Volume 9, Issue 1 (2018)                   JMBS 2018, 9(1): 79-92 | Back to browse issues page

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Ghasemi R, Hashemzadeh ‎ H, Razavi ‎ H, Yakhchali B. Production of Recombinant Human Growth Hormone and Future ‎Challenges. JMBS 2018; 9 (1) :79-92
URL: http://biot.modares.ac.ir/article-22-14265-en.html
1- Department Nanobiotechnology, Bioscience Faculty, Tarbiat Modares University, Tehran, Iran
2- ‎Nanobiotechnology Recearch Centre, Baqiyatallah University of Medical Sciences, Tehran, Iran
3- Department of Industrial and Environmental Biotechnology, National Institute of Genetic Engineering and ‎Biotechnology (NIGEB), Tehran, Iran, National Institute of Genetics & Biotechnology, Pajouhesh Boulevard, Town of Science & Technology Research, 15 ‎Kilometer, Highway Tehran- Karaj, Tehran, Iran. Postal Code: 1497716316‎ , bahar@nigeb.ac.ir
Abstract:   (6422 Views)
Introduction: Growth hormone is a non-glycosylated polypeptide strand of the pituitary glands of all vertebrates that has a wide range of biological activities and considering the importance of this hormone and its importance and diverse therapeutic applications in medicine, its recombinant production can be of great importance. In recent decades, protein engineering and genetic engineering have resulted in a high level of expression and production of this protein in a variety of hosts, including Escherichia coli bacteria using new techniques and methodes, hormone purification and assay are carried out easily. Therefore, the aim of this review was to investigate the production of recombinant human growth hormone (rhGH) and future challenges.
Conclusion: One of the problems of the expression and purification of the human growth hormone may involve that maybe noted the production of inclusion bodies in the expression of recombinant proteins in the cell cytoplasm, the contamination caused by host proteins, low protein recovery from these inclusion bodies, low protein secretion into the Periplasmic space, high cost of production, especially in Purification stage and so on. Due to the lack of need for glycosylated hormone and high efficiency and simplicity of work, bacterial systems, especially Escherichia coli, are the most economical and effective systems for the expression of heterologous proteins. The hormone purification stage is usually the most costly process. Therefore, an optimal design for achieving the highest target protein recovery with the elimination of all contamination from the final product and reducing the purification step is required.
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Article Type: Review | Subject: Agricultural Biotechnology
Received: 2016/04/25 | Accepted: 2017/10/27 | Published: 2018/05/22

References
1. Nielsen J, Villasen J, Liden, G. Bioreaction
engineering
principles. New York: Kluwer Academic/Plenum ‎Publishers; 2003.‎ [Link]
2. Zhan X, Giorgianni F, Desiderio DM. Proteomics analysis of growth hormone isoforms in the human ‎pituitary. Proteomics. 2005;5(5):1228-41.‎ [Link]
3. Baumann GP. Growth hormone isoforms. Growth Horm IGF Res. 2009;19(4):333-40.‎ [Link]
4. Shin NK, Kim DY, Shin CS, Hong MS, Lee J, Shin HC. High-level production of human growth hormone in ‎Escherichia Coli by a simple recombinant process. J Biotechnol. 1998;62(2):143-51.‎ [Link]
5. Sereikaite J, Statkute A, Morkunas M, Radzevicius K, Borromeo V, Secchi C, et al. Production of ‎recombinant mink growth hormone in E. Coli. Appl Microbiol Biotechnol. 2007;74(2):316-23.‎ [Link]
6. Saboury AA, Kordbacheh M, Sanati MH, Mizani F, Shamsipur M, Yakhchali MB, et al. Thermodynamics of ‎binding copper (II) ion by human growth hormone. Asian J Chem. 2005;17:2773-82.‎ [Link]
7. Inankur B. Recombinat human growth hormone production by Pichia pastoris and determination of its ‎interaction with peptide ligands [Dissertation]. Ankara: Middle East Technical University; 2010.‎ [Link]
8. Li CH, Evans HM. The isolation of pituitary growth hormone. Science. 1944;99(2566):183-4.‎ [Link]
9. Kopchick JJ. History and future of growth hormone research. Horm Res. 2003;60(Suppl 3):103-12.‎ [Link]
10. Koch TK, Berg BO, De Armond SJ, Gravina RF. Creutzfeldt-Jakob disease in a young adult with idiopathic ‎hypopituitarism: Possible relation to the administration of cadaveric human growth hormone. N Engl J Med. ‎‎1985;313(12):731-33.‎ [Link]
11. Brown P, Preece M, Brandel JP, Sato T, McShane L, Zerr I, et al. Iatrogenic Creutzfeldt-Jakob disease at ‎the millennium. Neurology. 2000;55(8):1075-81.‎ [Link]
12. Gray GL, Baldridge JS, McKeown KS, Heyneker HL, Chang CN. Periplasmic production of correctly ‎processed human growth hormone in Escherichia Coli: Natural and bacterial signal sequences are ‎interchangeable. Gene. 1985;39(2-3):247-54.‎ [Link]
13. Ghorpade A, Garg LC. Efficient processing and export of human growth hormone by heat labile ‎enterotoxin chain B signal sequence. FEBS Lett. 1993;330(1):61-5.‎ [Link]
14. Martial JA, Hallewell RA, Baxter JD, Goodman HM. Human growth hormone: Complementary DNA cloning ‎and expression in bacteria. Science. 1979;205(4406):602-7.‎ [Link]
15. Goeddel DV, Heyneker HL, Hozumi T, Arentzen R, Itakura K, Yansura DG, et al. Direct expression in ‎Escherichia Coli of a DNA sequence coding for human growth hormone. Nature. 1979;281(5732):544-8.‎ [Link]
16. Tritos NA, Mantzoros CS. Recombinant human growth hormone: Old and novel uses. Am J Med. ‎‎1998;105(1):44-57.‎ [Link]
17. Jorgensen KD. Comparison of the pharmacological properties of pituitary and biosynthetic human ‎growth-hormone-demonstration of antinatriuretic antidiuretic and barbital sleep effects of human growth-‎hormone in rats. Acta Endocrinol (Copenh). 1987;114(1):124-31.‎ [Link]
18. Fong Y, Rosenbaum M, Tracey KJ, Raman G, Hesse DG, Matthews DE, et al. Recombinant growth hormone ‎enhances muscle myosin heavy-chain mRNA accumulation and amino acid accrual in humans. Proc Natl Acad ‎Sci U S A. 1989;86(9):3371-4. ‎ [Link]
19. Ecamilla-Trevino LL, Viader-Salvadó JM, Barrera-Salda-a HA, Guerrero-Olazarán M. Biosynthesis and ‎secretion of recombinant human growth hormone in Pichia pastoris. Biotechnol Lett. 2000;22(2):109-14.‎ [Link]
20. Roehr B. The many faces of human growth hormone. BETA. 2003;15(4):12-6.‎ [Link]
21. Krysiak R, Gdula-Dymek A, Bednarska-Czerwińska A, Okopień B. Growth hormone therapy in children ‎and adults. Pharmacol Rep. 2007;59(5):500-16.‎ [Link]
22. Nakayama A, Ando K, Kawamura K, Mita I, Fukazawa K, Hori M, et al. Efficient secretion of the authentic ‎mature human growth hormone by Bacillus subtilis. J Biotechnol. 1988;8(2):123-34.‎ [Link]
23. Franchi E, Maisano F, Testori SA, Galli G, Toma S, Parente L, et al. A new human growth hormone ‎production process using a recombinant Bacillus subtilis strain. J Biotechnol. 1991;18(1-2):41-54.‎ [Link]
24. Ozdamar TH, Sentürk B, Yilmaz OD, Calik G, Celik E, Calik P. Expression system for recombinant human ‎growth hormone production from Bacillus subtilis. Biotechnol Prog. 2009;25(1):75-84.‎ [Link]
25. Tokunaga T, Iwai S, Gomi H, Kodama K, Ohtsuka E, Ikehara M, et al. Expression of a synthetic human ‎growth hormone gene in yeast. Gene. 1985;39(1):117-20.‎ [Link]
26. Eurwilaichitr L, Roytrakul S, Suprasongsin C, Manitchotpisit P, Panyim S. Glutamic acid and alanine ‎spacer is not necessary for removal of MFα-1 signal sequence fused to the human growth hormone produced ‎from Pichia pastoris. World J Microbiol Biotechnol. 2002;18(6):493-8.‎ [Link]
27. Ascacio-Martínez JA, Barrera-Salda-a HA. Production and secretion of biologically active recombinant ‎canine growth hormone by Pichia pastoris. Gene. 2004;340(2):261-6.‎ [Link]
28. Calik P, Orman MA, Celik E, Halloran SM, Calik G, Ozdamar TH. Expression system for biosynthesis and ‎purification of recombinant human growth in Pichia pastoris and structural analysis by MALDI-ToF mass ‎spectrometry. Biotechnol Prog. 2008;24(1):221-6. ‎ [Link]
29. Apte-Deshpande A, Rewanwar S, Kotwal P, Raiker VA, Padmanabhan S. Efficient expression and ‎secretion of recombinant human growth hormone in the methylotrophic yeast Pichia pastoris: Potential ‎applications for other proteins. Biotechnol Appl Biochem. 2009;54(4):197-205.‎ [Link]
30. Gray GL, McKeown KA, Jones AJ, Seeburg PH, Heyneker HL. Pseudomonas aeruginosa secretes and ‎correctly processes human growth hormone. Bio Technol. 1984;2:161-5.‎ [Link]
31. Catzel D, Lalevski H, Marquis CP, Gray PP, Van Dyk D, Mahler SM. Purification of recombinant human ‎growth hormone from CHO cell culture supernatant by Gradiflow preparative electrophoresis ‎technology. Protein Expr Purif. 2003;32(1):126-34.‎ [Link] [DOI:10.1016/j.pep.2003.07.002]
32. Geng ZH, Liu Y, Gao P, Zhao DM, Li S, Yu XD, et al. Enhancing hGH expression level in insect cells by ‎shortening the 5'-UTR of hGH cDNA. Sheng Wu Gong Cheng Xue Bao. 2002;18(4):505-8. [Chinese]‎ [Link]
33. Jayapal KP, Wlaschin KF, Hu W, Yap MGS. Recombinant protein therapeutics from CHO cells-20 years ‎and counting. Chem Eng Prog. 2007;103(10):40-7.‎ [Link]
34. Wurm FM. Production of recombinant protein therapeutics in cultivated mammalian cells. Nat Biotechnol. ‎‎2004;22(11):1393-8.‎ [Link] [DOI:10.1038/nbt1026]
35. Chang CN, Key M, Bochner B, Heyneker H, Gray G. High-level secretion of human growth hormone by ‎Escherichia Coli. Gene. 1987;55(2-3):189-96.‎ [Link] [DOI:10.1016/0378-1119(87)90279-4]
36. Kato C, Kobayashi T, Kudo T, Furusato T, Murakami Y, Tanaka T, et al. Construction of an excretion ‎vector and extracellular production of human growth hormone from Escherichia Coli. Gene. 1987;54(2-‎‎3):197-202.‎ [Link]
37. Becker GW, Hsiung HM. Expression, secretion and folding of human growth hormone in Escherichia Coli: ‎Purification and characterization. FEBS Lett. 1986;204(1):145-50. ‎ [Link] [DOI:10.1016/0014-5793(86)81403-X]
38. Hsiung HM, Cantrell A, Luirink J, Oudega B, Veros AJ, Becker GW. Use of bacteriocin release protein in E. ‎Coli for excretion of human growth hormone into the culture medium. Bio Technol. 1989;7:267-71.‎ [Link]
39. Patra AK, Mukhopadhyay R, Mukhija R, Krishnan A, Garg LC, Panda AK. Optimization of inclusion body ‎solubilization and renaturation of recombinant human growth hormone from Escherichia Coli. Protein Expres ‎Purif. 2000;18(2):182-92.‎ [Link]
40. Khodabandeh M, Yakhchali B, Rahimi M, Vaseli N, Moghaddasi Jahromi Z, Zomorrodipour A, et al. ‎Purification of large quantities of biologically active recombinant human growth hormone. Iran J Biotechnol. ‎‎2003;1(4):207-12.‎ [Link]
41. Soares CRJ, Gomide FIC, Ueda EKM, Bartolini P. Periplasmic expression of human growth hormone via ‎plasmid vectors containing the λPL promoter: Use of HPLC for product quantification. Protein Eng. ‎‎2003;16(12):1131-8.‎ [Link] [DOI:10.1093/protein/gzg114]
42. Ghasemi F, Zomorodipour A, Shojai S, Ataei F, Khodabandeh M, Sanati MH. Using L-arabinose for ‎production of human growth hormone in Escherichia Coli, studying the processing of gIII: hGH precursor. ‎Iran J Biotechnol. 2004;2(4):250-60.‎ [Link]
43. Zomorrodipour A, Yakhchali B, Khodabandeh M, Deezagi A, Hosseini Mazinani SM, Valian Borujeni S, et ‎al. The over-expression of biologically active human growth hormone in a T5-based system in Escherichia ‎Coli, studying temperature effect. J Sci Islam Repub Iran. 2004;15(1):27-32.‎ [Link]
44. Tabandeh F, Shojaosadati SA, Zomorodipour A, Khodabandeh M, Sanati MH, Yakhchali B. Heat-induced ‎production of human growth hormone by high cell density cultivation of recombinant Escherichia Coli. ‎Biotechnol Lett. 2004;26(3):245-50.‎ [Link] [DOI:10.1023/B:BILE.0000013714.88796.5f]
45. Tabandeh F, Yakhchali B, Shojaosadati SA, Khodabandeh M, Sanati MH. Growth kinetics and human ‎growth hormone production of a heat-inducible recombinant Echerichia Coli during batch fermentation. Iran ‎J Sci Technol Trans A. 2004;28(A1):11-7.‎ [Link]
46. Tabandeh F, Shojaosadati SA, Yakhchali B, Khodabandeh M, Sanati MH. Evaluation of heat induction ‎strategy for recombinant human growth hormone expression in fed-batch fermentation. Iran J ‎Biotechnol. 2005;3(1):24-30.‎ [Link]
47. Singh SM, Sharma A, Panda AK. High throughput purification of recombinant human growth hormone ‎using radial flow chromatography. Protein Expres Purif. 2009;68(1):54-9.‎ [Link] [DOI:10.1016/j.pep.2009.05.014]
48. Soorapaneni S, Apte-Deshpande A, Sabnis-Prasad K, Kumar J, Raiker VA, Kotwal P, et al. Arabinose ‎promoter based expression of biologically active recombinant human growth hormone in E. Coli: Strategies ‎for over expression and simple purification methods. J Microb Biochem Technol. 2010;2(2):38-45.‎ [Link]
49. Rezaei M, Zarkesh-Esfahani SH. Optimization of production of recombinant human growth hormone in ‎Escherichia Coli. J Res Med Sci. 2012;17(7):681-5.‎ [Link]
50. Kim MJ, Park HS, Seo KH, Yang HJ, Kim SK, Choi JH. Complete solubilization and purification of ‎recombinant human growth hormone produced in Escherichia Coli. PloS One. 2013;8(2):e56168. ‎ [Link] [DOI:10.1371/journal.pone.0056168]
51. Sockolosky JT, Szoka FC. Periplasmic production via the pET expression system of soluble, bioactive ‎human growth hormone. Protein Expres Purif. 2013;87(2):129-35.‎ [Link] [DOI:10.1016/j.pep.2012.11.002]
52. Ahangari G, Ostadali MR, Rabani A, Rashidian J, Sanati MH, Zarindast MR. Growth hormone antibodies ‎formation in patients treated with recombinant human growth hormone. Int J Immunopathol Pharmacol. ‎‎2004;17(1):33-8.‎ [Link] [DOI:10.1177/039463200401700105]
53. Hsiung HM, Mayne NG, Becker GW. High–level expression, efficient secretion and folding of human ‎growth hormone in Escherichia Coli. Bio Technol. 1986;4:991-5.‎ [Link] [DOI:10.1038/nbt1186-991]
54. Nakayama A, Kawamura K, Shimada H, Akaoka A, Mita I, Honjo M, et al. Extracellular production of ‎human growth hormone by a head portion of the prepropeptide derived from Bacillus amyloliquefaciens ‎neutral protease in Bacillus subtilis. J Biotechnol. 1987;5(3):171-9.‎ [Link]
55. 55- Kiany J, Zomorodipour A, Ahmadzadeh Raji M, Sanati MH. Construction of recombinant plasmids for periplasmic expression of human growth hormone in Escherichia Coli under T7 and lac promoters. J Sci Islam Repub Iran. 2003;14(4):311-6. [Link]
56. Kohara A, Yamamoto Y, Kikuchi M. Processing and secretion of human growth hormone with an artificial signal sequence. Biosci Biotechnol Biochem. 1994;58(4):779-81. [Link] [DOI:10.1271/bbb.58.779]
57. Vassileva-Atanassova A, Mironova R, Nacheva G, Ivanov I. N-terminal methionine in recombinant proteins expressed in two different Escherichia Coli strains. J Biotechnol. 1999;69(1):63-7. [Link] [DOI:10.1016/S0168-1656(98)00207-7]
58. Makrides SC. Strategies for achieving high-level expression of genes in Escherichia Coli. Microbiol Rev. 1996;60(3):512-38. [Link]
59. Wilkinson DL, Harrison RG. Predicting the solubility of recombinant proteins in Escherichia Coli. Biotechnology (N Y). 1991;9(5):443-8. [Link] [DOI:10.1038/nbt0591-443]
60. Thamann TJ. Raman spectroscopic studies of a dimeric form of recombinant bovine growth hormone. Anal Biochem. 1998;265(2):202-7. [Link] [DOI:10.1006/abio.1998.2879]
61. St John RJ, Carpenter JF, Balny C, Randolph TW. High pressure refolding of recombinant human growth hormone from insoluble aggregates, Structural transformations, kinetic barriers, and energetics. J Biol Chem. 2001;276:46856-63. [Link] [DOI:10.1074/jbc.M107671200]
62. Singh SM, Panda AK. Solubilization and refolding of bacterial inclusion body proteins. J Biosci Bioeng. 2005;99(4):303-10. [Link] [DOI:10.1263/jbb.99.303]
63. Sonoda H, Sugimura A. Improved solubilization of recombinant human growth hormone inclusion body produced in Escherichia Coli. Biosci Biotechnol Biochem. 2008;72(10):2675-80. [Link] [DOI:10.1271/bbb.80332]
64. Clark ED. Protein refolding for industrial processes. Curr Opin Biotechnol. 2001;12(2):202-7. [Link] [DOI:10.1016/S0958-1669(00)00200-7]

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