Recombinant Mouse Granulocyte–Macrophage Colony-Stimulating Factor Is Glycosylated in Transgenic Tobacco and Maintains its Biological Activity

Góra-Sochacka, Anna; Redkiewicz, Patrycja; Napiórkowska, Bogusława; Gaganidze, Dali; Brodzik, Robert; Sirko, Agnieszka

doi:10.1089/jir.2009.0053

Cited by 19 publications

(19 citation statements)

References 27 publications

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“…Because of different system than the one used in work discussed above (tobacco suspension cells and potato tubers), we cannot make reliable comparison of the efficiency. Previously, using exactly the same plant expression system, we reported about twofold higher accumulation of recombinant murine granulocyte–macrophage colony‐stimulating factor, mGM‐CSF (Gora‐Sochacka et al. , 2010), than the accumulation of hIL‐2 reported in this study.…”

Section: Discussionsupporting

confidence: 59%

Transgenic tobacco plants as production platform for biologically active human interleukin 2 and its fusion with proteinase inhibitors

Redkiewicz¹,

Więsyk²,

Góra-Sochacka³

et al. 2012

Plant Biotechnology Journal

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SummaryTransgenic plants offer a low-cost approach for the production of pharmaceutically important and commercially valuable recombinant proteins. Our studies were focused on the plantbased production of human interleukin 2 (hIL-2) and its fusion with proteinase inhibitors, either SPI2 from Galleria mellonella or CMTI from Cucurbita maxima. Finally, five plant expression cassettes were obtained. Three of them contained the single cDNA encoding CMTI I, SPI2 and hIL-2, respectively, while two of them contained the translational fusion, SPI2::hIL-2 and CMTI::hIL-2. In all cases, the transgenes were controlled by the RbcS1 promoter and terminator and the recombinant proteins were targeted to the endoplasmic reticulum. After tobacco transformation, five groups of transgenic plants were obtained and analysed. The level of recombinant proteins was estimated either by Western blot or by ELISA. The biological activity of plant-produced hIL-2 alone or in a fusion with SPI2 or CMTI was confirmed using the mammalian cells proliferation assay. The activities of proteinase inhibitors were confirmed in proteolysis assay using azocoll as a substrate. The usefulness of using proteinase inhibitor CMTI I in a fusion with hIL-2 as a protective agent against trypsin digestion was demonstrated.

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Section: Discussionsupporting

confidence: 59%

Transgenic tobacco plants as production platform for biologically active human interleukin 2 and its fusion with proteinase inhibitors

Redkiewicz¹,

Więsyk²,

Góra-Sochacka³

et al. 2012

Plant Biotechnology Journal

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“…In our lab, we have isolated the duck FST fusion protein and confirmed it by the MALDI-TOF method. To further investigate the recombinant protein activities, the protein was purified and refolded and the purified protein was added to the medium of myoblasts cultured in vitro (Gora-Sochacka et al 2010). The results show that the fusion protein isolated and purified exhibited biology activities that could increase myoblast proliferation.…”

Section: Discussionmentioning

confidence: 99%

Injection of duck recombinant follistatin fusion protein into duck muscle tissues stimulates satellite cell proliferation and muscle fiber hypertrophy

Liu

Wang

et al. 2012

Appl Microbiol Biotechnol

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Follistatin (FST) can inhibit the expression of myostatin, which is a predominant inhibitor of muscle development. The potential application of myostatin-based technology has been prompted in different ways in agriculture. We previously constructed an expression vector of duck FST and isolated the FST fusion protein. After the protein was purified and refolded, it was added to the medium of duck myoblasts cultured in vitro. The results show that the 3-(4,5-dimethylthiazol-2-yl)-2, 5-diphenyltetrazolium bromide value of the myoblasts in the duck FST treatment group is higher than that in the control group, which indicates that the duck FST fusion protein exhibits the biological activities that can accelerate myoblast proliferation. To further investigate the roles of duck FST on muscle development, we injected the protein into the duck muscle tissues in vivo. The results show that both the duck muscle fiber cross-sectional area and the satellite cell activation frequency are influenced more in the FST treatment group than they are in the control group. In addition to these phenomena, expression of MyoD and Myf5 were increased, and the expression of myostatin was decreased. Together, these results suggest the potential for using duck FST fusion protein to inhibit myostatin activity and subsequently to enhance muscle growth in vivo. The mechanism by which FST regulates muscle development in the duck is similar to that in mammals and fishes.

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“…Mouse GM-CSF (mGM-CSF) was successfully produced using rice suspension cells, with yield of 24.6 mg/L of medium [25]. The same glycoprotein was also produced in tobacco leaves, and the yield was 19 μg/g of fresh leaves [37]. The biological activities of recombinant human and mouse GM-CSF produced in rice suspension culture has also been confirmed using GM-CSF dependent TF1 cells and murine myeloblastic leukemia NFS-60 cells, respectively [8,25].…”

Section: Recombinant Pharmaceuticals In Ricementioning

confidence: 99%

Improving Pharmaceutical Protein Production in Oryza sativa

Kuo

Tan

et al. 2013

IJMS

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Application of plant expression systems in the production of recombinant proteins has several advantages, such as low maintenance cost, absence of human pathogens, and possession of complex post-translational glycosylation capabilities. Plants have been successfully used to produce recombinant cytokines, vaccines, antibodies, and other proteins, and rice (Oryza sativa) is a potential plant used as recombinant protein expression system. After successful transformation, transgenic rice cells can be either regenerated into whole plants or grown as cell cultures that can be upscaled into bioreactors. This review summarizes recent advances in the production of different recombinant protein produced in rice and describes their production methods as well as methods to improve protein yield and quality. Glycosylation and its impact in plant development and protein production are discussed, and several methods of improving yield and quality that have not been incorporated in rice expression systems are also proposed. Finally, different bioreactor options are explored and their advantages are analyzed.

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Recombinant Mouse Granulocyte–Macrophage Colony-Stimulating Factor Is Glycosylated in Transgenic Tobacco and Maintains its Biological Activity

Cited by 19 publications

References 27 publications

Transgenic tobacco plants as production platform for biologically active human interleukin 2 and its fusion with proteinase inhibitors

Transgenic tobacco plants as production platform for biologically active human interleukin 2 and its fusion with proteinase inhibitors

Injection of duck recombinant follistatin fusion protein into duck muscle tissues stimulates satellite cell proliferation and muscle fiber hypertrophy

Improving Pharmaceutical Protein Production in Oryza sativa

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