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 Asn16 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 Asn16 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 αsubunit.
| Original language | English |
|---|---|
| Pages (from-to) | 1686-1690 |
| Number of pages | 5 |
| Journal | Biology of Reproduction |
| Volume | 65 |
| Issue number | 6 |
| Publication status | Published - 2001 |
| Externally published | Yes |
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Keywords
- FSH
- Hormone action
ASJC Scopus subject areas
- Cell Biology
- Developmental Biology
- Embryology
Cite this
Equine follicle-stimulating hormone : Molecular cloning of β subunit and biological role of the asparagine-linked oligosaccharide at asparagine56 of α subunit. / Saneyoshi, T.; Min, K. S.; Ma, X. J.; Nambo, Y.; Hiyama, T.; Tanaka, S.; Shiota, K.
In: Biology of Reproduction, Vol. 65, No. 6, 2001, p. 1686-1690.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Equine follicle-stimulating hormone
T2 - Molecular cloning of β subunit and biological role of the asparagine-linked oligosaccharide at asparagine56 of α subunit
AU - Saneyoshi, T.
AU - Min, K. S.
AU - Ma, X. J.
AU - Nambo, Y.
AU - Hiyama, T.
AU - Tanaka, S.
AU - Shiota, K.
PY - 2001
Y1 - 2001
N2 - 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 Asn16 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 Asn16 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 αsubunit.
AB - 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 Asn16 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 Asn16 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 αsubunit.
KW - FSH
KW - Hormone action
UR - http://www.scopus.com/inward/record.url?scp=0035179025&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035179025&partnerID=8YFLogxK
M3 - Article
C2 - 11717129
AN - SCOPUS:0035179025
VL - 65
SP - 1686
EP - 1690
JO - Biology of Reproduction
JF - Biology of Reproduction
SN - 0006-3363
IS - 6
ER -