Université Lyon 1, Univ Lyon, CNRS, FRE 3310, Dysfonctionnement de l'Homéostasie Tissulaire et Ingénierie Thérapeutique, IBCP, 7 passage du Vercors, F-69367, France.
Université Lyon 1, Univ Lyon, CNRS, UMR 5086, Bases Moléculaires et Structurales des Systèmes Infectieux, IBCP 7 passage du Vercors, F-69367, France.
Mar Drugs. 2011;9(6):967-983. doi: 10.3390/md9060967. Epub 2011 Jun 7.
Fibrillar collagens are the more abundant extracellular proteins. They form a metazoan-specific family, and are highly conserved from sponge to human. Their structural and physiological properties have been successfully used in the food, cosmetic, and pharmaceutical industries. On the other hand, the increase of jellyfish has led us to consider this marine animal as a natural product for food and medicine. Here, we have tested different Mediterranean jellyfish species in order to investigate the economic potential of their collagens. We have studied different methods of collagen purification (tissues and experimental procedures). The best collagen yield was obtained using Rhizostoma pulmo oral arms and the pepsin extraction method (2-10 mg collagen/g of wet tissue). Although a significant yield was obtained with Cotylorhiza tuberculata (0.45 mg/g), R. pulmo was used for further experiments, this jellyfish being considered as harmless to humans and being an abundant source of material. Then, we compared the biological properties of R. pulmo collagen with mammalian fibrillar collagens in cell cytotoxicity assays and cell adhesion. There was no statistical difference in cytotoxicity (p > 0.05) between R. pulmo collagen and rat type I collagen. However, since heparin inhibits cell adhesion to jellyfish-native collagen by 55%, the main difference is that heparan sulfate proteoglycans could be preferentially involved in fibroblast and osteoblast adhesion to jellyfish collagens. Our data confirm the broad harmlessness of jellyfish collagens, and their biological effect on human cells that are similar to that of mammalian type I collagen. Given the bioavailability of jellyfish collagen and its biological properties, this marine material is thus a good candidate for replacing bovine or human collagens in selected biomedical applications.
纤维胶原蛋白是更为丰富的细胞外蛋白质。它们形成后生动物特有的家族，并且在海绵到人类之间具有高度的保守性。它们的结构和生理特性已成功应用于食品、化妆品和制药行业。另一方面，水母数量的增加促使我们将这种海洋动物视为食品和药物的天然产物。在这里，我们测试了不同的地中海水母物种，以研究其胶原蛋白的经济潜力。我们研究了不同的胶原蛋白纯化方法（组织和实验程序）。使用海蜇口腕和胃蛋白酶提取方法（2-10mg 胶原蛋白/克湿组织）可获得最佳胶原蛋白产量。尽管从海月水母中获得了显著的产量（0.45mg/g），但我们还是使用海蜇进行了进一步的实验，因为这种水母被认为对人类无害，并且是一种丰富的材料来源。然后，我们在细胞毒性测定和细胞黏附中比较了海蜇胶原蛋白与哺乳动物纤维胶原蛋白的生物学特性。在细胞毒性方面（p>0.05），海蜇胶原蛋白与大鼠 I 型胶原蛋白之间没有统计学差异。然而，由于肝素可抑制 55%的肝素硫酸盐蛋白聚糖与水母天然胶原蛋白的黏附，因此主要区别在于肝素硫酸盐蛋白聚糖可能优先参与成纤维细胞和成骨细胞与水母胶原蛋白的黏附。我们的数据证实了水母胶原蛋白的广泛无害性，以及其对人类细胞的生物学效应与哺乳动物 I 型胶原蛋白相似。鉴于水母胶原蛋白的生物利用度及其生物学特性，这种海洋材料是替代某些生物医学应用中的牛或人胶原蛋白的良好候选物。
