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- Title
Structural and functional characterization of recombinant human growth hormone isolated from transgenic pig milk.
- Authors
Lee, So-Young; Han, Joo-Hee; Lee, Eun-Kyeong; Kim, Young Kyu; Hwang, Seo-Ah; Lee, Sung-Hyun; Kim, Maria; Cho, Gye Yoon; Hwang, Jae-Ha; Kim, Su-Jin; Yoo, Jae-Gyu; Cho, Seong-Keun; Lee, Kyung-Ju; Cho, Weon-Ki
- Abstract
This study aimed to establish and reproduce transgenic pigs expressing human growth hormone (hGH) in their milk. We also aimed to purify hGH from the milk, to characterize the purified protein, and to assess the potential of our model for mass production of therapeutic proteins using transgenic techniques. Using ~15.5 L transgenic pig milk, we obtained proteins with ≥ 99% purity after three pre-treatments and five column chromatography steps. To confirm the biosimilarity of our milk-derived purified recombinant hGH (CGH942) with commercially available somatropin (Genotropin), we performed spectroscopy, structural, and biological analyses. We observed no difference between the purified protein and Genotropin samples. Furthermore, rat models were used to assess growth promotion potential. Our results indicate that CGH942 promotes growth, by increasing bone development and body weight. Toxicity assessments revealed no abnormal findings after 4 weeks of continuous administration and 2 weeks of recovery. The no-observed-adverse-effect level for both males and females was determined to be 0.6 mg/kg/day. Thus, no toxicological differences were observed between commercially available somatropin and CGH942 obtained from transgenic pig milk. In conclusion, we describe a transgenic technique using pigs, providing a new platform to produce human therapeutic proteins.
- Subjects
HUMAN growth hormone; MILK proteins; SWINE; BONE growth; MILK; COLUMN chromatography; MILK microbiology
- Publication
PLoS ONE, 2020, Vol 15, Issue 7, p1
- ISSN
1932-6203
- Publication type
Article
- DOI
10.1371/journal.pone.0236788