In the quest of the optimal tissue source (porcine male and female articular, tracheal and auricular cartilage) for the development of collagen sponges for articular cartilage
dc.contributor.author | Wu, Z | |
dc.contributor.author | Korntner, SH | |
dc.contributor.author | Mullen, AM | |
dc.contributor.author | Skoufos, I | |
dc.contributor.author | Tzora, A. | |
dc.contributor.author | Zeugolis, DI | |
dc.date.accessioned | 2023-08-09T11:48:04Z | |
dc.date.available | 2023-08-09T11:48:04Z | |
dc.date.issued | 2021-06 | |
dc.identifier.citation | Z Wu, SH Korntner, AM Mullen, I Skoufos, A Tzora, DI Zeugolis, In the quest of the optimal tissue source (porcine male and female articular, tracheal and auricular cartilage) for the development of collagen sponges for articular cartilage, Biomedical Engineering Advances, Volume 1, 2021, 100002, ISSN 2667-0992, https://doi.org/10.1016/j.bea.2021.100002. | en_US |
dc.identifier.uri | http://hdl.handle.net/11019/3111 | |
dc.description | peer-reviewed | en_US |
dc.description.abstract | Background In the quest of the ideal material for scaffold fabrication for cartilage engineering, the use of collagen type II has been advocated, as it is the major constituent of cartilage tissue. Considering though the high batch-to-batch variability of animal-derived products, it is essential to identify suitable collagen type II sources. Methods Herein, we ventured to assess the influence of biological sex (male, female) and tissue (articular, tracheal, auricular) on the biophysical, biochemical and biological properties of pepsin extracted porcine collagen type II scaffolds. Results Articular cartilage resulted in pure collagen type II preparations, whilst tracheal and auricular cartilage preparations were contaminated with collagen type I. Pore size, porosity and denaturation temperature were not affected (p > 0.05) as a function of tissue and biological sex. Articular cartilage derived sponges exhibited significantly (p < 0.05) higher resistance to enzymatic degradation and biomechanical properties in comparison to tracheal and auricular cartilage sponges. Biological analysis using human adipose derived stem cells revealed no significant (p > 0.05) differences between the groups in cell viability, DNA concentration, metabolic activity and Alcian blue staining. In general, the articular cartilage groups induced the highest (p < 0.05) sulphated glycosaminoglycans synthesis and aggrecan and collagen type II mRNA expression (fold change ≥ 2.0). Conclusions Our data indicate a tissue memory of collagen type II and indicate that for cartilage engineering, articular cartilage derived collagen type II scaffolds may be more suitable for effective chondrogenesis. | en_US |
dc.language.iso | en | en_US |
dc.publisher | Elsevier | en_US |
dc.relation.ispartofseries | Biomedical Engineering Advances;Vol 1 | |
dc.rights | Attribution-NonCommercial-ShareAlike 4.0 International | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/4.0/ | * |
dc.subject | Collagen type II | en_US |
dc.subject | Adipose-derived stem cells | en_US |
dc.subject | Chondrogenic induction | en_US |
dc.subject | Cartilage engineering | en_US |
dc.title | In the quest of the optimal tissue source (porcine male and female articular, tracheal and auricular cartilage) for the development of collagen sponges for articular cartilage | en_US |
dc.type | Article | en_US |
dc.identifier.doi | https://doi.org/10.1016/j.bea.2021.100002 | |
dc.contributor.sponsor | Teagasc Walsh Fellowship | en_US |
dc.contributor.sponsor | Department of Agriculture, Food and the Marine under the National Development Plan 2007-2013 funded by the Irish Government | en_US |
dc.contributor.sponsor | Science Foundation Ireland | en_US |
dc.contributor.sponsor | Science Foundation Ireland | en_US |
dc.contributor.sponsor | Science Foundation Ireland / European Regional Development Fund | en_US |
dc.contributor.sponsor | European Research Council (ERC) | en_US |
dc.contributor.sponsor | European Union's Horizon 2020 research and innovation programme under the Marie Skłodowska-Curie | en_US |
dc.contributor.sponsorGrantNumber | 2014045 | en_US |
dc.contributor.sponsorGrantNumber | ReValueProtein Research Project (grant number: 11/F/043) | en_US |
dc.contributor.sponsorGrantNumber | 15/CDA/3629 | en_US |
dc.contributor.sponsorGrantNumber | 19/FFP/6982 | en_US |
dc.contributor.sponsorGrantNumber | 13/RC/2073 | en_US |
dc.contributor.sponsorGrantNumber | No. 866126 | en_US |
dc.contributor.sponsorGrantNumber | No. 676338 | en_US |
refterms.dateFOA | 2023-08-09T11:48:05Z |
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