Human extracellular superoxide dismutase (EC-SOD) expression in transgenic chicken
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Extracellular superoxide dismutase (EC-SOD) is a metalloprotein and functions as an antioxidant enzyme. In this study,we used lentiviral vectors to generate transgenic chickens that express the human EC-SOD gene. The recombinant lentiviruses were injected into the subgerminal cavity of freshly laid eggs. Subsequently, the embryos were incubated to hatch using phases II and III of the surrogate shell ex vivo culture system. Of 158 injected embryos, 16 chicks (G0) hatched and were screened for the hEC-SOD by PCR. Only 1 chick was identified as a transgenic bird containing the transgene in its germline. This founder (G0) bird was mated with wild-type hens to produce transgenic progeny, and 2 transgenic chicks (G1) were produced. In the generated transgenic hens (G2),the hEC-SOD protein was expressed in the egg white and showed antioxidant activity. These results highlight the potential of the chicken for production of biologically active proteins in egg white.
Abstract
Extracellular superoxide dismutase (EC-SOD) is a metalloprotein and functions as an antioxidant enzyme. In this study,we used lentiviral vectors to generate transgenic chickens that express the human EC-SOD gene. The recombinant lentiviruses were injected into the subgerminal cavity of freshly laid eggs. Subsequently, the embryos were incubated to hatch using phases II and III of the surrogate shell ex vivo culture system. Of 158 injected embryos, 16 chicks (G0) hatched and were screened for the hEC-SOD by PCR. Only 1 chick was identified as a transgenic bird containing the transgene in its germline. This founder (G0) bird was mated with wild-type hens to produce transgenic progeny, and 2 transgenic chicks (G1) were produced. In the generated transgenic hens (G2),the hEC-SOD protein was expressed in the egg white and showed antioxidant activity. These results highlight the potential of the chicken for production of biologically active proteins in egg white.
참고문헌 (27)
- Durocher, Y, "Expression systems for therapeutic glycoprotein production", Curr. Opin. Biotechnol, 20, pp.700~707 (2009)
- O'Callaghan, P. M., "Systems biotechnology of mammalian cell factories", Brief Funct. Genomic. Proteomic, 7, pp.95~110 (2008)
- Harrison, R. L., "Protein N-glycosylation in the baculovirus-insect cell expression system and engineering of insect cells to produce "mammalianized" recombinant glycoproteins", Adv. Virus Res, 68, pp.159~191 (2006)
- Ward, M., "Characterization of humanized antibodies secreted by Aspergillus niger", Appl. Environ. Microbiol, 70, pp.2567~2576 (2004)
- Koo, B. C., "Tetracycline-dependent expression of the human erythropoietin gene in transgenic chickens", Transgenic Res, 19, pp.437~447 (2010)
- Kling, J., "First US approval for a transgenic animal drug", Nat. Biotechnol, 27, pp.302~304 (2009)
- Zhu, L., "Production of human monoclonal antibody in eggs of chimeric chickens", Nat. Biotechnol, 23, pp.1159~1169 (2005)
- Kwon, S. C., "Production of biofunctional recombinant human interleukin 1 receptor antagonist (rhIL1RN) from transgenic quail egg white", Biol. Reprod, 82, pp.1057~1064 (2010)
- Lillico, S. G., "Transgenic chickens as bioreactors for protein- based drugs", Drug Discov. Today, 10, pp.191~196 (2005)
- Harvey, A. J., "Expression of exogenous protein in the egg white of transgenic chickens", Nat. Biotechnol, 20, pp.396~399 (2002)
- Kwon, M. S., "Development of transgenic chickens expressing enhanced green fluorescent protein", Biochem. Biophys. Res. Commun, 320, pp.442~448 (2004)
- Lillico, S. G., "Oviduct-specific expression of two therapeutic proteins in transgenic hens", Proc. Natl. Acad. Sci. U.S.A, 104, pp.1771~1776 (2007)
- Antonyuk, S. V., "The structure of human extracellular copper-zinc superoxide dismutase at 1.7 A resolution: insights into heparin and collagen binding", J. Mol. Biol, 388, pp.310~326 (2009)
- Fattman, C. L., "Extracellular superoxide dismutase in biology and medicine", Free Radic. Biol. Med, 35, pp.236~256 (2003)
- Petersen, S. V., "The high concentration of Arg213-->Gly extracellular superoxide dismutase (EC-SOD) in plasma is caused by a reduction of both heparin and collagen affinities", Biochem. J, 385, pp.427~432 (2005)
- Nozik-Grayck, E., "Extracellular superoxide dismutase", Int. J. Biochem. Cell Biol, 37, pp.2466~2471 (2005)
- Oury, T. D., "Extracellular superoxide dismutase in vessels and airways of humans and baboons", Free Radic. Biol. Med, 20, pp.957~965 (1996)
- Byun, S. J., "Oviduct-specific enhanced green fluorescent protein expression in transgenic chickens", Biosci. Biotechnol. Biochem, 75, pp.646~649 (2011)
- Tibell, L., "Expression of human extracellular superoxide dismutase in Chinese hamster ovary cells and characterization of the product", Proc. Natl. Acad. Sci. U.S.A, 84, pp.6634~6638 (1987)
- He, H. J., "High-level expression of human extracellular superoxide dismutase in Escherichia coli and insect cells", Protein. Expr. Purif, 24, pp.13~17 (2002)
- Chen, H. L., "Production and characterization of human extracellular superoxide dismutase in the methylotrophic yeast Pichia pastoris", J. Agric. Food Chem, 54, pp.8041~8047 (2006)
- Son, Y. J., "Expression, high cell density culture and purification of recombinant EC-SOD in Escherichia coli", Appl. Biochem. Biotechnol, 162, pp.1585~1598 (2010)
- Houdebine, L. M., "Production of pharmaceutical proteins by transgenic animals", Comp. Immunol. Microbiol. Infect. Dis, 32, pp.107~121 (2009)
- Alper, J., "Biotechnology. Hatching the golden egg: a new way to make drugs", Science, 300, pp.729~730 (2003)
- Robertson, G., "Position-dependent variegation of globin transgene expression in mice", Proc. Natl. Acad. Sci. U. S. A, 92, pp.5371~5375 (1995)
- Dobie, K. W., "Variegated transgene expression in mouse mammary gland is determined by the transgene integration locus", Proc. Natl. Acad. Sci. U. S. A, 93, pp.6659~6664 (1996)
- Thiels, E., "Impairment of long-term potentiation and associative memory in mice that overexpress extracellular superoxide dismutase", J. Neurosci, 20, pp.7631~7639.9 (2000)
