Abstract
Most of the efforts in the pharmaceutical industry are directed toward human medicine, but quite often these concepts and breakthroughs also find parallel applications in veterinary medicine. However, we will not discuss here those possible applications to veterinary science which are not primarily directed towards alleviation of disease such as the possible use of growth hormones in animal husbandry. The term “genetic engineering” will be used to designate the cloning of genes in a heterologous genetic context, and especially the efficient expression of these cloned genes in heterologous cells. Therefore, the use of chemically synthesized peptides in medicine will not be further considered here. It is generally accepted that the cutoff for economical chemical synthesis of peptides is about 20–30 amino acids; above that, genetic engineering methodology becomes the method of choice.
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References
Content, J.; De Wit, L.; Derynck, R.; De Clercq, E.; and Fiers, W. 1982. In vitro cotranslation processing of human pre interferon β1 enhances its biological activity. Virology 122: 466–470.
Crea, R.; Kraszewski, A.; Hirose, T.; and Itakura, K. 1978. Chemical synthesis of genes for human insulin. Proc. Natl. Acad. Sci. USA 75: 5765–5769.
Derynck, R.; Content, J.; De Clercq, E.; Volckaert, G.; Tavernier, J.; Devos, R.; and Fiers, W. 1980. Isolation and structure of a human fibroblast interferon gene. Nature 285: 542–546.
Devos, R.; Cheroutre, H.; Taya, Y.; Degrave, W.; Van Heuverswyn, H.; and Fiers, W. 1982. Molecular cloning of human immune interferon cDNA and its expression in eukaryotic cells. Nucl. Acids Res. 10: 2487–2501.
Devos, R.; Plaetinck, G.; Cheroutre, H.; Simons, G.; Degrave, W.; Tavernier, J.; Remaut, E.; and Fiers, W. 1983. Molecular cloning of human interleukin 2 cDNA and its expression in E. coli. Nucl. Acids Res. 11: 4307–4323.
Edge, M.D.; Greene, S.R.; Heathcliffe, G.R.; Meacock, P.A.; Schuch, W.; Scanlon, D.B.; Atkinson, T.C.; Newton, C.R.; and Markham, S.F. 1981. Total synthesis of a human leucocyte interferon gene. Nature 292: 756–762.
Gray, P., et al. 1982. Expression of human immune interferon cDNA in E. coli and monkey cells. Nature 295: 503–508.
Itakura, K.; Hirose, T.; Crea, R.; Riggs, A.D.; Heyneker, H.L.; Bolivar, F. ; and Boyer, H.W. 1977. Expression in Escherichia coli of a chemically synthesized gene for the hormone somatostatin. Science 198: 1056–1063.
Kaufman, R.J., and Sharp, P.A. 1982. Construction of a modular dihydrofolate reductase cDNA gene: Analysis of signals utilized for efficient expression. Molec. Cell. Biol. 2: 1304–1319.
Mark, D.V.; Ru, S.D.; Creasey, A.; Yaniamoto, R.; and Lin, L. 1984. Site-specific mutagenesis of the Human Fibroblast Interferon Gene: A structure-function analysis of the protein. Proc. Natl. Acad. Sci. USA 81: 5662–5666.
Nagata, S.; Taira, H.; Hall, A.; Johnsrud, L.; Streuli, M.; Ecsodi, J.; Boll, W.; Cantell, K.; and Weissmann, C. 1980. Synthesis in E. coli of a polypeptide with human leukocyte interferon activity. Nature 284: 316–320
Okayama, H., and Berg, P. 1982. High-efficiency cloning of full length cDNA. Molec. Cell. Biol. 2: 161–170.
Palva, I.; Petterson, R.F.; Kalkkinen, N.; Lehtovaara, P.; Sarvas, M.; Söderland, H.; Takkinen, K.; and Kääriäinnen, L. 1981. Nucleotide sequence of the promoter and NH2-terminal signal peptide region of the α-amylase gene from Bacillus amyloliquefaciens. Gene 15: 43–51.
Scahill, S.J.; Devos, R.; Van der Heyden, J.; and Fiers, W. 1983. Expression and characterization of the product of a human immune interferon cDNA gene in Chinese hamster ovary cells. Proc. Natl. Acad. Sci. USA 80: 4654–4658.
Simons, G.; Remaut, E.; Allet, B.; and Fiers, W. 1984. High-level expression of human interferon gamma in Escherichia coli under control of the pL promoter of bacteriophage lambda. Gene 28: 55–64.
Taniguchi, T.; Matsui, H.; Fujita, T.; Takaoka, C.; Kashima, N.; Yoshimoto, R.; and Hamuro, J. 1983. Structure and expression of a cloned cDNA for human interleukin-2. Nature 302: 305–310.
Taniguchi, T.; Sakai, M.; Fujii-Kuriyama, Y.; Muramatsu, M.; Kobayashi, S.; and Sudo, T. 1979. Construction and identification of a bacterial plasmid containing the human fibroblast interferon gene sequence. Proc. Jpn. Acad. 55(B): 464–469.
Toole, J.J., et al. 1984. Molecular cloning of a cDNA encoding human antihaemophilic factor. Nature 312: 342–347.
Wood, W.I., et al. 1984. Expression of active human factor VIII from recombinant DNA clones. Nature 312: 330–337.
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© 1986 Dr. S. Bernhard, Dahlem Konferenzen, Berlin
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Fiers, W. (1986). The Future Role in Medicine of Proteins Made by Genetic Engineering. In: Silver, S. (eds) Biotechnology: Potentials and Limitations. Dahlem Workshop Reports, vol 35. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-70535-9_13
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DOI: https://doi.org/10.1007/978-3-642-70535-9_13
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