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1 December 2001 Equine Follicle-Stimulating Hormone: Molecular Cloning of β Subunit and Biological Role of the Asparagine-Linked Oligosaccharide at Asparagine56 of α Subunit
Takeo Saneyoshi, Kwan-Sik Min, Xiao Jing Ma, Yasuo Nambo, Takashi Hiyama, Satoshi Tanaka, Kunio Shiota
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Abstract

Equine FSH (eFSH) and eCG are members of the glycoprotein hormone family. These proteins are heterodimeric, composed of noncovalently associated α and β subunits. We have previously reported that recombinant eCG has potent LH- and FSH-like activities and that the oligosaccharide at Asn56 of the α subunit plays an indispensable role in expressing LH- but not FSH-like activity. In the present study, we cloned eFSH β subunit cDNA and expressed wild-type recombinant eFSH and a partially deglycosylated mutant FSH (eFSH α56/β) to investigate the biological role of the oligosaccharide at Asn56 in FSH activity. The wild-type eFSH and eCG stimulated estradiol production in a dose-dependent manner in the primary cultures of rat granulosa cells, indicating that these equine gonadotropins have FSH activity. Partially deglycosylated eCG (eCG α56/β) also stimulated estradiol production, confirming that the FSH-like activity of eCG is resistant to the removal of the N-linked oligosaccharide. Partially deglycosylated eFSH (eFSH α56/β), however, did not show any FSH activity, indicating that the oligosaccharide at Asn56 was necessary for eFSH. Thus, FSH-like activities of two gonadotropins, eCG and eFSH, are evoked through the distinct molecular mechanisms regarding the biological role of oligosaccharide at Asn56 of the α subunit.

Takeo Saneyoshi, Kwan-Sik Min, Xiao Jing Ma, Yasuo Nambo, Takashi Hiyama, Satoshi Tanaka, and Kunio Shiota "Equine Follicle-Stimulating Hormone: Molecular Cloning of β Subunit and Biological Role of the Asparagine-Linked Oligosaccharide at Asparagine56 of α Subunit," Biology of Reproduction 65(6), 1686-1690, (1 December 2001). https://doi.org/10.1095/biolreprod65.6.1686
Published: 1 December 2001
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