The pilot-scale preparation of the SA-hGM-CSF bi-functional fusion protein

References

• Brem H, Howell R, Criscitelli T, et al. Practical application of granulocyte-macrophage colony-stimulating factor (GM-CSF) in patients with wounds. Surg Technol Int. 2018;32:61–66.
   Google Scholar
• Walter MR, Cook WJ, Ealick SE, Nagabhushan TL, Trotta PP, Bugg CE (1992) Three-dimensional structure of recombinant human granulocyte-macrophage colony-stimulating factor. Journal of Molecular Biology 224 (4):1075–1085
   Google Scholar
• Yan WL, Shen KY, Tien CY, Chen YA, Liu SJ (2017) Recent progress in GM-CSF-based cancer immunotherapy. Immunotherapy 9 (4):347–360.
   Google Scholar
• Van Overmeire E, Stijlemans B, Heymann F, Keirsse J, Morias Y, Elkrim Y, Brys L, Abels C, Lahmar Q, Ergen C, Vereecke L, Tacke F, De Baetselier P, Van Ginderachter JA, Laoui D (2016) M-CSF and GM-CSF receptor signaling differentially regulate monocyte maturation and macrophage polarization in the tumor microenvironment. Cancer Research 76 (1):35–42.
   Google Scholar
• Hamilton JA (2008) Colony-stimulating factors in inflammation and autoimmunity. Nature Reviews Immunology 8 (7):533–544.
   Google Scholar
• Metcalf D (2010) The colony-stimulating factors and cancer. Nature Reviews Cancer 10 (6):425–434.
   Google Scholar
• Kaufman HL, Ruby CE, Hughes T, Slingluff CL, Jr. (2014) Current status of granulocyte-macrophage colony-stimulating factor in the immunotherapy of melanoma. Journal for Immunotherapy of Cancer 2:11. doi:https://doi.org/10.1186/2051-1426-2-11.
   Google Scholar
• Finocchiaro LME, Agnetti L, Fondello C, Glikin GC (2019) Combination of cytokine-enhanced vaccine and chemo-gene therapy as surgery adjuvant treatments for spontaneous canine melanoma. Gene Therapy. doi:https://doi.org/10.1038/s41434-019-0066-7.
   Google Scholar
• Noda S, Matsumoto T, Tanaka T, Kondo A (2015) Secretory production of tetrameric native full-length streptavidin with thermostability using Streptomyces lividans as a host. Microbial Cell Factories 14:5.
   Google Scholar
• Ikonomova SP, Le MT, Kalla N, Karlsson AJ (2018) Effect of linkers on immobilization of scFvs with biotin-streptavidin interaction. Biotechnology and Applied Biochemistry 65 (4):580–585.
   Google Scholar
• Hu Z, Tan W, Zhang L, Liang Z, Xu C, Su H, Lu J, Gao J (2010) A novel immunotherapy for superficial bladder cancer by intravesical immobilization of GM-CSF. Journal of Cellular and Molecular Medicine 14 (6B):1836–1844.
   Google Scholar
• Yin W, He Q, Hu Z, Chen Z, Qifeng M, Zhichun S, Zhihui Q, Xiaoxia N, Li J, Gao J (2010) A novel therapeutic vaccine of GM-CSF/TNFalpha surface-modified RM-1 cells against the orthotopic prostatic cancer. Vaccine 28 (31):4937–4944.
   Google Scholar
• Vermasvuori R, Koskinen J, Salonen K, Siren N, Weegar J, Dahlbacka J, Kalkkinen N, von Weymarn N (2009) Production of recombinant HIV-1 nef protein using different expression host systems: a techno-economical comparison. Biotechnology Progress 25 (1):95–102.
   Google Scholar
• Thomson CA, Olson M, Jackson LM, Schrader JW (2012) A simplified method for the efficient refolding and purification of recombinant human GM-CSF. PloS One 7 (11):e49891.
   Google Scholar
• Singh SM, Panda AK (2005) Solubilization and refolding of bacterial inclusion body proteins. Journal of Bioscience and Bioengineering 99 (4):303–310.
   Google Scholar
• Lilie H, Schwarz E, Rudolph R (1998) Advances in refolding of proteins produced in E. Coli. Current Opinion in Biotechnology 9 (5):497–501
   Google Scholar
• Son YJ, Bae JY, Chong SH, Lee HS, Mo SH, Kim TY, Choe H (2010) Expression, high cell density culture and purification of recombinant EC-SOD in Escherichia coli. Applied Biochemistry and Biotechnology 162 (6):1585–1598.
   Google Scholar
• Arakawa T, Ejima D, Tsumoto K, Obeyama N, Tanaka Y, Kita Y, Timasheff SN (2007) Suppression of protein interactions by arginine: a proposed mechanism of the arginine effects. Biophysical Chemistry 127 (1–2):1–8.
   Google Scholar
• Chang LS, Lin SR, Chang CC (1998) Unfolding/folding studies on cobrotoxin from Taiwan cobra venom: pH and GSH/GSSG govern disulfide isomerization at the C-terminus. Archives of Biochemistry and Biophysics 354 (1):1–8.
   Google Scholar
• Hwang C, Sinskey AJ, Lodish HF (1992) Oxidized redox state of glutathione in the endoplasmic reticulum. Science (New York, NY) 257 (5076):1496–1502
   Google Scholar
• Tsumoto K, Ejima D, Kumagai I, Arakawa T (2003) Practical considerations in refolding proteins from inclusion bodies. Protein Expression and Purification 28 (1):1–8
   Google Scholar
• Feng Y, Zhang M, Zhang L, Zhang T, Ding J, Zhuang Y, Wang X, Yang Z (2012) An automatic refolding apparatus for preparative-scale protein production. PloS One 7 (9):e45891.
   Google Scholar
• Hollien J, Marqusee S (2002) Comparison of the folding processes of T. thermophilus and E. coli ribonucleases H. Journal of Molecular Biology 316 (2):327–340.
   Google Scholar
• Li M, Su ZG, Janson JC (2004) In vitro protein refolding by chromatographic procedures. Protein Expression and Purification 33 (1):1–10.
   Google Scholar
• Pace CN, Creighton TE (1986) The disulphide folding pathway of ribonuclease T1. Journal of Molecular Biology 188 (3):477–486
   Google Scholar
• Wicks IP, Roberts AW (2016) Targeting GM-CSF in inflammatory diseases. Nature Reviews Rheumatology 12 (1):37–48.
   Google Scholar
• Hamilton JA (2015) GM-CSF as a target in inflammatory/autoimmune disease: current evidence and future therapeutic potential. Expert Review of Clinical Immunology 11 (4):457–465.
   Google Scholar
• Truong MD, Choi BH, Kim YJ, Kim MS, Min BH (2017) Granulocyte macrophage - colony stimulating factor (GM-CSF) significantly enhances articular cartilage repair potential by microfracture. Osteoarthritis and Cartilage 25 (8):1345–1352.
   Google Scholar