Abstract
Luteinizing hormone as other glycoprotein hormones is characterized by a heterodimeric structure composed a common α-subunit noncovalently linked to a specific β-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 α- and β- 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 α/β 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. (Asian-Aust. J. Anim. Sci. 2003. Vol 16, No. 4 : 498-503)
Highlights
Luteinizing hormone (LH) belongs to the glycoprotein hormone family, which includes follicle-stimulating hormone (FSH), thyroid-stimulating hormone (TSH) of the pituitary and chorionic gonadotropin (CG) of the placenta.This hormone family is characterized by a heterodimeric structure composed a common α-subunit noncovalently linked to a hormone specific β-subunit (Pierce and Parsons, 1981)
FSH administrated alone or in combination with semipurified human menopausal gonadotropins containing a mixture of FSH and LH has been used to stimulate the development of ovarian follicles for in vitro fertilization (Keene et al, 1989)
These results indicate that the tetheredmolecules were secreted efficiently, and that is similar to wild type glycoprotein hormones in the LH-and FSH-like activities
Summary
Luteinizing hormone (LH) belongs to the glycoprotein hormone family, which includes follicle-stimulating hormone (FSH), thyroid-stimulating hormone (TSH) of the pituitary and chorionic gonadotropin (CG) of the placenta. To determine bovine α-and β-subunits can be synthesized as a single polypeptide chain (tethered-bLH and FSH) and display biological activity, the tetheredmolecules by fusing the amino terminus of the α-subunit to the carboxyl terminus of the each β-subunit were constructed and transfected into chinese hamster ovary (CHO-K1) cells. These results indicate that the tetheredmolecules were secreted efficiently, and that is similar to wild type glycoprotein hormones in the LH-and FSH-like activities. The fragments were annealed and subjected to the second and Methods
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