title: Isolation, characterization and biological evaluation of jellyfish collagen for use in biomedical applications.
abstract: 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.
authors: Université Lyon 1, Univ Lyon, CNRS, FRE 3310, Dysfonctionnement de l'Homéostasie Tissulaire et Ingénierie Thérapeutique, IBCP, 7 passage du Vercors, F-69367, France.
authors: Sourour
authors: S
authors: Addad
authors: Université Lyon 1, Univ Lyon, CNRS, FRE 3310, Dysfonctionnement de l'Homéostasie Tissulaire et Ingénierie Thérapeutique, IBCP, 7 passage du Vercors, F-69367, France.
authors: Jean-Yves
authors: JY
authors: Exposito
authors: Université Lyon 1, Univ Lyon, CNRS, UMR 5086, Bases Moléculaires et Structurales des Systèmes Infectieux, IBCP 7 passage du Vercors, F-69367, France.
authors: Clément
authors: C
authors: Faye
authors: Université Lyon 1, Univ Lyon, CNRS, UMR 5086, Bases Moléculaires et Structurales des Systèmes Infectieux, IBCP 7 passage du Vercors, F-69367, France.
authors: Sylvie
authors: S
authors: Ricard-Blum
authors: Université Lyon 1, Univ Lyon, CNRS, FRE 3310, Dysfonctionnement de l'Homéostasie Tissulaire et Ingénierie Thérapeutique, IBCP, 7 passage du Vercors, F-69367, France.
authors: Claire
authors: C
authors: Lethias
mesh_terms: D000818:Animals; D016466:CHO Cells; D002448:Cell Adhesion / Q000187:drug effects / Q000502:physiology; D002460:Cell Line; D003094:Collagen / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D006224:Cricetinae; D003412:Cricetulus; D005347:Fibroblasts / Q000187:drug effects / Q000378:metabolism; D006801:Humans; D008522:Mediterranean Sea; D051381:Rats; D037401:Scyphozoa / Q000737:chemistry*
chemical_list: D003094:Collagen