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Production of Biological Active Single Chain Bovine LH and FSH |
K. S. Min, M. H. Kang, J. T. Yoon, H. J. Jin, H. H. Seong, Y. M. Chang, H. J. Chung, S. J. Oh, S. G. Yun, W. K. Chang |
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Abstract |
Luteinizing hormone as other glycoprotein hormones is characterized by a heterodimeric structure composed a common a-subunit noncovalently linked to a specific b-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 a- and b-subunits can be synthesized as a single polypeptide chain (tethered-bLH and -bFSH) and also display biological activities, the tethered-bLH 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 a/b 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 structure-function relationships of LH and FSH. |
Keywords:
Tethered-bLH and -FSH; Biological Activity |
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