High-yield production of functional human lactoferrin in transgenic cell cultures of Siberian ginseng(Acanthopanax senticosus)

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Title
High-yield production of functional human lactoferrin in transgenic cell cultures of Siberian ginseng(Acanthopanax senticosus)
Author(s)
S H Jo; Suk Yoon KwonDoo Sang Park; Kyoung Sil Yang; J W Kim; K T Lee; Sang Soo Kwak; Haeng Soon Lee
Bibliographic Citation
Biotechnology and Bioprocess Engineering, vol. 11, no. 5, pp. 442-448
Publication Year
2006
Abstract
Human lactoferrin (hLf) is an iron-binding glycoprotein that has been considered to play many biological roles in the human, including the stimulation of the immune system, antimicrobial and anti-inflammatory effects, and regulation of iron absorption. We generated transgenic Siberian ginseng (Acanthopanax senticosus) cell cultures producing a functional hLf protein using the signal peptide sequence from the endoplasmic reticulum and driven by an oxidative stress-inducible SWPA2 promoter which is highly expressed in plant cell cultures. The production of hLf increased proportionally to cell growth and showed a maximal level (up to 3.6% of total soluble protein) at the stationary phase in suspension cultures. Full-length hLf protein was identified by immunoblot analysis in transgenic cell cultures of Siberian ginseng. Recombinant hlf (rhLf) was purified from suspension cells of Siberian ginseng by ammonium sulfate precipitation, cation-exchange and gel filtration chromatography. N-terminal sequences of rhLf were identical to native hLf (nhLf). The overall monosaccharide composition of rhLf showed the presence of plant specific xylose while sialic acid is absent. Antibacterial activity of purified rhlf was higher than that of nhLf. Taken together, we anticipate that medicinal Siberian ginseng cultured cells, as demonstrated by this study, will be a biotechnologically useful source for commercial production of functional hLf not requiring further purification.
Keyword
High expression promoterHuman lactoferrinCell cultureMedicinal plantRecombinant protein
ISSN
1226-8372
Publisher
Springer
DOI
http://dx.doi.org/10.1007/BF02932312
Type
Article
Appears in Collections:
Jeonbuk Branch Institute > Biological Resource Center > 1. Journal Articles
Division of Research on National Challenges > Plant Systems Engineering Research > 1. Journal Articles
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