 cites W2143659399 @default.
• W4295648533 cites W2144166902 @default.
• W4295648533 cites W2152637989 @default.
• W4295648533 cites W2154265816 @default.
• W4295648533 cites W2159216779 @default.
• W4295648533 cites W2159255182 @default.
• W4295648533 cites W2161574825 @default.
• W4295648533 cites W2163920091 @default.
• W4295648533 cites W2169685756 @default.
• W4295648533 cites W2259346105 @default.
• W4295648533 cites W2336335772 @default.
• W4295648533 cites W2336959864 @default.
• W4295648533 cites W2469683796 @default.
• W4295648533 cites W2471983803 @default.
• W4295648533 cites W2537670537 @default.
• W4295648533 cites W2606250728 @default.
• W4295648533 cites W2762429861 @default.
• W4295648533 cites W2884940358 @default.
• W4295648533 cites W2911572729 @default.
• W4295648533 cites W2942251351 @default.
• W4295648533 cites W2948816540 @default.
• W4295648533 cites W2969810988 @default.
• W4295648533 cites W2972319559 @default.
• W4295648533 cites W2998563523 @default.
• W4295648533 cites W3040718936 @default.
• W4295648533 cites W3110536617 @default.
• W4295648533 cites W3136699826 @default.
• W4295648533 cites W3138342549 @default.
• W4295648533 cites W3179889696 @default.
• W4295648533 cites W4205502895 @default.
• W4295648533 cites W4212981105 @default.
• W4295648533 cites W4224920804 @default.
• W4295648533 cites W770081596 @default.

• next