کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2017882 | 1067821 | 2009 | 8 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Production and characterization of soluble human lysosomal enzyme α-iduronidase with high activity from culture media of transgenic tobacco BY-2 cells Production and characterization of soluble human lysosomal enzyme α-iduronidase with high activity from culture media of transgenic tobacco BY-2 cells](/preview/png/2017882.png)
Lysosomal storage diseases (LSDs), that collectively represent over 50 disorders, are amenable to enzyme replacement therapies. However, the current methods used to commercially produce recombinant lysosomal enzymes for this purpose, most commonly Chinese Hamster Ovary cells and human fibroblasts, are prohibitively costly. Plant bioreactors hold great promise for economic production of functional human α-l-iduronidase (hIDUA; glycosaminoglycan α-l-iduronohydrolase; EC 3.2.1.76), the enzyme deficient in the human LSD, Mucopolysaccharidosis I. We have developed and tested an expression system using transgenic tobacco BY-2 cells to produce high amounts of active hIDUA. A plant signal peptide was essential for proper expression and secretion of the 78 kDa glycosylated hIDUA into the cultured media of transgenic BY-2 cells. The yield and activity of the secreted hIDUA from long-term cultures of transgenic BY-2 cell lines were as high as 10 μg/mL media and 53,000 pmol/min/mg proteins, respectively. Thus, this transgenic BY-2 cell line presents an attractive platform for economic production and easy downstream purification of hIDUA for enzyme replacement therapy. Furthermore, this system can be used for the production and purification of other human lysosomal enzymes or pharmaceuticals.
Journal: Plant Science - Volume 177, Issue 6, December 2009, Pages 668–675