Recombinant expression systems for the production of collagen.
The ability of triple-helical collagen molecules to assemble into supramolecular structures forms the basis of commercial uses of collagen in the food industry and in medical applications such as cosmetic surgery and tissue repair. We have used cDNA techniques to engineer novel collagens with potentially enhanced biological properties; however, expression of fully functional novel molecules is difficult due to the complex nature of procollagen biosynthesis. This article outlines the application of various expression systems to procollagen production and details the use of the mammary gland as a suitable bioreactor for the synthesis of significant amounts of novel procollagens from cDNA constructs.
Bulleid
N J
NJ
School of Biological Sciences, Wellcome Trust Centre For Cell-Matrix Research, 2.205 Stopford Building, University of Manchester, Oxford Road, Manchester M13 9PT, U.K. neil.bulleid@man.ac.uk
John
D C
DC
Kadler
K E
KE
D000818:Animals; D001709:Biotechnology / Q000379:methods*; D002460:Cell Line; D003094:Collagen / Q000096:biosynthesis* / Q000737:chemistry*; D018076:DNA, Complementary / Q000378:metabolism; D005260:Female; D006801:Humans; D008321:Mammary Glands, Animal / Q000378:metabolism; D011347:Procollagen / Q000096:biosynthesis; D017510:Protein Folding; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000737:chemistry
D018076:DNA, Complementary; D011347:Procollagen; D011994:Recombinant Proteins; D003094:Collagen