In Vivo Biological Responses and Bioresorption of Tilapia Scale Collagen as a Potential Biomaterial

In Vivo Biological Responses and Bioresorption of Tilapia Scale Collagen as a Potential Biomaterial
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DOI:
10.1163/092050609x12457418396658
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发表时间:
2009-01-01
影响因子:
3.6
通讯作者:
Yasuda, Kazunori
Yasuda, Kazunori
中科院分区:
工程技术4区
文献类型:
--
作者:
Sugiura, Hiroaki;Yunoki, Shunji;Yasuda, Kazunori

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迄今为止,用于生物医学用途的胶原蛋白已从哺乳动物来源获得。本研究的目的是评估在体内的生物反应和生物吸收的胶原蛋白从罗非鱼(Oreochromis niloticas)鳞片相比,从猪真皮胶原蛋白。具有微孔结构的胶原海绵由使用冷冻干燥和通过去水热处理(DHT处理)或用水溶性碳二亚胺的附加处理(WSC处理)交联的重构胶原原纤维制成。罗非鱼胶原海绵的机械性能与具有相同交联方法的猪胶原海绵的机械性能相似,其中WSC处理显著改善了单独的DHT处理的性能。将颗粒植入家兔椎旁肌的试验表明,罗非鱼胶原蛋白在植入1周和4周时引起罕见的炎症反应,在统计学上与猪胶原蛋白和作为阴性对照的高密度聚乙烯相似。两种胶原蛋白植入物的生物吸收率相似,除了在植入1周时经DHT处理的罗非鱼胶原蛋白海绵。这些结果表明,罗非鱼胶原蛋白是一个潜在的替代传统的哺乳动物胶原蛋白在生物医学用途。(C)Koninklijke Brill NV,莱顿,2009年
To date, collagen for biomedical uses has been obtained from mammalian sources. The purpose of this study was to evaluate the in vivo biological responses and bioresorption of collagen obtained from tilapia (Oreochromis niloticas) scales as compared to those of collagen from porcine dermis. Collagen sponges with micro-porous structures were fabricated from reconstituted collagen fibrils using freeze-drying and cross-linked by dehydrothermal treatment (DHT treatment) or additional treatment with a water-soluble carbodiimide (WSC treatment). The mechanical properties of the tilapia collagen sponges were similar to those of porcine collagen sponges with the same cross-linking methods, where WSC treatment remarkably improved the properties over DHT treatment alone. The pellet implantation tests into the paravertebral muscle of rabbits demonstrated that tilapia collagen caused rare inflammatory responses at 1- and 4-week implantations, statistically similar to those of porcine collagen and a high-density polyethylene as a negative control. The bioresorption rates of both the collagen implants were similar, except for the DHT-treated tilapia collagen sponges at 1-week implantation. These results suggest that tilapia collagen is a potential alternative to conventional mammalian collagens in biomedical uses. (C) Koninklijke Brill NV, Leiden, 2009