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Journal of Biomedicine and Biotechnology
Volume 2010 (2010), Article ID 405872, 11 pages
http://dx.doi.org/10.1155/2010/405872
Research Article

Enhancement of Human Prolactin Synthesis by Sodium Butyrate Addition to Serum-Free CHO Cell Culture

Biotechnology Department, IPEN-CNEN, Cidade Universitária, Avenida Professor Lineu Prestes 2242, 05508-900 São Paulo, SP, Brazil

Received 28 October 2009; Revised 9 February 2010; Accepted 1 April 2010

Academic Editor: Yujun George Zheng

Copyright © 2010 Herbert Rodrigues Goulart et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. M. C. Tettamanzi, C. Keeler, S. Meshack, and M. E. Hodsdon, “Analysis of site-specific histidine protonation in human prolactin,” Biochemistry, vol. 47, no. 33, pp. 8638–8647, 2008. View at Publisher · View at Google Scholar · View at Scopus
  2. M. E. Freeman, B. Kanyicska, A. Lerant, and G. Nagy, “Prolactin: structure, function, and regulation of secretion,” Physiological Reviews, vol. 80, no. 4, pp. 1523–1631, 2000. View at Google Scholar · View at Scopus
  3. G. Goodman and D. Bercovich, “Prolactin does not cause breast cancer and may prevent it or be therapeutic in some conditions,” Medical Hypotheses, vol. 70, no. 2, pp. 244–251, 2008. View at Publisher · View at Google Scholar · View at Scopus
  4. N. Ben-Jonathan, J. L. Mershon, D. L. Allen, and R. W. Steinmetz, “Extrapituitary prolactin: distribution, regulation, functions, and clinical aspects,” Endocrine Reviews, vol. 17, no. 6, pp. 639–669, 1996. View at Publisher · View at Google Scholar · View at Scopus
  5. N. Ben-Jonathan, K. Liby, M. McFarland, and M. Zinger, “Prolactin as an autocrine/paracrine growth factor in human cancer,” Trends in Endocrinology and Metabolism, vol. 13, no. 6, pp. 245–250, 2002. View at Publisher · View at Google Scholar · View at Scopus
  6. L. Morganti, M. Huyer, P. W. Gout, and P. Bartolini, “Production and characterization of biologically active Ala-Ser-(His)6-lle-Glu-Gly-Arg-human prolactin (tag-hPRL) secreted in the periplasmic space of Escherichia coli,” Biotechnology and Applied Biochemistry, vol. 23, no. 1, pp. 67–75, 1996. View at Google Scholar · View at Scopus
  7. L. Morganti, C. R. J. Scares, R. Affonso, P. W. Gout, and P. Bartolini, “Synthesis and characterization of recombinant, authentic human prolactin secreted into the periplasmic space of Escherichia coli,” Biotechnology and Applied Biochemistry, vol. 27, part 1, pp. 63–70, 1998. View at Google Scholar · View at Scopus
  8. C. R. J. Soares, L. Morganti, B. Miloux, J. H. Lupker, P. Ferrara, and P. Bartolini, “High-level synthesis of human prolactin in Chinese-hamster ovary cells,” Biotechnology and Applied Biochemistry, vol. 32, no. 2, pp. 127–135, 2000. View at Google Scholar · View at Scopus
  9. C. R. J. Soares, A. Glezer, K. Okazaki et al., “Physico-chemical and biological characterizations of two human prolactin analogs exhibiting controversial bioactivity, synthesized in Chinese hamster ovary (CHO) cells,” Protein Expression and Purification, vol. 48, no. 2, pp. 182–194, 2006. View at Publisher · View at Google Scholar · View at Scopus
  10. C. R. J. Soares, E. K. M. Ueda, T. L. Oliveira, F. I. C. Gomide, S. R. Heller, and P. Bartolini, “Distinct human prolactin (hPRL) and growth hormone (hGH) behavior under bacteriophage lambda P promoter control: temperature plays a major role in protein yields,” Journal of Biotechnology, vol. 133, no. 1, pp. 27–35, 2008. View at Publisher · View at Google Scholar · View at Scopus
  11. J. R. Davie, “Inhibition of histone deacetylase activity by butyrate,” Journal of Nutrition, vol. 133, no. 7, supplement, pp. 2485S–2493S, 2003. View at Google Scholar · View at Scopus
  12. M.-P. Leibovitch, S.-A. Leibovitch, J. Harel, and J. Kruh, “Effect of sodium butyrate on messenger RNA populations in myogenic cells in culture,” Differentiation, vol. 22, no. 2, pp. 106–112, 1982. View at Google Scholar · View at Scopus
  13. D. Y. Lee, J. J. Hayes, D. Pruss, and A. P. Wolffe, “A positive role for histone acetylation in transcription factor access to nucleosomal DNA,” Cell, vol. 72, no. 1, pp. 73–84, 1993. View at Publisher · View at Google Scholar · View at Scopus
  14. N. S. Kim and G. M. Lee, “Overexpression of bcl-2 inhibits sodium butyrate-induced apoptosis in Chinese hamster ovary cells resulting in enhanced humanized antibody production,” Biotechnology and Bioengineering, vol. 71, no. 3, pp. 184–193, 2000. View at Publisher · View at Google Scholar · View at Scopus
  15. Y. Mimura, J. Lund, S. Church et al., “Butyrate increases production of human chimeric IgG in CHO-K1 cells whilst maintaining function and glycoform profile,” Journal of Immunological Methods, vol. 247, no. 1-2, pp. 205–216, 2001. View at Publisher · View at Google Scholar · View at Scopus
  16. K. O. Han, K. S. Moon, J. Yang et al., “Effect of N-Acetylcystein on butyrate-treated Chinese hamster ovary cells to improve the production of recombinant human interferon-beta-1a,” Biotechnology Progress, vol. 21, no. 4, pp. 1154–1164, 2005. View at Publisher · View at Google Scholar · View at Scopus
  17. H. S. Yun and M. L. Gyun, “Enhanced human thrombopoietin production by sodium butyrate addition to serum-free suspension culture of Bcl-2-overexpressing CHO cells,” Biotechnology Progress, vol. 21, no. 1, pp. 50–57, 2005. View at Publisher · View at Google Scholar · View at Scopus
  18. C. R. J. Soares, I. M. C. Camargo, L. Morganti et al., “Reversed-phase high-performance liquid chromatography method for the determination of prolactin in bacterial extracts and in its purified form,” Journal of Chromatography A, vol. 955, no. 2, pp. 229–236, 2002. View at Publisher · View at Google Scholar · View at Scopus
  19. S. Dalmora, J. E. Oliveira, R. Affonso, E. Gimbo, M. T. C. P. Ribela, and P. Bartolini, “Analysis of recombinant human growth hormone directly in osmotic shock fluids,” Journal of Chromatography A, vol. 782, no. 2, pp. 199–210, 1997. View at Publisher · View at Google Scholar · View at Scopus
  20. J. R. Tennant, “Evaluation of the trypan blue technique for determination of cell viability,” Transplantation, vol. 2, pp. 685–694, 1964. View at Google Scholar · View at Scopus
  21. B. J. Bassam, G. Caetano-Anolles, and P. M. Gresshoff, “Fast and sensitive silver staining of DNA in polyacrylamide gels,” Analytical Biochemistry, vol. 196, no. 1, pp. 80–83, 1991. View at Google Scholar · View at Scopus
  22. U. K. Laemmli, “Cleavage of structural proteins during the assembly of the head of bacteriophage T4,” Nature, vol. 227, no. 5259, pp. 680–685, 1970. View at Publisher · View at Google Scholar · View at Scopus
  23. D. D. Bannerman, J. C. Tupper, R. D. Erwert, R. K. Winn, and J. M. Harlan, “Divergence of bacterial lipopolysaccharide pro-apoptotic signaling downstream of IRAK-1,” Journal of Biological Chemistry, vol. 277, no. 10, pp. 8048–8053, 2002. View at Publisher · View at Google Scholar · View at Scopus
  24. M. T. C. P. Ribela, A. C. Bianco, and P. Bartolini, “The use of recombinant human thyrotropin produced by Chinese hamster ovary cells for the preparation of immunoassay reagents,” Journal of Clinical Endocrinology and Metabolism, vol. 81, no. 1, pp. 249–256, 1996. View at Publisher · View at Google Scholar · View at Scopus
  25. M. T. C. P. Ribela, P. W. Gout, J. E. Oliveira, and P. Bartolini, “HPLC analysis of human pituitary hormones for pharmaceutical applications,” Current Pharmaceutical Analysis, vol. 2, no. 2, pp. 103–126, 2006. View at Publisher · View at Google Scholar · View at Scopus
  26. G. W. White, T. Katona, and J. P. Zodda, “The use of high-performance size exclusion chromatography (HPSEC) as a molecular weight screening technique for polygalacturonic acid for use in pharmaceutical applications,” Journal of Pharmaceutical and Biomedical Analysis, vol. 20, no. 6, pp. 905–912, 1999. View at Publisher · View at Google Scholar · View at Scopus
  27. A. Glezer, C. R. J. Soares, J. G. Vieira et al., “Human macroprolactin displays low biological activity via its homologous receptor in a new sensitive bioassay,” Journal of Clinical Endocrinology and Metabolism, vol. 91, no. 3, pp. 1048–1055, 2006. View at Publisher · View at Google Scholar · View at Scopus
  28. B. Rafferty, P. Rigsby, R. E. Gaines-Das et al., “Draft report of an international collaborative study of proposed WHO reference reagents for rDNA-derived prolactin and its glycosylated and non-glycosylated componentes,” WHO Technical Report Series, vol. 52, no. 924, 2001. View at Google Scholar
  29. T.-J. Chen, C. B. Kuo, K. F. Tsai, J. O.-W. Liu, D.-Y. Chen, and A. M. Walker, “Development of recombinant human prolactin receptor antagonists by molecular mimicry of the phosphorylated hormone,” Endocrinology, vol. 139, no. 2, pp. 609–616, 1998. View at Publisher · View at Google Scholar · View at Scopus
  30. Y.-S. Lee, H. Nakajima, Y.-C. Chang et al., “Alleviation of apoptosis by serum in Chinese hamster ovary cells ectopically expressing human Fas antigen,” Molecules and Cells, vol. 8, no. 3, pp. 272–279, 1998. View at Google Scholar · View at Scopus
  31. S. R. Heller, H. Rodrigues Goulart, F. S. Arthuso, T. L. Oliveira, P. Bartolini, and C. R. J. Soares, “Synthesis, purification and characterization of recombinant glycosylated human prolactin (G-hPRL) secreted by cycloheximide-treated CHO cells,” Journal of Biotechnology, vol. 145, no. 4, pp. 334–340, 2010. View at Publisher · View at Google Scholar · View at Scopus
  32. M. T. C. P. Ribella and P. Bartolini, “Stokes radius determination of radioiodinated polypeptide hormones by gel filtration,” Analytical Biochemistry, vol. 174, no. 2, pp. 693–697, 1988. View at Google Scholar · View at Scopus
  33. C. M. Carvalho, J. E. Oliveira, B. E. Almeida et al., “Efficient isolation of the subunits of recombinant and pituitary glycoprotein hormones,” Journal of Chromatography A, vol. 1216, no. 9, pp. 1431–1438, 2009. View at Publisher · View at Google Scholar · View at Scopus
  34. V. Medina, B. Edmonds, G. P. Young, R. James, S. Appleton, and P. D. Zalewski, “Induction of caspase-3 protease activity and apoptosis by butyrate and trichostatin a (inhibitors of histone deacetylase): dependence on protein synthesis and synergy with a mitochondrial/cytochrome c-dependent pathway,” Cancer Research, vol. 57, no. 17, pp. 3697–3707, 1997. View at Google Scholar · View at Scopus
  35. P. J. Smith, “n-Butyrate alters chromatin accessibility to DNA repair enzymes,” Carcinogenesis, vol. 7, no. 3, pp. 423–429, 1986. View at Google Scholar · View at Scopus
  36. T. Tanaka, R. P. C. Shiu, and P. W. Gout, “A new sensitive and specific bioassay for lactogenic hormones: measurement of prolactin and growth hormone in human serum,” Journal of Clinical Endocrinology & Metabolism, vol. 51, no. 5, pp. 1058–1063, 1980. View at Google Scholar · View at Scopus
  37. S. Bernichtein, S. Jeay, R. Vaudry, P. A. Kelly, and V. Goffin, “New homologous bioassays for human lactogens show that agonism or antagonism of various analogs is a function of assay sensitivity,” Endocrine, vol. 20, no. 1-2, pp. 177–190, 2003. View at Publisher · View at Google Scholar · View at Scopus
  38. C. K. Crowell, Q. Qin, G. E. Grampp, R. A. Radcliffe, G. N. Rogers, and R. I. Scheinman, “Sodium butyrate alters erythropoietin glycosylation via multiple mechanisms,” Biotechnology and Bioengineering, vol. 99, no. 1, pp. 201–213, 2008. View at Publisher · View at Google Scholar · View at Scopus
  39. R. Damiani, J. E. Oliveira, K. Vorauer-Uhl et al., “Stable expression of a human-like sialylated recombinant thyrotropin in a Chinese hamster ovary cell line expressing alpha2,6-sialyltransferase,” Protein Expression and Purification, vol. 67, no. 1, pp. 7–14, 2009. View at Publisher · View at Google Scholar · View at Scopus
  40. C. F. Goochee, M. J. Gramer, D. C. Andersen, J. B. Bahr, and J. R. Rasmussen, “The oligosaccharides of glycoproteins: bioprocess factors affecting oligosaccharide structure and their effect on glycoprotein properties,” Biotechnology, vol. 9, no. 12, pp. 1347–1355, 1991. View at Publisher · View at Google Scholar · View at Scopus
  41. F. Mendonça, J. E. Oliveira, P. Bartolini, and M. T. C. P. Ribela, “Two-step chromatographic purification of recombinant human thyrotrophin and its immunological, biological, physico-chemical and mass spectral characterization,” Journal of Chromatography A, vol. 1062, no. 1, pp. 103–112, 2005. View at Publisher · View at Google Scholar · View at Scopus
  42. M. W. Szkudlinski, V. Fremont, C. Ronin, and B. D. Weintraub, “Thyroid-stimulating hormone and thyroid-stimulating hormone receptor structure-function relationships,” Physiological Reviews, vol. 82, no. 2, pp. 473–502, 2002. View at Google Scholar · View at Scopus
  43. C. N. Peroni, C. R. J. Soares, E. Gimbo, L. Morganti, M. T. C. P. Ribela, and P. Bartolini, “High-level expression of human thyroid-stimulating hormone in Chinese hamster ovary cells by co-transfection of dicistronic expression vectors followed by a dual-marker amplification strategy,” Biotechnology and Applied Biochemistry, vol. 35, part 1, pp. 19–26, 2002. View at Publisher · View at Google Scholar · View at Scopus