Page 80 - ebook
P. 80

[A. Biochemistry/Molecular Biology] A-40




                     Expression of Recombinant human IGF-1 protein in


               transgenic Nicotiana benthamiana and Nicotiana tabacum


                                                     BY-2 cells





                                     Kwangkyun Park¹, Il-Chul Kim¹, Dong Ju Lee¹,²*

           ¹Biological Sciences, Chonnam National University, Gwangju 61186, Korea, ²Basic Science Institute, Chonnam

                                         National University, Gwangju 61186, Korea





        Human Insulin-like Growth Factor (IGF-1)’s functions of cell proliferation, cell survival, damaged tissue recovery, and

        glycemic response have been known as one of the most promising parts in treating growth disorders, diabetes, and
        neurodegenerative diseases. Molecular farming is to exploit plant hosts as a recombinant protein expression system

        for the sake of the production and utilization of medically valuable proteins. Nicotiana benthamiana and Nicotiana
        tabacum BY-2 cells were transformed with Ti plasmid containing a new promoter and the recombinant human IGF-

        1  (rhIGF-1)  gene.  The  expression  of  rhIGF-1  mRNA  was detected  by  RT-PCR  (approximately  500  bp)  in  N.
        benthamiana and N. tabacum BY-2 cell. The expressed amount of rhIGF-1 protein was quantified by Western Blot.

        The yield of rhIGF-1 was estimated at 0.096~0.11% of the total soluble proteins in transgenic N. benthamiana and
        0.034~0.19% in transgenic N. tabacum BY-2 cells. Furthermore, other biomolecular and environmental factors will
        be considered and examined to improve the amount of the expressed rhIGF-1, and its activity estimation will be

        conducted after the purification process.
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