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Production of Biological Active Single Chain Bovine LH and FSH

  • Min, K.S. (Graduate School of Bio. & Information Technology, Dept. of Animal Resource Science Hankyong National University) ;
  • Kang, M.H. (Dept. of Food and Nutrition, Hoseo University) ;
  • Yoon, J.T. (Dept. of Animal Resource Science, Hankyong National University) ;
  • Jin, H.J. (NARI, RDA) ;
  • Seong, H.H. (NARI, RDA) ;
  • Chang, Y.M. (NARI, RDA) ;
  • Chung, H.J. (NARI, RDA) ;
  • Oh, S.J. (NARI, RDA) ;
  • Yun, S.G. (NARI, RDA) ;
  • Chang, W.K. (NARI, RDA)
  • Received : 2002.09.02
  • Accepted : 2002.12.31
  • Published : 2003.04.01

Abstract

Luteinizing hormone as other glycoprotein hormones is characterized by a heterodimeric structure composed a common $\alpha$-subunit noncovalently linked to a specific $\beta$-subunit. The correct conformation of the heterodimer is important for efficient secretion, hormonal-specific post-translational modifications, receptor binding and signal transduction. To determine whether $\alpha$- and $\beta$- subunits can be synthesized as a single polypeptide chain (tethered-bLH and -bFSH) and also display biological activities, the tetheredbLH and -bFSH molecules were constructed and transfected into chinese hamster ovary (CHO-K1) cells. LH and FSH activities were assayed by using the human embryonic kidney (HEK) 293 cells expressing rat LH and FSH receptor genes. The tethered-bLH and - bFSH proteins were efficiently secreted and showed a similar activity to the dimeric bovine LH and FSH $\alpha$/$\beta$ wild type and native purified from bovine pituitary. The tethered-molecules can be permit development of potent new analogues that stimulate ovarian development. Taken together, a single-chain analog can also be constructed to include additional hormone-specific bioactive generating potentially efficacious compounds. These data indicate the potentiality of the single chain approach to further investigate structurefunction relationships of LH and FSH.

Keywords

References

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