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.

Preparation and characterization of monomers to tetramers of a collagen-like domain fromStreptococcus pyogenes

“…5 C. This value is about 0.7 C higher than previously reported (36.8 C). 21 A T m was determined for V-(CL) 2 of 37.6 C ( Table 1), which was also slightly higher than a value (37.1 C) previously reported.…”

“…There have also been concerns that these animalderived collagens may also lead to the transmission of diseases, particularly spongiform encephalopathies including "mad cow disease." Other non-mammalian tissue sources have been proposed to minimize risks of disease, including avian, 3 piscine 4 and cnidarian (jellyfish) 5 sources. The alternative, which also addresses variability and quality issues, is to examine production of recombinant collagens.…”

Jellyfish fisheries in the Americas: origin, state of the art, and perspectives on new fishing grounds

“…Most of the above applications do not require the removal of jellyfish from the wild at commercial scales. One exception is the processing of jellyfish to extract collagen, which may be used in a variety of applications including cosmetics and pharmaceuticals (Addad et al 2011). One company based in France (www.javenech.com, accessed 26 June 2015) processes several tonnes of Rhizostoma pulmo caught in the Atlantic Ocean for collagen each year.…”

Preliminary assessment of the jellyfish bycatch captured off southern and southeastern Brazil

“…This fact has prompted interest in these organisms, both ecologically and in terms of use in different segments of human activity, involving its use in food (Schiariti, 2008), obtaining bioactive products for pharmacology (Addad et al, 2011) as well as interest on public health due to poisoning of bathers (Resgalla Jr. et al, 2011).…”