Abstract
The collagens are a family of closely related but distinct extracellular matrix proteins that play a dominant role in maintaining the structural integrity of various tissues and organs (1). Type I collagen is the most abundant member of the collagen family and it is found in most connective tissues. It is currently used as a biomaterial in numerous medical applications and as a delivery system for various drugs. In addition, all gelatins widely used in pharmaceutical, food and beverage industries are prepared from collagens. The collagens used in all these applications have been isolated from animal tissues and are liable to cause allergic reactions in some subjects and carry a risk of disease-causing contaminants. More than 20 proteins have now been defined as collagens (1). The various collagen types have different properties, and therefore some of the other collagens might be more suitable for certain applications than type I. However, it has been difficult or impossible to isolate sufficient quantities of the other collagens from animal tissues. An efficient large-scale recombinant system for the production of human collagens would thus have numerous applications in medicine.
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Myllyharju, J. (2003). Recombinant expression of human collagens. In: Yagasaki, K., Miura, Y., Hatori, M., Nomura, Y. (eds) Animal Cell Technology: Basic & Applied Aspects. Animal Cell Technology: Basic & Applied Aspects, vol 13. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-0726-8_1
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DOI: https://doi.org/10.1007/978-94-017-0726-8_1
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