Producción de proteínas recombinantes a partir de animales transgénicos: Sistemas y aplicaciones
Barra lateral del artículo
Publicado:
oct. 23, 2019
Palabras clave:
Biotecnología, Ingeniería Genética, animales transgénicos, proteínas recombinantes
Contenido principal del artículo
Resumen
El uso de animales transgénicos para la producción de proteínas recombinantes con fines terapéuticos ha sido una alternativa utilizada para la producción de medicamentos. La habilidad de realizar complejas modificaciones post traduccionales de una manera eficiente es una ventaja que este tipo de tecnología posee sobre el uso de otros organismos transgénicos. Por esta razón, a lo largo de los años se han desarrollado diferentes animales transgénicos (rumiantes, conejos, cerdos, aves e insectos) y se han estudiado distintos sistemas (leche, huevo, sangre, orina y fluido seminal) para la obtención de proteínas recombinantes. Cada animal y cada sistema cuenta con ventajas y desventajas, las cuales deben ser consideradas antes de comenzar el proceso productivo de la proteína de interés. Medicamentos como el ATryn®, el Ruconest® y el Kanuma® ya han sido aprobados por la FDA para la administración en humanos. El futuro de este tipo de preparados debe ser tomado en consideración, pues existen varias proteínas terapéuticas que se hallan en fase de investigación o a la espera de ser aprobadas y comercializadas.
Detalles del artículo
Cómo citar
Alvarado-Madrigal, M. F., Chavarría-Quirós, T., Leiva-Montero, B., & Mora-Román, J. J. (2019). Producción de proteínas recombinantes a partir de animales transgénicos: Sistemas y aplicaciones. Revista Tecnología En Marcha, 32(4), Pág. 133–144. https://doi.org/10.18845/tm.v32i4.4798
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Artículo científico
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Citas
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[23] Y. Durocher and Butler M, “Expression systems for therapeutic glycoprotein production,” Current Opinion in Biotechnology, 20(6), 700-707, 2009.
[24] A. L. Demain and P. Vaishnav, “Production of recombinant proteins by microbes and higher organisms,” Biotechnology Advances, 27(3), 297-306, 2009.
[25] A. Dove, “Uncorking the biomanufacturing bottleneck,” Nature Biotechnology, 20(8), 777-779, 2002.
[26] L. M. Houdebine, “Production of pharmaceutical proteins by transgenic animals,” Comparative Immunology, Microbiology & Infectious Diseases, 32(2), 107-121, 2009.
[27] M. K Dyck, D. Lacroix, F. Pothier, and M. -A. Sirard, “Making recombinant proteins in animals – different systems, different applications,” Trends in Biotechnology, 21(9), 394-399, 2003.
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[30] W. H. Eyestone, “Production and breeding of transgenic cattle using in vitro embryo production technology,” Theriogenology, 51(2), 509-517, 1999.
[31] M. Massoud, J. Attal, D. Thépot, H. Pointu, M. G. Stinnakre, M. C. Théron et al, “The deleterious effects of human erythropoietin gene driven by the rabbit when acidic protein gene promoter in transgenic rabbits”, Reproduction Nutrition Development, 36(5), 555-563, 1996.
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[33] K. Potočnik, V. Gantner, K. Kuterovac, and A. Cividini, “Mare´s milk: composition and protein fraction in comparison with different milk species,” Mljekarstvo, 61(2), 107-113, 2011.
[34] R. J. Wall, D. E. Kerr, and K. R. Bondioli, “Transgenic Dairy Cattle: Genetic Engineering on a Large Scale,” Journal of Dairy Science, 80(9), 2213-2224, 1997.
[35] T. D. Wilkins and W. Velander, “Isolation of recombinant proteins from milk,” Journal of Cellular Biochemistry, 49(4), 333-338, 1992.
[36] Z. L. Nikolov and S. L. Woodward, “Downstream processing of recombinant proteins from transgenic feedstock,” Current Opinion in Biotechnology, 15(5), 479-486, 2004.
[37] T. Morçöl, Q. He, and S. J. D. Bell, “Model Process for Removal of Caseins from Milk of Transgenic Animals,” Biotechnology Progress, 17(3), 577-582, 2001.
[38] A. J. Harvey, G. Speksnijder, L. R. Baugh, J. A. Morris, and R. Ivarie, “Expression of exogenous protein in the egg white of transgenic chickens,” Nature Biotechnology, 20(4), 396-399, 2002.
[39] T. S. Park, H. G. Lee, J. K. Moon, H. J. Lee, J. W. Yoon, B. N. Yun et al, “Deposition of bioactive human epidermal growth factor in the egg white of transgenic hens using an oviduct-specific minisynthetic promoter,” The FASEB Journal, 29(6), 2386-2396, 2015.
[40] Y. Wang, S. Zhao, L. Bai, J. Fan, and E. Liu, “Expression Systems and Species Used for Transgenic Animal Bioreactors,” BioMed Research International, 2013, 2013.
[41] E. Rehbinder, M. Engelhard, K. Hagen, and R. B. Jørgensen, R. Pardo-Avellaneda, A. Schnieke et al, “Promises and risks of biopharmaceuticals derived from genetically modified plants and animals,” Berlin: Springer-Verlag Berlin Heidelberg, 2009, p. 26.
[42] M. E. Swanson, M. J. Martin, J. K. O´Donnell, K. Hoover, W. Lago, V. Huntress et al, “Production of functional human hemoglobin in transgenic swine,” Biotechnology (N Y), 10(5), 557-559, 1992.
[43] V. G. Pursel, D. J. Bolt, K. F. Miller, C. A. Pinkert, R. E. Hammer, R. D. Palmiter et al, “Expression and performance in transgenic pigs,” Journal of Reproduction and Fertility. Supplement, 40, 235-245, 1990.
[44] D. E. Kerr, F. Liang, K. R. Bondioli, H. Zhao, G. Kreibich, R. J. Wall et al, “The bladder as a biorreactor: Urothelium production and secretion of growth hormone into urine,” Nature Biotechnology, 16 (1), 75-79, 1998.
[45] H. M. Zbikowska, N. Soukhareva, R. Behnam, R. Chang, R. Drews, H. Lubon et al, “The use of the uromodulin promoter to target production of recombinant proteins into urine of transgenic animals,” Transgenic Research, 11(4), 425-435, 2002.
[46] H. M. Zbikowska, N. Soukhareva, R. Behnam, H. Lubon, D. Hammond, and S. Soukharev, “Uromodulin promoter directs high-level expression of biologically active human α1-antitrypsin into mouse urine,” Biochemical Journal, 365 (Pt 1), 7-11, 2002.
[47] Z. Y. Ryoo, M. O. Kim, K. E. Kim, Y. Y. Bahk, J. W. Lee, S. H. Park et al, “Expression of recombinant human granulocyte macrophage-colony stimulating factor (hGM-CSF) in mouse urine,” Transgenic Research, 10(3), 193-200, 2001.
[48] P. Chrenek, A. V. Makarevich, J. Pivko, and J. Bulla, “Transgenic Farm Animal Production and Application,” Slovak Journal of Animal Science, 43(2): 45-49, 2010.
[49] L. R. Bertolini, H. Meade, C. R. Lazzarotto, L. T. Martins, K. C. Tavares, M. Bertolini et al, “The transgenic animal platform for biopharmaceutical production,” Transgenic Research, 25(3), 329-343, 2016.
[50] G. Wright, A. Carver, D. Cottom, D. Reeves, A. Scott, P. Simons et al, “High Level Expression of Active Human Alpha-1-Antitrypsin in the Milk of Transgenic Sheep,” Biotechnology (N Y), 9(9), 830-834, 1991.
[51] N. Rudolph, “Technologies and economics for protein production in transgenic animal milk”, Genetic Engineering News, 17(16), 36-37, 1997.
[52] H. Luboń and R. K. Paleyanda, “Vitamin K-dependent protein production in transgenic animals,” Thrombosis and Haemostasis, 78(1), 532-536.
[53] M. Tomita, H. Munetsuna, T. Sato, T. Adachi, R. Hino, M. Hayashi et al, “Transgenic silkworms produce recombinant human type III procollagen in cocoons,” Nature Biotechnology, 21(1), 52-56, 2003.
[54] S. Maeda, T. Kawai, M. Obinata, H. Fujiwara, T. Horuchi, Y. Saeki et al, “Production of human alpha-interferon in silkworm using a baculovirus vector,” Nature, 315 (6020), 592-594.
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